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- PDB-8vzp: Crystal Structure of the ER-alpha Ligand-binding Domain (L372S, L... -

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Basic information

Entry
Database: PDB / ID: 8vzp
TitleCrystal Structure of the ER-alpha Ligand-binding Domain (L372S, L536S) in complex with k-403
ComponentsEstrogen receptor
KeywordsNUCLEAR PROTEIN / 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 / regulation of inflammatory response / fibroblast proliferation / 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
: / Estrogen receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.72 Å
AuthorsMin, C.K. / Nwachukwu, J.C. / Hou, Y. / Russo, R.J. / Papa, A. / Min, J. / Peng, R. / Kim, S.H. / Ziegler, Y. / Rangarajan, E.S. ...Min, C.K. / Nwachukwu, J.C. / Hou, Y. / Russo, R.J. / Papa, A. / Min, J. / Peng, R. / Kim, S.H. / Ziegler, Y. / Rangarajan, E.S. / Izard, T. / Katzenellenbogen, B.S. / Katzenellenbogen, J.A. / Nettles, K.W.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI) United States
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2024
Title: Asymmetric allostery in estrogen receptor-alpha homodimers drives responses to the ensemble of estrogens in the hormonal milieu.
Authors: Min, C.K. / Nwachukwu, J.C. / Hou, Y. / Russo, R.J. / Papa, A. / Min, J. / Peng, R. / Kim, S.H. / Ziegler, Y. / Rangarajan, E.S. / Izard, T. / Katzenellenbogen, B.S. / Katzenellenbogen, J.A. / Nettles, K.W.
History
DepositionFeb 12, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 12, 2024Provider: repository / Type: Initial release

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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: Estrogen receptor
D: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)112,2848
Polymers110,2464
Non-polymers2,0384
Water5,314295
1
A: Estrogen receptor
B: Estrogen receptor
hetero molecules


  • defined by author&software
  • 56.1 kDa, 2 polymers
Theoretical massNumber of molelcules
Total (without water)56,1424
Polymers55,1232
Non-polymers1,0192
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2950 Å2
ΔGint-11 kcal/mol
Surface area18720 Å2
MethodPISA
2
C: Estrogen receptor
D: Estrogen receptor
hetero molecules


  • defined by author&software
  • 56.1 kDa, 2 polymers
Theoretical massNumber of molelcules
Total (without water)56,1424
Polymers55,1232
Non-polymers1,0192
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3020 Å2
ΔGint-14 kcal/mol
Surface area18810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.558, 58.906, 93.244
Angle α, β, γ (deg.)86.76, 74.95, 63.05
Int Tables number1
Space group name H-MP1

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Components

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


Mass: 27561.377 Da / Num. of mol.: 4 / Mutation: L372S, L536S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESR1, ESR, NR3A1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P03372
#2: Chemical
ChemComp-A1AHW / (1S,2R,4S)-N-(2-hydroxyethyl)-5,6-bis(4-hydroxyphenyl)-N-(4-methoxyphenyl)-7-oxabicyclo[2.2.1]hept-5-ene-2-sulfonamide


Mass: 509.571 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H27NO7S / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 295 / 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: 2.29 Å3/Da / Density % sol: 46.4 %
Crystal growTemperature: 298 K / Method: evaporation
Details: 20-25% PEG 3350, 200 mM MgCl2, 0.1 M Bis-Tris/Hepes/Tris-HCl

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Feb 12, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.72→37.454 Å / Num. obs: 62082 / % possible obs: 85.6 % / Redundancy: 7.7 % / CC1/2: 0.997 / Net I/σ(I): 8.2
Reflection shellResolution: 1.726→1.927 Å / Num. unique obs: 3104 / CC1/2: 0.821

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Processing

Software
NameVersionClassification
PHENIX1.18.2_3874refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.72→37.2 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.91 / Phase error: 29.99 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2216 3104 5 %
Rwork0.1809 --
obs0.183 62076 59.33 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.72→37.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7103 0 139 295 7537
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0117381
X-RAY DIFFRACTIONf_angle_d1.77510009
X-RAY DIFFRACTIONf_dihedral_angle_d9.1871038
X-RAY DIFFRACTIONf_chiral_restr0.0611186
X-RAY DIFFRACTIONf_plane_restr0.011230
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.72-1.7400.386939X-RAY DIFFRACTION1
1.74-1.770.302680.368157X-RAY DIFFRACTION4
1.77-1.80.3714180.3242257X-RAY DIFFRACTION6
1.8-1.840.421200.2987502X-RAY DIFFRACTION11
1.84-1.870.3172380.2971627X-RAY DIFFRACTION14
1.87-1.910.3472500.2855898X-RAY DIFFRACTION20
1.91-1.950.298580.26071152X-RAY DIFFRACTION25
1.95-20.2732780.2531527X-RAY DIFFRACTION34
2-2.050.2644950.24552291X-RAY DIFFRACTION50
2.05-2.10.26621380.22932940X-RAY DIFFRACTION65
2.1-2.160.2592060.21963725X-RAY DIFFRACTION83
2.16-2.230.24842190.20594095X-RAY DIFFRACTION90
2.23-2.310.23442230.19564088X-RAY DIFFRACTION91
2.31-2.40.22352250.18374071X-RAY DIFFRACTION90
2.4-2.510.22592070.18083940X-RAY DIFFRACTION87
2.51-2.650.24611970.18584001X-RAY DIFFRACTION88
2.65-2.810.2192380.18314233X-RAY DIFFRACTION93
2.81-3.030.23551960.18374093X-RAY DIFFRACTION91
3.03-3.330.22232310.17893894X-RAY DIFFRACTION86
3.33-3.820.19842360.15834239X-RAY DIFFRACTION94
3.82-4.810.19012240.14484049X-RAY DIFFRACTION90
4.81-37.20.22541990.1924154X-RAY DIFFRACTION92
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)
19.50854.5586-0.27567.1434-1.14832.21920.21810.15580.2372-0.1481-1.0107-1.4073-0.0530.95630.36560.25060.10710.00660.65450.11020.55672.4613-27.2818-10.9049
29.34114.26150.42554.94160.44341.3115-0.1254-0.2073-1.2341-0.209-0.0891-0.11340.4305-0.22850.05720.30340.055-0.02220.27940.05880.5154-20.8926-49.2067-8.2369
37.83336.3741-0.45595.5634-1.60221.9917-0.0458-0.1076-0.24060.3164-0.0384-0.25590.26530.12930.11240.21450.08990.02050.1872-0.02730.3083-16.1307-40.9132-1.6927
47.05852.36273.77274.02321.75678.15020.0735-0.1904-0.05180.2284-0.0442-0.2889-0.01460.35240.01570.13720.0558-0.02290.12020.01920.156-12.1967-29.8076-1.7641
51.3634-2.56172.02338.1477-6.02134.52180.0230.7248-0.6504-1.2621-0.0612-0.30860.63340.064-0.07140.4684-0.0224-0.08840.3577-0.13140.3947-21.3058-41.8052-17.2995
65.2318-0.55892.12389.91770.66370.92740.3117-0.058-0.03890.65250.01821.99380.0863-0.8492-0.26310.6383-0.05760.0020.47950.05320.7671-32.0427-42.0063-12.0426
78.27262.051-2.1683.4077-1.30112.4425-0.6640.4607-0.748-0.82830.1960.764-0.014-0.63020.16660.2766-0.0102-0.08720.32940.02280.3287-25.5182-31.3425-16.645
84.34591.29383.0416.7120.78448.204-0.1853-0.06840.03610.02160.0509-0.1559-0.14970.27460.09020.10520.03750.02460.12630.01830.2173-10.9189-24.7332-8.2809
92.3726-1.38231.94014.6871-2.30586.2203-0.1247-0.05560.39150.1051-0.0131-0.8167-0.7640.23740.00080.1386-0.00720.01140.3433-0.02690.4002-3.9133-18.1575-9.6588
104.98021.3562-2.28265.7022-2.12536.7376-0.02490.2972-0.1027-0.0460.0983-0.0880.0737-0.2554-0.15690.11710.0456-0.05090.1396-0.0210.1135-20.0091-22.5841-12.428
115.7973-0.02241.24314.7997-0.84745.13660.9366-0.7689-0.60651.0403-0.2166-0.21430.1392-0.3443-0.02590.5838-0.0417-0.01510.42850.12920.3351-14.2203-35.30378.8374
124.8595-0.6745-2.00392.77350.97033.03490.00330.14820.2537-0.3178-0.00270.3454-0.497-0.0374-0.070.21020.0268-0.02810.15550.06560.2803-27.44210.4058-14.5396
137.2341-1.15-1.73244.04853.08016.17-0.0844-0.5053-0.15170.0435-0.22860.742-0.20270.32820.19130.20260.07920.02030.19930.02090.2878-37.0055-3.968-5.1975
142.38611.44172.0393.02121.94255.75040.01770.10660.0034-0.2220.07330.2848-0.15-0.4038-0.07580.13460.0459-0.03190.20140.03010.1787-31.6323-10.5274-12.3177
156.1208-1.43072.32756.77551.36025.3022-0.4952-1.74710.11981.93490.70740.2876-0.354-0.2712-0.01160.53540.1355-0.01370.4584-0.02970.2099-25.9611-3.29238.7955
169.38154.82-6.80442.8861-4.19589.00830.114-0.675-0.05910.9375-0.1903-0.1916-0.41470.5419-0.02590.38790.0664-0.05670.28750.00190.2188-19.1643-9.95423.5921
176.53484.98433.76415.46751.48855.30240.05890.3159-0.1298-0.070.1901-0.13820.23520.0279-0.22570.12280.04890.03640.1359-0.0020.1145-23.9722-11.7095-14.3284
188.11294.93493.62286.42353.33335.7397-0.39750.72250.3886-0.9440.2214-0.0129-0.35680.20070.16670.31920.00790.00310.22990.06560.1707-20.0838-11.4469-23.1393
193.1612.0839-2.83455.0994-2.9247.4505-0.1672-0.1607-0.0430.14180.0774-0.30460.10670.25390.08950.12040.0498-0.05310.1137-0.0150.1731-18.303-14.8669-6.6159
205.72622.472.34624.9402-1.33428.99890.1096-0.72930.07390.0422-0.06321.01210.125-1.499-0.30990.27530.03060.00330.7417-0.03260.6197-43.3742-13.4209-10.139
217.4021-3.72340.20915.3472-0.41862.4858-0.09380.02041.07410.1902-0.0239-0.8199-0.0810.15560.12830.1427-0.1029-0.03270.2430.01380.2987-9.833-16.810338.4943
223.433-5.08420.56827.0742-0.37612.28260.0520.1651-0.2471-0.488-0.05920.067-0.31660.13670.04020.1823-0.065-0.0270.1542-0.00830.263-16.5491-14.799730.6791
237.7336-2.1557-4.63443.68711.6859.08560.13070.38950.0358-0.3786-0.1495-0.25930.0610.1010.00220.1631-0.01650.03470.1130.03730.1686-11.9417-26.163830.2582
243.18640.0262-0.94433.1264-2.978.66130.1062-0.42150.62230.32440.17240.6709-0.5099-1.0412-0.15970.3190.0733-0.0240.3187-0.03910.4054-26.4119-13.910843.9609
254.6893-4.1364.37347.6469-3.39324.5342-0.5183-0.12560.05180.3710.30990.73520.0728-0.51740.17060.1982-0.0010.0670.3510.02720.2678-25.4819-24.408245.5972
265.1048-1.7127-2.91587.0932.16133.1383-0.10840.324-0.0198-0.3405-0.06950.01650.2061-0.06440.07710.1199-0.0344-0.01050.09820.01110.1659-10.8242-31.45436.3895
271.970.93050.52413.6311-1.33169.3678-0.11220.1397-0.1447-0.27210.1233-0.51580.68121.0143-0.04410.19590.01830.03890.3239-0.00330.3533-3.5651-37.619938.5392
284.5373-3.72654.10256.2405-2.33594.80480.0312-0.00570.082-0.14940.0110.26180.1727-0.0458-0.11820.1287-0.02660.04890.21750.02570.262-19.6009-33.364441.745
293.7787-2.2036-5.29554.7952.68117.61980.96971.16510.8131-0.8505-0.4310.4196-0.2084-0.7174-0.50530.57090.1015-0.05940.45460.09960.3541-15.6389-20.664820.3656
305.2431.34453.50121.97832.45373.6759-0.2603-0.0751-0.09080.31650.0170.20160.03630.04280.22980.302-0.05360.04480.17430.07260.2588-26.9931-56.08445.1086
316.18840.82222.68954.86093.75225.4849-0.14480.21120.0525-0.2499-0.17730.9405-0.0830.03450.19560.1697-0.03550.00070.16810.04410.3313-36.897-51.67634.2452
323.1313-0.4375-2.05712.69990.16986.95020.1103-0.14590.30030.15090.06250.2424-0.2545-0.5321-0.15120.0887-0.0370.03780.17120.00360.2717-31.8266-44.830241.6793
337.20130.5419-0.4575.20890.91945.6940.08350.254-0.5408-1.0440.1362-0.260.39120.2095-0.26070.4086-0.07420.0540.2604-0.04420.2094-24.6647-55.643923.436
345.6471-1.7858-1.75717.70280.48868.08190.32531.4572-0.3357-1.4112-0.26440.3363-0.05110.59690.05280.4618-0.0504-0.0020.2878-0.02280.1996-21.0517-46.348722.5382
354.027-2.5186-1.72928.12192.20417.152-0.1407-0.28160.4096-0.03340.3292-0.2127-0.0835-0.0481-0.11880.1507-0.0649-0.00470.1350.00220.2399-22.5162-45.732242.3146
363.306-2.9607-3.00158.49992.78436.792-0.032-0.33880.29110.86930.0152-0.20060.18650.04330.06230.249-0.0142-0.00040.18030.0120.1975-17.5116-46.073551.1837
377.6722-4.93614.6885.7304-3.29356.5757-0.02540.22210.0757-0.1412-0.0380.0246-0.03910.15110.08220.1698-0.03620.0330.0866-0.01540.1864-18.1938-40.926635.6249
386.5995-0.8570.46588.6248-1.79092.7370.04770.74660.4524-0.00840.07651.3310.094-1.1678-0.3290.25460.04630.01840.48880.01750.646-43.3634-42.193139.3431
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 306 through 322 )
2X-RAY DIFFRACTION2chain 'A' and (resid 323 through 338 )
3X-RAY DIFFRACTION3chain 'A' and (resid 339 through 363 )
4X-RAY DIFFRACTION4chain 'A' and (resid 364 through 395 )
5X-RAY DIFFRACTION5chain 'A' and (resid 396 through 407 )
6X-RAY DIFFRACTION6chain 'A' and (resid 408 through 420 )
7X-RAY DIFFRACTION7chain 'A' and (resid 421 through 438 )
8X-RAY DIFFRACTION8chain 'A' and (resid 439 through 465 )
9X-RAY DIFFRACTION9chain 'A' and (resid 466 through 496 )
10X-RAY DIFFRACTION10chain 'A' and (resid 497 through 526 )
11X-RAY DIFFRACTION11chain 'A' and (resid 527 through 546 )
12X-RAY DIFFRACTION12chain 'B' and (resid 305 through 341 )
13X-RAY DIFFRACTION13chain 'B' and (resid 342 through 363 )
14X-RAY DIFFRACTION14chain 'B' and (resid 364 through 395 )
15X-RAY DIFFRACTION15chain 'B' and (resid 396 through 421 )
16X-RAY DIFFRACTION16chain 'B' and (resid 422 through 437 )
17X-RAY DIFFRACTION17chain 'B' and (resid 438 through 465 )
18X-RAY DIFFRACTION18chain 'B' and (resid 466 through 496 )
19X-RAY DIFFRACTION19chain 'B' and (resid 497 through 525 )
20X-RAY DIFFRACTION20chain 'B' and (resid 526 through 546 )
21X-RAY DIFFRACTION21chain 'C' and (resid 306 through 338 )
22X-RAY DIFFRACTION22chain 'C' and (resid 339 through 363 )
23X-RAY DIFFRACTION23chain 'C' and (resid 364 through 394 )
24X-RAY DIFFRACTION24chain 'C' and (resid 395 through 420 )
25X-RAY DIFFRACTION25chain 'C' and (resid 421 through 438 )
26X-RAY DIFFRACTION26chain 'C' and (resid 439 through 465 )
27X-RAY DIFFRACTION27chain 'C' and (resid 466 through 496 )
28X-RAY DIFFRACTION28chain 'C' and (resid 497 through 525 )
29X-RAY DIFFRACTION29chain 'C' and (resid 526 through 546 )
30X-RAY DIFFRACTION30chain 'D' and (resid 305 through 341 )
31X-RAY DIFFRACTION31chain 'D' and (resid 342 through 363 )
32X-RAY DIFFRACTION32chain 'D' and (resid 364 through 394 )
33X-RAY DIFFRACTION33chain 'D' and (resid 395 through 410 )
34X-RAY DIFFRACTION34chain 'D' and (resid 411 through 437 )
35X-RAY DIFFRACTION35chain 'D' and (resid 438 through 468 )
36X-RAY DIFFRACTION36chain 'D' and (resid 469 through 496 )
37X-RAY DIFFRACTION37chain 'D' and (resid 497 through 525 )
38X-RAY DIFFRACTION38chain 'D' and (resid 526 through 546 )

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