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- PDB-7rry: Crystal Structure of the ER-alpha Ligand-binding Domain (L372S, L... -

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Basic information

Entry
Database: PDB / ID: 7rry
TitleCrystal Structure of the ER-alpha Ligand-binding Domain (L372S, L536S) in complex with DMERI-20
ComponentsEstrogen receptor
KeywordsTRANSCRIPTION/TRANSCRIPTION INHIBITOR / ER-alpha / ligand complex / DMERI / TRANSCRIPTION / TRANSCRIPTION-TRANSCRIPTION INHIBITOR complex
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
Chem-L84 / Estrogen receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.87 Å
AuthorsMin, J. / Nwachukwu, J.C. / Min, C.K. / Njeri, J.W. / Srinivasan, S. / Rangarajan, E.S. / Nettles, C.C. / Yan, S. / Houtman, R. / Griffin, P.R. ...Min, J. / Nwachukwu, J.C. / Min, C.K. / Njeri, J.W. / Srinivasan, S. / Rangarajan, E.S. / Nettles, C.C. / Yan, S. / Houtman, R. / Griffin, P.R. / 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: 2021
Title: Dual-mechanism estrogen receptor inhibitors.
Authors: Min, J. / Nwachukwu, J.C. / Min, C.K. / Njeri, J.W. / Srinivasan, S. / Rangarajan, E.S. / Nettles, C.C. / Sanabria Guillen, V. / Ziegler, Y. / Yan, S. / Carlson, K.E. / Hou, Y. / Kim, S.H. / ...Authors: Min, J. / Nwachukwu, J.C. / Min, C.K. / Njeri, J.W. / Srinivasan, S. / Rangarajan, E.S. / Nettles, C.C. / Sanabria Guillen, V. / Ziegler, Y. / Yan, S. / Carlson, K.E. / Hou, Y. / Kim, S.H. / Novick, S. / Pascal, B.D. / Houtman, R. / Griffin, P.R. / Izard, T. / Katzenellenbogen, B.S. / Katzenellenbogen, J.A. / Nettles, K.W.
History
DepositionAug 10, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 8, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 26, 2022Group: Derived calculations
Category: pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list
Item: _pdbx_struct_assembly_prop.value
Revision 1.2Oct 18, 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
C: Estrogen receptor
D: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,45610
Polymers117,7504
Non-polymers2,7066
Water3,945219
1
A: Estrogen receptor
B: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,2285
Polymers58,8752
Non-polymers1,3533
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3080 Å2
ΔGint-15 kcal/mol
Surface area18780 Å2
MethodPISA
2
C: Estrogen receptor
D: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,2285
Polymers58,8752
Non-polymers1,3533
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3130 Å2
ΔGint-13 kcal/mol
Surface area18320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.416, 59.119, 93.522
Angle α, β, γ (deg.)86.540, 74.980, 63.190
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14B
24C
15B
25D
16C
26D

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1010A306 - 546
2010B306 - 546
1020A306 - 551
2020C306 - 551
1030A306 - 544
2030D306 - 544
1040B306 - 546
2040C306 - 546
1050B305 - 544
2050D305 - 544
1060C306 - 544
2060D306 - 544

NCS ensembles :
ID
1
2
3
4
5
6

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Components

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


Mass: 29437.570 Da / Num. of mol.: 4 / Fragment: Ligand binding domain / 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-L84 / (1S,2R,4S,5S,6S)-5,6-bis(4-hydroxyphenyl)-N-{4-[3-(piperidin-1-yl)propoxy]phenyl}-N-(2,2,2-trifluoroethyl)-7-oxabicyclo[2.2.1]heptane-2-sulfonamide


Mass: 658.728 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H37F3N2O6S / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 219 / 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: 42.99 %
Crystal growTemperature: 298 K / Method: evaporation
Details: 20-25% PEG 3350, 200 mM MgCl2, 0.1 M Bis-Tris/Hepes/Tris-HCl
PH range: 6.5 - 8.0

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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: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 18, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.869→90.134 Å / Num. obs: 61892 / % possible obs: 76 % / Redundancy: 6.9 % / CC1/2: 0.99 / Net I/σ(I): 7.5
Reflection shellResolution: 1.869→2.045 Å / Mean I/σ(I) obs: 1.4 / Num. unique obs: 2861 / CC1/2: 0.49

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
AutoProcessdata reduction
PHASERphasing
REFMAC5.8.0253refinement
PDB_EXTRACT3.25data extraction
Aimlessdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2QXS

2qxs


Resolution: 1.87→90.13 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.924 / SU B: 10.609 / SU ML: 0.147 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.232 / ESU R Free: 0.18 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2356 3095 5 %RANDOM
Rwork0.2073 ---
obs0.2087 58796 75.97 %-
Solvent computationIon probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1.1 Å / Solvent model: MASK
Displacement parametersBiso max: 120.86 Å2 / Biso mean: 44.747 Å2 / Biso min: 19.46 Å2
Baniso -1Baniso -2Baniso -3
1--0.35 Å2-0.08 Å2-0.3 Å2
2---0.41 Å20.32 Å2
3---0.47 Å2
Refinement stepCycle: final / Resolution: 1.87→90.13 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6994 0 177 219 7390
Biso mean--51.25 42.6 -
Num. residues----890
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0137807
X-RAY DIFFRACTIONr_bond_other_d0.0010.0177440
X-RAY DIFFRACTIONr_angle_refined_deg1.4661.65710570
X-RAY DIFFRACTIONr_angle_other_deg1.2951.59217246
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.1935925
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.17122.446368
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.837151432
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.6111542
X-RAY DIFFRACTIONr_chiral_restr0.0740.2987
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.028366
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021544
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A71210.11
12B71210.11
21A76880.09
22C76880.09
31A69700.1
32D69700.1
41B71190.11
42C71190.11
51B71060.09
52D71060.09
61C70530.1
62D70530.1
LS refinement shellResolution: 1.87→1.918 Å / Rfactor Rfree error: 0
RfactorNum. reflection% reflection
Rfree0.23 6 -
Rwork0.329 103 -
obs--1.78 %
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)
16.99884.1553-0.2737.141-0.51062.71520.0656-0.0080.03910.09080.0015-0.20860.18990.178-0.06710.12530.12380.01440.1508-0.02150.154312.947-10.341-25.662
212.28677.22620.03597.15330.12572.4251-0.14480.0350.15660.33670.17450.06830.2656-0.0185-0.02970.16350.0884-0.01520.0773-0.01530.01756.084-12.772-17.976
33.2711.31711.64636.32390.78634.3303-0.03820.0356-0.0576-0.18190.0660.26130.1359-0.0919-0.02780.08920.0593-0.00120.0724-0.0030.0263.918-6.888-23.694
413.24322.6591-6.69475.6909-2.294813.2293-0.2470.46920.084-0.47580.29180.69010.0659-0.4728-0.04480.15450.026-0.09580.0997-0.02940.1334-2.976-3.272-32.735
52.5002-0.09280.2756.1397-2.02425.3164-0.0618-0.13730.23550.38580.0017-0.8992-0.20460.47260.06010.06230.0318-0.02440.1443-0.05070.237615.7447.192-24.331
67.14983.6574-5.86196.0093-4.270110.1269-0.0218-0.0310.0319-0.03450.16140.18790.2435-0.1626-0.13970.07520.05-0.04560.0653-0.03810.05942.2724.958-27.893
720.2815-7.8564-1.77795.4627-0.57691.70180.0598-0.5095-0.11320.49530.1044-0.13820.20070.0567-0.16420.50490.0059-0.06050.3372-0.01180.226711.966-8.457-7.156
83.4944-0.6425-1.63617.83172.414910.1764-0.14260.35540.0654-0.5201-0.06760.1458-0.1253-0.13750.21020.2596-0.00440.03420.12520.04360.0333-0.21926.972-40.675
96.7775-0.1978-4.93555.3496-0.43411.6984-0.1697-0.74880.20690.3651-0.32580.3612-0.434-0.10120.49550.20190.1178-0.04220.2145-0.09140.1888-11.98731.27-16.84
104.7287-0.0047-4.47364.0519-0.106913.9322-0.0888-0.2497-0.05920.0535-0.07550.57070.1525-0.06550.16430.09980.07450.00170.0834-0.01680.0838-14.3124.449-21.312
112.59850.18032.59533.75411.61947.97240.06680.0961-0.1807-0.14010.01520.23330.0146-0.2555-0.0820.0450.0433-0.01540.1002-0.01360.0301-8.9917.841-28.622
1213.3532-7.1971.87697.99680.04323.2069-0.1676-0.45920.44850.24480.2907-0.6091-0.38740.038-0.1230.45290.0332-0.10660.2223-0.07260.0855-0.93728.431-11.431
131.1878-1.91181.43979.3136-7.49856.4248-0.3777-0.4102-0.21670.86620.2384-0.0037-0.2153-0.33480.13920.770.050.14080.62450.0310.3733-5.90620.83-3.368
142.39660.26271.25774.57380.53565.26470.0226-0.1382-0.07410.30630.0966-0.17860.0925-0.0445-0.11930.11250.0557-0.00460.0663-0.01110.01860.15917.415-23.12
1513.06057.61194.76837.49643.55424.2511-0.13240.36690.2016-0.53510.0814-0.1132-0.1490.18470.0510.17350.02410.04250.08420.01760.0222.43416.944-39.432
1611.88983.0328-5.56955.0219-2.06125.95810.0021-0.005-0.10620.24390.0382-0.2646-0.03690.0663-0.04030.0550.0591-0.04130.0803-0.04310.03774.57313.705-23.382
177.3382-3.48654.283810.5409-7.050416.0073-0.00810.35340.10620.0654-0.29130.4311-0.4713-0.72540.29940.21220.0124-0.01850.40380.03860.4362-20.66715.3-27.629
185.686-2.652-0.00675.3982-0.06472.2191-0.08060.01310.2043-0.03810.0312-0.3903-0.1850.20210.04950.0803-0.08330.01680.1225-0.01890.059613.35810.96321.931
192.4021-1.2323-0.57165.31610.51663.0385-0.0369-0.01980.1314-0.10080.03580.2122-0.1528-0.0750.00110.0746-0.0441-0.00610.0637-0.01760.03284.619.54318.377
204.1399-1.3597-0.8724.7463-0.23473.3675-0.1675-0.0313-0.05560.01010.0680.29450.1574-0.15440.09950.0619-0.0381-0.0010.0549-0.02230.04645.637-0.10823.516
211.48750.10440.14043.00810.889615.1159-0.03680.1455-0.011-0.1543-0.0035-0.37820.35060.42290.04030.02810.00950.02060.1384-0.04260.149618.703-8.77922.624
228.8607-4.13577.88736.0674-4.853111.3898-0.1539-0.09730.2358-0.03260.0520.27130.016-0.32510.10190.0766-0.04220.0320.0538-0.03550.07642.327-4.03724.384
2319.93552.35753.67523.57570.36432.38060.43830.65560.7655-0.4672-0.0539-0.3051-0.6169-0.0279-0.38440.64970.04540.1740.3910.04320.31911.939.3363.334
244.7692.49844.25793.85350.014713.92280.0451-0.4721-0.04790.4481-0.22710.0906-0.0713-0.1720.18190.2543-0.02450.03120.13110.0190.0188-0.478-25.92537.41
253.5902-0.11851.87565.3801-2.998314.1669-0.19210.666-0.4032-0.4920.15370.63670.241-0.32620.03840.1344-0.08450.00620.1995-0.07390.249-12.032-30.61713.198
265.0520.51784.66433.61091.421312.3881-0.0940.32640.1916-0.1450.07160.8471-0.29950.11390.02240.0979-0.06450.00760.08940.01170.2351-14.383-23.47117.182
273.07390.4562-1.74433.50640.75157.63140.0272-0.18650.36610.19110.01410.4255-0.1789-0.4341-0.04130.0523-0.01430.03960.111-0.0290.1015-9.017-16.80125.043
284.22174.4594-1.650310.76911.22476.9628-0.36410.3372-0.1037-0.39380.5042-0.31180.52930.2434-0.14010.2941-0.01370.0380.222-0.03930.0234-0.821-27.4377.919
290.47811.3367-2.1044.1244-6.52810.4026-0.1740.09910.0887-0.6615-0.0673-0.06250.83290.16480.24130.9153-0.0919-0.13410.77880.04450.5588-5.389-20.6650.078
3013.5043-9.25278.696511.9291-6.8713.06690.00960.66130.1826-0.74090.10170.0605-0.1670.048-0.11130.2413-0.09140.03430.15180.00950.03762.635-17.3538.704
316.3567-3.5293-2.19716.64072.415.3249-0.05670.0109-0.05590.24580.11120.03510.23370.107-0.05450.0949-0.01740.02590.0257-0.01310.01231.961-21.12424.702
321.3867-2.68490.2625.4375-2.567917.9532-0.13550.08530.15330.32-0.1007-0.3366-0.4416-0.39340.23620.2983-0.0642-0.02020.2091-0.09790.3786-7.199-5.80931.146
3313.4042-5.0183-3.99646.12152.0934.4625-0.1139-0.28160.14730.83580.0783-0.03680.1946-0.01240.03560.2166-0.02330.01140.07-0.00390.00484.489-17.55735.224
3411.7396-3.39026.00164.5461-2.50595.8355-0.00540.07420.144-0.21670.01480.05190.03940.0297-0.00940.0866-0.04460.04570.0498-0.04380.05224.673-12.83219.821
358.36977.1146-8.336314.3872-10.870215.1833-0.0624-0.10430.1228-0.0684-0.04810.15190.2769-0.67050.11060.2848-0.0083-0.02750.4357-0.02290.4157-20.487-13.79223.99
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A308 - 338
2X-RAY DIFFRACTION2A339 - 363
3X-RAY DIFFRACTION3A364 - 420
4X-RAY DIFFRACTION4A421 - 438
5X-RAY DIFFRACTION5A439 - 496
6X-RAY DIFFRACTION6A497 - 528
7X-RAY DIFFRACTION7A536 - 551
8X-RAY DIFFRACTION8B305 - 321
9X-RAY DIFFRACTION9B322 - 341
10X-RAY DIFFRACTION10B342 - 363
11X-RAY DIFFRACTION11B364 - 394
12X-RAY DIFFRACTION12B395 - 407
13X-RAY DIFFRACTION13B408 - 418
14X-RAY DIFFRACTION14B421 - 465
15X-RAY DIFFRACTION15B466 - 496
16X-RAY DIFFRACTION16B497 - 525
17X-RAY DIFFRACTION17B526 - 544
18X-RAY DIFFRACTION18C307 - 338
19X-RAY DIFFRACTION19C339 - 419
20X-RAY DIFFRACTION20C421 - 466
21X-RAY DIFFRACTION21C467 - 496
22X-RAY DIFFRACTION22C497 - 525
23X-RAY DIFFRACTION23C537 - 548
24X-RAY DIFFRACTION24D306 - 321
25X-RAY DIFFRACTION25D322 - 330
26X-RAY DIFFRACTION26D341 - 363
27X-RAY DIFFRACTION27D364 - 394
28X-RAY DIFFRACTION28D395 - 407
29X-RAY DIFFRACTION29D408 - 420
30X-RAY DIFFRACTION30D421 - 437
31X-RAY DIFFRACTION31D438 - 455
32X-RAY DIFFRACTION32D456 - 468
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