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- PDB-7rs2: Crystal Structure of the ER-alpha Ligand-binding Domain (L372S, L... -

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Basic information

Entry
Database: PDB / ID: 7rs2
TitleCrystal Structure of the ER-alpha Ligand-binding Domain (L372S, L536S) in complex with DMERI-23
ComponentsEstrogen receptor
KeywordsTRANSCRIPTION/TRANSCRIPTION INHIBITOR / ER-alpha / ligand complex / DMERI / 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 / prostate epithelial cord elongation / epithelial cell development / negative regulation of smooth muscle cell apoptotic process / mammary gland branching involved in pregnancy / uterus development / vagina development / androgen metabolic process / TFIIB-class transcription factor binding / steroid hormone mediated signaling pathway / mammary gland alveolus development / intracellular estrogen receptor signaling pathway / cellular response to estrogen stimulus / estrogen response element binding / positive regulation of phospholipase C activity / intracellular steroid hormone receptor signaling pathway / negative regulation of canonical NF-kappaB signal transduction / Nuclear signaling by ERBB4 / RNA polymerase II preinitiation complex assembly / protein localization to chromatin / TBP-class protein binding / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / steroid binding / nitric-oxide synthase regulator activity / ESR-mediated signaling / 14-3-3 protein binding / transcription corepressor binding / negative regulation of miRNA transcription / cellular response to estradiol stimulus / transcription coregulator binding / stem cell differentiation / nuclear estrogen receptor binding / positive regulation of nitric-oxide synthase activity / euchromatin / SUMOylation of intracellular receptors / negative regulation of DNA-binding transcription factor activity / transcription coactivator binding / beta-catenin binding / Nuclear Receptor transcription pathway / response to estrogen / male gonad development / Constitutive Signaling by Aberrant PI3K in Cancer / Regulation of RUNX2 expression and activity / nuclear receptor activity / positive regulation of nitric oxide biosynthetic process / positive regulation of DNA-binding transcription factor activity / positive regulation of fibroblast proliferation / Ovarian tumor domain proteases / sequence-specific double-stranded DNA binding / response to estradiol / PIP3 activates AKT signaling / phospholipase C-activating G protein-coupled receptor signaling pathway / ATPase binding / positive regulation of cytosolic calcium ion concentration / 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 / chromatin / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / protein kinase binding / positive regulation of DNA-templated transcription / Golgi apparatus / negative regulation of transcription by RNA polymerase II / enzyme binding / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / membrane / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
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-7I5 / Estrogen receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.72 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 1.1Sep 15, 2021Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 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

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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)121,1908
Polymers118,8394
Non-polymers2,3504
Water6,215345
1
A: Estrogen receptor
B: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,5954
Polymers59,4202
Non-polymers1,1752
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3190 Å2
ΔGint-15 kcal/mol
Surface area20040 Å2
MethodPISA
2
C: Estrogen receptor
D: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,5954
Polymers59,4202
Non-polymers1,1752
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3200 Å2
ΔGint-14 kcal/mol
Surface area20390 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.860, 58.761, 93.698
Angle α, β, γ (deg.)86.450, 75.110, 62.820
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:

Component-ID: 0 / End auth comp-ID: ALA / End label comp-ID: ALA / Refine code: 0

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LYSLYSAA303 - 5469 - 252
21LYSLYSBB303 - 5469 - 252
12SERSERAA295 - 5461 - 252
22SERSERCC295 - 5461 - 252
13LYSLYSAA303 - 5469 - 252
23LYSLYSDD303 - 5469 - 252
14LYSLYSBB303 - 5469 - 252
24LYSLYSCC303 - 5469 - 252
15LYSLYSBB303 - 5469 - 252
25LYSLYSDD303 - 5469 - 252
16LYSLYSCC303 - 5469 - 252
26LYSLYSDD303 - 5469 - 252

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: 29709.824 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-7I5 / (2E)-3-(4-{[(1S,2R,4S,5S,6S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]heptane-2-sulfonyl](2,2,2-trifluoroethyl)amino}phenyl)prop-2-enoic acid


Mass: 587.564 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C29H24F3NO7S / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 345 / 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: 2.14 Å3/Da / Density % sol: 42.54 %
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: RAYONIX MX300-HS / Detector: CCD / Date: Mar 22, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.72→90.36 Å / Num. obs: 75804 / % possible obs: 89 % / Redundancy: 7.8 % / CC1/2: 0.994 / Net I/σ(I): 10.8
Reflection shellResolution: 1.72→1.88 Å / Num. unique obs: 3791 / CC1/2: 0.436

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Phasing

PhasingMethod: molecular replacement

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Processing

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

2qxs


Resolution: 1.72→90.36 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.926 / SU B: 6.696 / SU ML: 0.102 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.172 / ESU R Free: 0.145 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.221 3761 5 %RANDOM
Rwork0.1942 ---
obs0.1955 72054 72.78 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: MASK
Displacement parametersBiso max: 120.22 Å2 / Biso mean: 32.008 Å2 / Biso min: 9.47 Å2
Baniso -1Baniso -2Baniso -3
1--0.37 Å2-0.02 Å20.07 Å2
2--0.13 Å20.01 Å2
3---0.16 Å2
Refinement stepCycle: final / Resolution: 1.72→90.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7616 0 148 345 8109
Biso mean--35.01 32.7 -
Num. residues----956
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0137938
X-RAY DIFFRACTIONr_bond_other_d0.0010.0177599
X-RAY DIFFRACTIONr_angle_refined_deg1.4211.6410741
X-RAY DIFFRACTIONr_angle_other_deg1.3161.57917619
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.7065951
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.45122.81363
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.564151488
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.2861540
X-RAY DIFFRACTIONr_chiral_restr0.0740.21017
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.028531
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021541
Refine LS restraints NCS

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

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A71540.1
12B71540.1
21A80420.07
22C80420.07
31A72180.1
32D72180.1
41B71950.1
42C71950.1
51B75720.07
52D75720.07
61C72610.1
62D72610.1
LS refinement shellResolution: 1.723→1.768 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.127 6 -
Rwork0.324 256 -
all-262 -
obs--3.42 %
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)
11.7326-0.09781.46940.51.15094.35210.2611-0.10010.0384-0.018-0.0043-0.14770.2458-0.1804-0.25680.2569-0.0261-0.01180.27070.03790.408931.524-17.51414.602
24.0094-4.85590.90758.08131.2642.943-0.0390.00730.17740.00630.0162-0.326-0.03630.12960.02290.0347-0.0277-0.00910.1240.02530.13427.953-3.24426.129
38.4971-0.68690.91390.1760.03930.3717-0.1344-0.21180.39250.015-0.00040.1139-0.1808-0.09440.13480.20630.02260.01920.11650.01480.22545.52618.78123.647
48.985-5.89590.82635.3729-0.65311.97910.04920.1252-0.036-0.166-0.06720.1518-0.1464-0.04780.0180.1125-0.0481-0.01190.0402-0.01460.0479.20710.9616.689
52.9734-1.6251-1.69693.00371.2343.37210.0414-0.01890.09280.05850.00390.0666-0.1303-0.0204-0.04530.0457-0.0165-0.01920.01040.00580.0529.9294.11921.816
67.3077-3.45186.08323.0203-2.72085.0883-0.11280.0016-0.1823-0.61470.12950.7998-0.2234-0.0477-0.01680.54550.0803-0.0990.4472-0.01820.8128-9.27710.31325.794
714.664-3.81718.0875.1087-1.932610.048-0.2676-0.08920.13540.15960.04490.3604-0.2201-0.2740.22270.0705-0.01520.03380.04-0.04390.131-0.0091.54731.302
83.0165-0.6068-0.26052.61981.26428.562-0.0171-0.04370.06270.17960.0337-0.0324-0.16850.4012-0.01650.0434-0.0161-0.02910.0210.00650.092415.539-2.34627.512
98.3482-6.2636-7.50518.52224.186910.05690.07281.0544-0.0275-0.6932-0.19870.16051.0575-0.96910.12590.4228-0.036-0.02840.2841-0.04130.238912.554-13.3369.644
101.3066-0.0868-0.8941.72381.032913.21470.02010.1158-0.013-0.1315-0.0606-0.12790.1930.14550.04040.02740.004-0.01650.05-0.00470.119721.922-11.80623.484
116.2906-4.06726.62674.7721-4.644710.45150.01790.05410.0556-0.0312-0.01860.1251-0.1187-0.03740.00060.0367-0.01740.02260.0187-0.02040.08096.64-7.65228.058
1217.20360.33170.62743.07072.64414.35010.38720.00350.5448-0.1974-0.19450.1637-0.2858-0.0108-0.19270.23540.027-0.01520.20720.07110.157311.94.7746.294
134.09451.30884.16144.2419-1.88388.1728-0.0041-0.39680.20130.5938-0.220.156-0.1851-0.42750.22410.2489-0.04910.04230.1141-0.00740.1021.4-27.01140.739
142.41880.21550.68322.70640.59912.95640.00220.2771-0.0112-0.22630.01670.23520.0541-0.212-0.0190.0737-0.0563-0.04150.13060.02440.0982-10.778-27.61719.204
152.16450.07190.48631.6085-0.14592.9786-0.0030.13840.0795-0.06850.0212-0.00470.013-0.1879-0.01810.08-0.0179-0.01060.02990.01670.06061.13-20.66823.748
163.2012-0.321-0.09191.1713-0.18640.9819-0.06110.14070.1133-0.11060.04610.1458-0.0197-0.15950.0150.088-0.0039-0.01920.0396-0.01370.0784-2.59-15.17521.73
171.61711.6659-1.3583.2802-0.64011.61990.2451-0.1526-0.00820.4965-0.0829-0.4218-0.1843-0.0232-0.16220.3840.0597-0.10970.39390.03670.534155.5797.19476.665
184.30694.7426-0.49068.00490.3413.6172-0.01930.0785-0.1045-0.0667-0.0533-0.30830.01470.17530.07260.07280.04820.00480.17690.02780.158552.111-7.05665.013
198.80661.9399-0.30591.2874-0.06220.936-0.10520.0876-0.4761-0.2070.07360.14230.2529-0.23480.03160.28020.0301-0.02740.17670.00280.192629.759-29.13167.623
2010.15676.9353-0.07056.217-0.45641.82930.0801-0.12760.06360.1606-0.10690.11480.2077-0.03020.02680.17020.0525-0.02170.0391-0.03740.055733.369-21.31274.523
213.21171.56062.11013.31591.10023.29050.01870.0572-0.0942-0.1279-0.0030.03530.19350.1242-0.01580.08580.0321-0.01140.0188-0.00570.028835.063-13.40970.101
226.88080.65412.00172.93691.34351.04630.2488-0.0761-0.54150.1469-0.2850.45390.1472-0.13920.03630.4586-0.0547-0.0020.28930.09440.472318.542-22.89663.174
2313.63352.4138-7.57315.4152-0.62311.089-0.27750.0329-0.1252-0.02540.13080.53030.3981-0.28090.14670.1565-0.0064-0.05350.0724-0.02950.125222.893-12.460.832
242.39870.41860.0282.81210.3526.6324-0.07010.2171-0.0187-0.26650.0255-0.15860.2980.2250.04470.07210.01910.0040.0369-0.00130.08439.294-7.90862.99
2510.14474.52486.13533.56723.914310.2954-0.0091-0.99120.44770.3104-0.28160.2043-0.8021-0.66180.29070.51430.0824-0.08470.1982-0.09760.244836.6132.9581.557
261.6275-0.2108-0.0712.1696-0.244811.25780.0410.01220.04990.1055-0.1091-0.2122-0.11840.3880.06810.0184-0.0069-0.00020.1206-0.00630.130246.0531.47467.657
275.77132.7036-4.69893.8097-3.29658.698-0.0273-0.0452-0.1123-0.0026-0.05060.06560.19080.05680.07790.05820.023-0.0460.0107-0.02260.072230.836-2.93563.618
2817.96931.0301-1.92271.97470.91741.9006-0.10040.2743-0.55680.25040.03350.17850.1770.22840.06690.2590.00110.00010.19530.04680.149435.987-15.53684.855
293.6185-1.4517-3.60275.2277-1.28498.1056-0.05030.4068-0.1836-0.3611-0.11150.1963-0.004-0.4860.16170.3449-0.0138-0.06070.12710.01860.074526.01416.81750.689
301.4192-0.09440.35781.92210.73033.3084-0.0188-0.1418-0.0040.11650.02850.0588-0.2838-0.3016-0.00980.08980.05670.0010.09920.02110.031417.39414.07469.772
311.3503-4.39620.792518.0752-1.18111.825-0.3296-0.342-0.31521.44270.29280.87160.1081-0.21210.03680.6271-0.0172-0.00560.6980.08730.26921.65212.36189.367
321.6150.05980.12821.5551-0.07142.2685-0.0379-0.0846-0.04660.0275-0.00880.0416-0.076-0.06310.04670.09170.0048-0.02020.0130.00030.047825.5256.87965.092
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A295 - 306
2X-RAY DIFFRACTION2A307 - 321
3X-RAY DIFFRACTION3A322 - 338
4X-RAY DIFFRACTION4A339 - 363
5X-RAY DIFFRACTION5A364 - 411
6X-RAY DIFFRACTION6A412 - 420
7X-RAY DIFFRACTION7A421 - 438
8X-RAY DIFFRACTION8A439 - 455
9X-RAY DIFFRACTION9A456 - 465
10X-RAY DIFFRACTION10A466 - 496
11X-RAY DIFFRACTION11A497 - 525
12X-RAY DIFFRACTION12A526 - 546
13X-RAY DIFFRACTION13B303 - 321
14X-RAY DIFFRACTION14B322 - 363
15X-RAY DIFFRACTION15B364 - 496
16X-RAY DIFFRACTION16B497 - 546
17X-RAY DIFFRACTION17C295 - 306
18X-RAY DIFFRACTION18C307 - 321
19X-RAY DIFFRACTION19C322 - 338
20X-RAY DIFFRACTION20C339 - 363
21X-RAY DIFFRACTION21C364 - 407
22X-RAY DIFFRACTION22C408 - 418
23X-RAY DIFFRACTION23C419 - 437
24X-RAY DIFFRACTION24C438 - 455
25X-RAY DIFFRACTION25C456 - 465
26X-RAY DIFFRACTION26C466 - 496
27X-RAY DIFFRACTION27C497 - 526
28X-RAY DIFFRACTION28C527 - 546
29X-RAY DIFFRACTION29D303 - 321
30X-RAY DIFFRACTION30D322 - 407
31X-RAY DIFFRACTION31D408 - 421
32X-RAY DIFFRACTION32D422 - 546

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