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- PDB-5kra: Crystal Structure of the ER-alpha Ligand-binding Domain (Y537S) i... -

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Basic information

Entry
Database: PDB / ID: 5kra
TitleCrystal Structure of the ER-alpha Ligand-binding Domain (Y537S) in Complex with DDT and DDE
Components
  • Estrogen receptor
  • NCOA2
KeywordsTRANSCRIPTION / Nuclear receptor / transcription factor / ligand binding / protein-ligand complex
Function / homology
Function and homology information


regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding / 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 ...regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding / 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 / locomotor rhythm / negative regulation of smooth muscle cell apoptotic process / mammary gland branching involved in pregnancy / uterus development / vagina development / aryl hydrocarbon receptor binding / TFIIB-class transcription factor binding / regulation of lipid metabolic process / androgen metabolic process / steroid hormone receptor signaling pathway / cellular response to Thyroglobulin triiodothyronine / regulation of glucose metabolic process / Synthesis of bile acids and bile salts / mammary gland alveolus development / estrogen receptor signaling pathway / cellular response to estrogen stimulus / Endogenous sterols / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / estrogen response element binding / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / : / 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 / regulation of cellular response to insulin stimulus / Recycling of bile acids and salts / cellular response to hormone stimulus / protein localization to chromatin / 14-3-3 protein binding / positive regulation of adipose tissue development / peroxisome proliferator activated receptor signaling pathway / RORA activates gene expression / TBP-class protein binding / nitric-oxide synthase regulator activity / Regulation of lipid metabolism by PPARalpha / steroid binding / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / ESR-mediated signaling / transcription corepressor binding / BMAL1:CLOCK,NPAS2 activates circadian gene expression / negative regulation of miRNA transcription / SUMOylation of transcription cofactors / Activation of gene expression by SREBF (SREBP) / nuclear receptor coactivator activity / positive regulation of nitric-oxide synthase activity / cellular response to estradiol stimulus / transcription coregulator binding / response to progesterone / stem cell differentiation / nuclear receptor binding / nuclear estrogen receptor binding / circadian regulation of gene expression / Heme signaling / SUMOylation of intracellular receptors / euchromatin / mRNA transcription by RNA polymerase II / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Transcriptional activation of mitochondrial biogenesis / negative regulation of DNA-binding transcription factor activity / PPARA activates gene expression / Cytoprotection by HMOX1 / beta-catenin binding / transcription coactivator binding / positive regulation of DNA-binding transcription factor activity / Transcriptional regulation of white adipocyte differentiation / Nuclear Receptor transcription pathway / response to estrogen / RNA polymerase II transcription regulator complex / 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 / Circadian Clock / PIP3 activates AKT signaling / response to estradiol / phospholipase C-activating G protein-coupled receptor signaling pathway / HATs acetylate histones / regulation of inflammatory response / positive regulation of cytosolic calcium ion concentration / fibroblast proliferation / ATPase binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
Similarity search - Function
Nuclear receptor coactivator 2 / Nuclear receptor coactivator 2/3, DUF4927 / Domain of unknown function (DUF4927) / 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 receptor coactivator, DUF1518 ...Nuclear receptor coactivator 2 / Nuclear receptor coactivator 2/3, DUF4927 / Domain of unknown function (DUF4927) / 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 receptor coactivator, DUF1518 / Nuclear receptor coactivator, Ncoa-type, interlocking / Nuclear receptor coactivator, Ncoa-type, interlocking domain superfamily / Nuclear receptor coactivator, DUF1518 / Nuclear receptor coactivator / DUF1518 / Nuclear receptor coactivator, receptor-binding domain / Nuclear receptor coactivator / Steroid receptor coactivator / Unstructured region on nuclear receptor coactivator protein / PAS domain / Nuclear receptor coactivator, interlocking / Helix-loop-helix DNA-binding domain superfamily / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain / Myc-type, basic helix-loop-helix (bHLH) domain profile. / PAS fold / PAS fold / PAS domain / PAS repeat profile. / PAS domain / PAS domain superfamily / Retinoid X Receptor / Retinoid X 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 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Chem-6WS / Chem-6WT / Estrogen receptor / Nuclear receptor coactivator 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.401 Å
AuthorsNwachukwu, J.C. / Srinivasan, S. / Bruno, N.E. / Nowak, J. / Kojetin, D.J. / Elemento, O. / Katzenellenbogen, J.A. / Nettles, K.W.
CitationJournal: Cell Chem Biol / Year: 2017
Title: Systems Structural Biology Analysis of Ligand Effects on ER alpha Predicts Cellular Response to Environmental Estrogens and Anti-hormone Therapies.
Authors: Nwachukwu, J.C. / Srinivasan, S. / Bruno, N.E. / Nowak, J. / Wright, N.J. / Minutolo, F. / Rangarajan, E.S. / Izard, T. / Yao, X.Q. / Grant, B.J. / Kojetin, D.J. / Elemento, O. / ...Authors: Nwachukwu, J.C. / Srinivasan, S. / Bruno, N.E. / Nowak, J. / Wright, N.J. / Minutolo, F. / Rangarajan, E.S. / Izard, T. / Yao, X.Q. / Grant, B.J. / Kojetin, D.J. / Elemento, O. / Katzenellenbogen, J.A. / Nettles, K.W.
History
DepositionJul 7, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 15, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_radiation_wavelength
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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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
C: NCOA2
D: NCOA2
E: Estrogen receptor
F: Estrogen receptor
G: NCOA2
H: NCOA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)125,21112
Polymers123,8668
Non-polymers1,3454
Water5,332296
1
A: Estrogen receptor
B: Estrogen receptor
C: NCOA2
D: NCOA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,6056
Polymers61,9334
Non-polymers6732
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5130 Å2
ΔGint-29 kcal/mol
Surface area19760 Å2
MethodPISA
2
E: Estrogen receptor
F: Estrogen receptor
G: NCOA2
H: NCOA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,6056
Polymers61,9334
Non-polymers6732
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5260 Å2
ΔGint-29 kcal/mol
Surface area19790 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.580, 82.960, 104.970
Angle α, β, γ (deg.)90.00, 101.12, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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


Mass: 29299.535 Da / Num. of mol.: 4 / Fragment: ligand-binding domain / Mutation: Y537S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESR1, ESR, NR3A1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P03372
#2: Protein/peptide
NCOA2


Mass: 1666.943 Da / Num. of mol.: 4 / Fragment: Nuclear receptor-interacting peptide / Source method: obtained synthetically / Details: This sequence occurs naturally in humans / Source: (synth.) Homo sapiens (human) / References: UniProt: Q15596*PLUS
#3: Chemical ChemComp-6WS / 1-[2,2-bis(chloranyl)-1-(4-chlorophenyl)ethenyl]-4-chloranyl-benzene


Mass: 318.025 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C14H8Cl4
#4: Chemical ChemComp-6WT / 1-chloranyl-4-[2,2,2-tris(chloranyl)-1-(4-chlorophenyl)ethyl]benzene


Mass: 354.486 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C14H9Cl5
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 296 / Source method: isolated from a natural source / Formula: H2O

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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: 39.3 % / Mosaicity: 0.638 °
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 8.3 / Details: 15% PEG 3350, 0.05M MgCl2, 0.067M NaCl, 0.1M Tris

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 14, 2011
RadiationMonochromator: Side scattering bent cube i-beam single crystal asymmetric cut 4.965 degs
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→50 Å / Num. obs: 37877 / % possible obs: 98 % / Redundancy: 3.4 % / Biso Wilson estimate: 26.49 Å2 / Rmerge(I) obs: 0.072 / Rpim(I) all: 0.046 / Rrim(I) all: 0.086 / Χ2: 0.54 / Net I/av σ(I): 12.79 / Net I/σ(I): 4.5 / Num. measured all: 128694
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsCC1/2Diffraction-ID% possible all
2.4-2.443.40.4780.972195.6
2.44-2.493.40.4420.869196.4
2.49-2.533.40.4230.859197.7
2.53-2.593.40.3580.923198.2
2.59-2.643.40.3030.959197.1
2.64-2.73.30.2770.958197.7
2.7-2.773.10.2450.956197.3
2.77-2.8530.2140.953194.5
2.85-2.933.50.1780.979199.5
2.93-3.023.60.1440.983199.5
3.02-3.133.60.1260.99199.8
3.13-3.263.50.1040.992199.5
3.26-3.413.50.080.996199.2
3.41-3.583.50.070.996198.1
3.58-3.813.40.0550.997197.4
3.81-4.13.10.0460.998196.6
4.1-4.523.50.0450.998198.4
4.52-5.173.60.0420.997199.9
5.17-6.513.40.0480.998199.6
6.51-503.30.0320.999197.2

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
HKL-2000data scaling
PDB_EXTRACT3.2data extraction
HKL-2000data reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.401→40.576 Å / SU ML: 0.27 / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 30.69 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2485 1718 5.24 %
Rwork0.2038 --
obs0.2062 32802 84.76 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.401→40.576 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7576 0 74 296 7946
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0057801
X-RAY DIFFRACTIONf_angle_d0.97510546
X-RAY DIFFRACTIONf_dihedral_angle_d17.4252878
X-RAY DIFFRACTIONf_chiral_restr0.1521257
X-RAY DIFFRACTIONf_plane_restr0.0031305
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4008-2.47140.2601480.2325940X-RAY DIFFRACTION31
2.4714-2.55120.2974970.23981905X-RAY DIFFRACTION62
2.5512-2.64230.29371360.2322473X-RAY DIFFRACTION82
2.6423-2.74810.29941500.23242654X-RAY DIFFRACTION87
2.7481-2.87310.28561470.23822645X-RAY DIFFRACTION87
2.8731-3.02460.25431550.23292823X-RAY DIFFRACTION93
3.0246-3.2140.27341620.23132910X-RAY DIFFRACTION95
3.214-3.4620.26631590.21642928X-RAY DIFFRACTION96
3.462-3.81020.2281600.18392890X-RAY DIFFRACTION95
3.8102-4.3610.24241630.16612910X-RAY DIFFRACTION95
4.361-5.49220.2021700.17373052X-RAY DIFFRACTION99
5.4922-40.58190.22531710.20282954X-RAY DIFFRACTION95
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)
14.5024-1.95712.01413.8996-0.89134.06410.06490.03610.1031-0.1079-0.1911-0.46310.10050.44730.16310.17880.01630.04190.203-0.00370.1818-1.2719-17.0414-13.9218
24.7542-0.9890.81734.59410.72223.28650.0473-0.0508-0.3024-0.2875-0.20050.17040.00210.07380.16660.10770.00860.01660.18420.06670.2193-7.1089-19.227-13.1909
34.9776-0.51630.87366.7247-2.10624.51190.186-0.3949-1.479-0.0051-0.04310.09581.19060.1999-0.10810.32460.02510.00650.23170.05940.7501-12.6005-33.8732-15.036
43.2175-0.19691.53692.2504-0.69696.18010.0193-0.12910.01360.1478-0.06250.073-0.0413-0.09210.00820.12210.00430.04050.14030.00740.2093-14.2715-16.7776-16.4751
53.81330.6428-0.78330.7518-1.12996.8020.03570.0926-0.156-0.00260.21940.30480.0986-0.3035-0.17250.29850.0823-0.05610.25380.02130.3528-44.4963-17.8416-17.1123
65.3177-0.7784-1.69674.73131.07874.41440.0102-0.346-0.52330.1216-0.08820.22590.1722-0.19610.0830.1341-0.0031-0.00930.22930.03850.2896-38.8587-21.6393-12.4046
76.69410.30815.80580.05290.2135.3204-0.0142-1.39090.70180.74540.2824-0.30080.17330.7008-0.29380.6354-0.0430.05440.9123-0.31030.5798-38.7468-8.67030.2786
83.5235-0.0897-0.73612.60010.91924.10960.0396-0.27580.32090.00790.1568-0.1197-0.27670.0824-0.18670.1730.01510.01270.2511-0.02830.3381-30.7202-14.8951-17.2269
93.9344-0.1236-0.25192.9852-0.76473.13780.02890.05-0.3332-0.0928-0.06980.0350.0307-0.07770.05040.10230.0326-0.00930.15410.02930.2229-27.4345-18.9665-21.0786
102.6114-1.9894-0.86995.99121.91567.91460.9152-0.8144-0.81990.39821.5118-0.4216-0.08251.0513-0.55030.58570.29930.13370.3711.07620.7289-35.9014-30.5017-1.1328
111.68151.3273.02243.61893.04575.47040.1146-0.47280.740.0434-0.4836-0.393-1.23060.6420.01010.47720.0744-0.23240.5256-0.39960.6035-2.1103-6.6613-0.9756
122.1504-3.9820.70167.4329-0.47819.44640.1442-0.0688-2.6311-0.2368-0.44830.32731.4021-1.76380.18230.4503-0.14230.09730.42830.12261.1317-43.0283-37.3189-13.7531
134.70360.98531.07494.67711.10274.3207-0.4619-0.31460.66050.22980.37180.252-1.7549-0.1335-0.09290.4186-0.02620.10210.5221-0.20210.3405-14.8782-47.2416-24.191
144.2712-0.5227-0.08667.66012.73476.13310.34610.3461-0.5597-0.89390.1973-0.25220.1173-0.3471-0.3330.2549-0.0105-0.04070.2452-0.02040.2326-22.4346-67.4561-41.0611
154.89011.80460.93464.8879-2.05793.53420.01420.03250.04120.20750.01190.3859-0.1775-0.1163-0.00080.13950.03570.01020.12660.00830.2216-13.8727-59.8766-40.7041
160.2322-0.49570.56913.186-0.97192.37720.00940.3577-0.6734-0.58740.1665-0.18420.79310.6532-0.30210.4363-0.0451-0.11540.2696-0.05931.0578-13.4751-78.6526-43.8484
175.3478-2.2-2.62167.553.97712.0469-0.1925-0.0383-1.29080.12230.05250.18020.60250.31050.10290.15250.0213-0.01710.18950.00630.6674-5.6328-73.2698-34.9235
185.11850.10381.81662.2746-0.44534.94140.1088-0.6120.50710.1972-0.02480.2331-0.64550.1060.09990.24920.01370.05570.2354-0.10440.2363-5.623-53.5861-27.2536
194.8527-0.15952.23191.7981-0.14765.21060.08590.5424-0.4151-0.348-0.07690.07060.43030.4921-0.13910.2028-0.02360.02710.1302-0.00810.2613-4.2284-62.4661-42.1482
204.5859-0.1282-0.26144.3261-2.05388.28130.0345-0.1264-0.25340.1559-0.302-0.0888-0.13150.61740.28430.09040.0248-0.0010.2002-0.06050.16325.3427-59.481-34.3392
213.86541.1472-1.77842.836-0.09214.9645-0.05790.1351-0.5394-0.23720.108-0.21750.30710.436-0.03760.16740.01390.0350.1776-0.02120.289123.6538-63.613-44.1599
224.30451.04-0.86432.92150.24533.36030.1405-0.2259-0.4860.1304-0.18490.03440.3970.06530.03990.14780.03890.03960.16370.05190.277715.8809-67.1567-35.5249
237.8081-0.2495-1.06616.7356-0.33531.9437-0.07181.25910.8694-0.69970.14350.4335-0.3716-0.0384-0.01730.2935-0.0558-0.00350.35560.1680.364720.1943-47.9371-47.2702
244.50930.0452-0.47714.7733-1.3556.58030.2496-0.07490.61810.1402-0.00050.4105-0.7110.1527-0.14210.1326-0.05340.08440.17620.00390.322212.717-53.1353-35.6847
254.66675.2461-0.95186.9751-0.11881.7952-0.1977-0.3149-1.01290.9037-0.44260.54490.0141-0.35730.71430.4062-0.03790.0540.37810.00981.04264.5511-75.5342-30.7543
264.4698-0.0173-0.73375.3011.86175.7430.0409-0.7293-0.37420.9549-0.00660.34220.46020.5328-0.09190.20760.01460.03380.45720.05650.228210.026-62.2771-20.1899
274.04040.1188-1.12653.97753.06277.35920.08980.2403-0.02-0.2809-0.14950.2456-0.2283-0.15720.01030.10920.0222-0.01920.16790.06820.22387.237-57.9796-38.7431
289.38926.4091-5.5229.8046-7.41695.80650.12991.37580.07140.11690.78230.6434-0.356-0.8124-0.72720.46760.0593-0.00620.4775-0.18430.427316.0599-71.0264-51.4422
294.0393-0.647-1.49047.50327.10932.02490.62611.01080.4047-0.9926-0.73250.2166-1.943-0.97390.15510.4430.0516-0.15110.51060.14630.4359-17.2728-47.0774-49.9545
303.408-1.0310.51052.02786.12639.4220.93630.0472-2.12020.19221.0475-1.28660.43941.0099-1.63160.45180.1028-0.01660.3518-0.00010.722123.0414-78.8661-39.9708
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 305 through 363 )
2X-RAY DIFFRACTION2chain 'A' and (resid 364 through 410 )
3X-RAY DIFFRACTION3chain 'A' and (resid 411 through 437 )
4X-RAY DIFFRACTION4chain 'A' and (resid 438 through 548 )
5X-RAY DIFFRACTION5chain 'B' and (resid 305 through 338 )
6X-RAY DIFFRACTION6chain 'B' and (resid 339 through 405 )
7X-RAY DIFFRACTION7chain 'B' and (resid 406 through 421 )
8X-RAY DIFFRACTION8chain 'B' and (resid 422 through 465 )
9X-RAY DIFFRACTION9chain 'B' and (resid 466 through 531 )
10X-RAY DIFFRACTION10chain 'B' and (resid 532 through 549 )
11X-RAY DIFFRACTION11chain 'C' and (resid 687 through 696 )
12X-RAY DIFFRACTION12chain 'D' and (resid 688 through 696 )
13X-RAY DIFFRACTION13chain 'E' and (resid 305 through 321 )
14X-RAY DIFFRACTION14chain 'E' and (resid 322 through 338 )
15X-RAY DIFFRACTION15chain 'E' and (resid 339 through 405 )
16X-RAY DIFFRACTION16chain 'E' and (resid 406 through 420 )
17X-RAY DIFFRACTION17chain 'E' and (resid 421 through 437 )
18X-RAY DIFFRACTION18chain 'E' and (resid 438 through 496 )
19X-RAY DIFFRACTION19chain 'E' and (resid 497 through 548 )
20X-RAY DIFFRACTION20chain 'F' and (resid 305 through 338 )
21X-RAY DIFFRACTION21chain 'F' and (resid 339 through 363 )
22X-RAY DIFFRACTION22chain 'F' and (resid 364 through 395 )
23X-RAY DIFFRACTION23chain 'F' and (resid 396 through 420 )
24X-RAY DIFFRACTION24chain 'F' and (resid 421 through 455 )
25X-RAY DIFFRACTION25chain 'F' and (resid 456 through 470 )
26X-RAY DIFFRACTION26chain 'F' and (resid 471 through 496 )
27X-RAY DIFFRACTION27chain 'F' and (resid 497 through 531 )
28X-RAY DIFFRACTION28chain 'F' and (resid 532 through 549 )
29X-RAY DIFFRACTION29chain 'G' and (resid 687 through 696 )
30X-RAY DIFFRACTION30chain 'H' and (resid 687 through 696 )

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