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- PDB-2xkw: LIGAND BINDING DOMAIN OF HUMAN PPAR-GAMMA IN COMPLEX WITH THE AGO... -

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Basic information

Entry
Database: PDB / ID: 2xkw
TitleLIGAND BINDING DOMAIN OF HUMAN PPAR-GAMMA IN COMPLEX WITH THE AGONIST PIOGLITAZONE
ComponentsPEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA
KeywordsTRANSCRIPTION / NUCLEAR RECEPTOR / TRANSCRIPTION FACTOR / GENE REGULATION / THIAZOLIDINEDIONE
Function / homology
Function and homology information


prostaglandin receptor activity / negative regulation of receptor signaling pathway via STAT / MECP2 regulates transcription factors / negative regulation of vascular endothelial cell proliferation / negative regulation of extracellular matrix assembly / negative regulation of connective tissue replacement involved in inflammatory response wound healing / positive regulation of cholesterol transport / negative regulation of cellular response to transforming growth factor beta stimulus / : / arachidonate binding ...prostaglandin receptor activity / negative regulation of receptor signaling pathway via STAT / MECP2 regulates transcription factors / negative regulation of vascular endothelial cell proliferation / negative regulation of extracellular matrix assembly / negative regulation of connective tissue replacement involved in inflammatory response wound healing / positive regulation of cholesterol transport / negative regulation of cellular response to transforming growth factor beta stimulus / : / arachidonate binding / positive regulation of adiponectin secretion / negative regulation of cardiac muscle hypertrophy in response to stress / DNA binding domain binding / lipoprotein transport / positive regulation of vascular associated smooth muscle cell apoptotic process / WW domain binding / STAT family protein binding / positive regulation of fatty acid metabolic process / response to lipid / negative regulation of SMAD protein signal transduction / negative regulation of type II interferon-mediated signaling pathway / LBD domain binding / negative regulation of cholesterol storage / lipid homeostasis / E-box binding / alpha-actinin binding / negative regulation of vascular associated smooth muscle cell proliferation / R-SMAD binding / monocyte differentiation / negative regulation of blood vessel endothelial cell migration / white fat cell differentiation / negative regulation of macrophage derived foam cell differentiation / negative regulation of lipid storage / cellular response to low-density lipoprotein particle stimulus / negative regulation of BMP signaling pathway / positive regulation of cholesterol efflux / negative regulation of mitochondrial fission / cell fate commitment / negative regulation of osteoblast differentiation / positive regulation of fat cell differentiation / negative regulation of MAPK cascade / BMP signaling pathway / long-chain fatty acid transport / nuclear retinoid X receptor binding / Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 / retinoic acid receptor signaling pathway / cell maturation / intracellular receptor signaling pathway / positive regulation of adipose tissue development / hormone-mediated signaling pathway / peroxisome proliferator activated receptor signaling pathway / epithelial cell differentiation / regulation of cellular response to insulin stimulus / response to nutrient / peptide binding / negative regulation of miRNA transcription / negative regulation of angiogenesis / transcription coregulator binding / positive regulation of apoptotic signaling pathway / Regulation of PTEN gene transcription / fatty acid metabolic process / placenta development / SUMOylation of intracellular receptors / negative regulation of smooth muscle cell proliferation / negative regulation of transforming growth factor beta receptor signaling pathway / mRNA transcription by RNA polymerase II / PPARA activates gene expression / regulation of circadian rhythm / Nuclear Receptor transcription pathway / Transcriptional regulation of white adipocyte differentiation / positive regulation of miRNA transcription / regulation of blood pressure / lipid metabolic process / DNA-binding transcription repressor activity, RNA polymerase II-specific / negative regulation of inflammatory response / RNA polymerase II transcription regulator complex / cellular response to insulin stimulus / nuclear receptor activity / rhythmic process / glucose homeostasis / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / DNA-binding transcription activator activity, RNA polymerase II-specific / double-stranded DNA binding / DNA-binding transcription factor binding / cellular response to hypoxia / sequence-specific DNA binding / nucleic acid binding / cell differentiation / DNA-binding transcription factor activity, RNA polymerase II-specific / receptor complex / transcription cis-regulatory region binding / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / innate immune response / negative regulation of gene expression / negative regulation of DNA-templated transcription / intracellular membrane-bounded organelle / chromatin binding / positive regulation of gene expression / regulation of transcription by RNA polymerase II
Similarity search - Function
Peroxisome proliferator-activated receptor gamma / Peroxisome proliferator-activated receptor gamma, N-terminal / PPAR gamma N-terminal region / Peroxisome proliferator-activated receptor / : / Retinoid X Receptor / Retinoid X Receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type ...Peroxisome proliferator-activated receptor gamma / Peroxisome proliferator-activated receptor gamma, N-terminal / PPAR gamma N-terminal region / Peroxisome proliferator-activated receptor / : / Retinoid X Receptor / Retinoid X Receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Double treble clef zinc finger, C4 type / 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-P1B / Peroxisome proliferator-activated receptor gamma
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.02 Å
AuthorsMueller, J.J. / Schupp, M. / Unger, T. / Kintscher, U. / Heinemann, U.
CitationJournal: To be Published
Title: Binding Diversity of Pioglitazone by Peroxisome Proliferator-Activated Receptor-Gamma
Authors: Mueller, J.J. / Schupp, M. / Unger, T. / Kintscher, U. / Heinemann, U.
History
DepositionJul 14, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 10, 2011Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.2May 8, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.temp
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA
B: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,9486
Polymers62,6432
Non-polymers1,3064
Water3,279182
1
A: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,0323
Polymers31,3211
Non-polymers7112
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9163
Polymers31,3211
Non-polymers5952
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)92.861, 60.411, 119.849
Angle α, β, γ (deg.)90.00, 103.01, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA / PPAR-GAMMA / NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3


Mass: 31321.393 Da / Num. of mol.: 2 / Fragment: LIGAND BINDING DOMAIN, RESIDUES 204-477
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET-28A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P37231
#2: Chemical ChemComp-P1B / (5R)-5-{4-[2-(5-ethylpyridin-2-yl)ethoxy]benzyl}-1,3-thiazolidine-2,4-dione / PIOGLITAZONE


Mass: 356.439 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H20N2O3S / Comment: medication*YM
#3: Chemical ChemComp-PE4 / 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL / POLYETHYLENE GLYCOL PEG4000


Mass: 354.436 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H34O8 / Comment: precipitant*YM
#4: Chemical ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES


Mass: 238.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18N2O4S / Comment: pH buffer*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 182 / 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: 2.61 Å3/Da / Density % sol: 52.93 % / Description: NONE
Crystal growTemperature: 292 K / Method: vapor diffusion / pH: 7.5
Details: PROTEIN CONC. 17MG/ML, 50 MM TRIS PH 8.0,0.1M NACL, 0.5 MM DTT, 2 MM EDTA. RESERVOIR: 20% PEG4000,10% ISOPROPANOL, 0.1M HEPES PH 7.5 , VAPOR DIFFUSION,TEMPERATURE 292K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.9184
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 18, 2005 / Details: MIRRORS
RadiationMonochromator: SI-111 CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9184 Å / Relative weight: 1
ReflectionResolution: 2.01→20 Å / Num. obs: 39168 / % possible obs: 97.2 % / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Biso Wilson estimate: 34.8 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 18.3
Reflection shellResolution: 2.01→2.08 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 2.5 / % possible all: 63.1

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
HKL-2000data reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1PRG

1prg


Resolution: 2.02→20 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.951 / SU B: 7.208 / SU ML: 0.099 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.154 / ESU R Free: 0.141 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.202 2104 5.1 %RANDOM
Rwork0.162 ---
obs0.164 39168 97.2 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 33.61 Å2
Baniso -1Baniso -2Baniso -3
1--0.82 Å20 Å20.09 Å2
2--2.2 Å20 Å2
3----1.34 Å2
Refinement stepCycle: LAST / Resolution: 2.02→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4145 0 78 182 4405
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0224336
X-RAY DIFFRACTIONr_bond_other_d0.0010.024081
X-RAY DIFFRACTIONr_angle_refined_deg1.362.0165837
X-RAY DIFFRACTIONr_angle_other_deg0.9393.0019521
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.1995516
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.68625.323186
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.5615825
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.2451516
X-RAY DIFFRACTIONr_chiral_restr0.1050.2670
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.024622
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02808
X-RAY DIFFRACTIONr_nbd_refined0.2170.2992
X-RAY DIFFRACTIONr_nbd_other0.1630.23971
X-RAY DIFFRACTIONr_nbtor_refined0.1810.22152
X-RAY DIFFRACTIONr_nbtor_other0.0850.22372
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1320.2180
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2050.224
X-RAY DIFFRACTIONr_symmetry_vdw_other0.1780.296
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1010.212
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it4.85632709
X-RAY DIFFRACTIONr_mcbond_other1.6631044
X-RAY DIFFRACTIONr_mcangle_it5.95944193
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it9.43261856
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it11.8381643
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.02→2.09 Å / Total num. of bins used: 15
RfactorNum. reflection% reflection
Rfree0.285 169 -
Rwork0.201 3067 -
obs--78.85 %
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)
114.1851-6.6667-2.995319.18424.735610.5676-0.04210.2265-1.26250.19490.1826-0.18280.760.2731-0.1406-0.01810.0294-0.01720.1096-0.05550.161839.4841-19.524735.8681
24.27150.1871-3.85330.91860.00267.6873-0.0406-0.29850.1273-0.0230.1072-0.0332-0.33150.4864-0.0666-0.0508-0.052-0.0155-0.0633-0.0363-0.058231.6167-4.198845.4891
39.96070.96733.61469.05132.85611.99670.1619-0.7933-0.90370.83050.0322-0.35490.8199-0.0523-0.19410.09520.01830.02710.1140.01620.035526.2268-5.319560.0089
428.3438-8.34950.285711.86831.09937.9076-0.1033-0.77431.7527-0.21830.0231-0.3921-0.8585-0.13630.08020.16450.05220.02360.0878-0.0439-0.01815.66558.263661.1357
549.01541.315332.710619.43161.939835.6562-0.7165-1.12232.0590.2979-0.3529-0.6421-2.8108-0.32181.06950.31330.04140.25180.2442-0.00070.358214.007116.508855.4847
624.4427-14.3412-17.10679.80179.39812.26670.3392-0.45060.8568-0.2750.2834-0.1495-0.8096-0.0992-0.62270.10270.0071-0.04040.088-0.02030.129518.44787.99942.1821
73.7052-0.1297-2.58040.9875-0.07586.69860.03030.29730.21-0.16230.04840.0888-0.2763-0.1783-0.0787-0.0114-0.0592-0.0286-0.0846-0.0164-0.026724.6888-2.926631.1351
85.0821-2.5650.06026.52680.20887.3946-0.1447-0.0227-0.0813-0.02120.17580.5879-0.2984-0.5814-0.03110.05030.01450.01570.02880.0037-0.027211.5692.398753.0404
913.1478-6.8797-0.872910.42742.3915.36810.06910.1624-0.4304-0.0587-0.27321.0875-0.1593-0.63710.2040.0133-0.09140.01730.077-0.04170.061412.6612-8.068547.2996
102.8552-0.49561.7223.1583-1.95559.927-0.04020.2788-0.1274-0.35530.11050.16390.2137-0.3467-0.0703-0.0341-0.0695-0.0089-0.0529-0.0618-0.01524.4212-10.094831.0303
112.0667-0.76862.16247.5273-7.69417.5448-0.0820.1458-0.3129-0.3251-0.0171-0.22560.69450.20450.0992-0.0695-0.01940.01-0.0698-0.07210.041529.4913-18.691734.4915
128.4676-11.26471.637719.2986-3.01530.7292-0.0399-0.0079-0.28990.02880.16960.7709-0.0981-0.2314-0.12970.0273-0.0504-0.01850.0114-0.01910.071811.4596-7.719237.9417
1324.6593-13.5595-6.740816.07335.60853.0903-0.8433-1.0548-0.5190.67350.7604-0.16210.70520.15990.08290.32440.0462-0.06920.07220.10210.106210.149614.667636.3045
149.23721.09171.970332.390612.652610.40440.24660.2349-0.1657-1.95660.05181.7363-0.724-1.5025-0.29840.2430.0622-0.04480.25480.12150.276313.46164.331828.912
1565.2446-10.714529.082358.3171-12.187948.40861.2366-1.0681-2.2443.61270.2569-3.59641.36771.6799-1.49350.24010.0933-0.34390.0772-0.12680.453320.5494-40.746738.8514
162.076-0.5452-0.30883.7393-2.9487.14240.17380.4257-0.3173-0.42780.02590.03750.70130.1012-0.19960.0913-0.0211-0.0285-0.0287-0.10280.02938.31-36.699122.0905
17184.501-21.52435.576343.709724.877815.98691.26661.2569-8.6051-0.4652-0.43840.84551.19790.3092-0.82820.57930.0199-0.00890.4688-0.02020.37535.4926-37.04925.5893
186.4234-0.4608-2.44980.36030.44312.9078-0.02730.5163-0.3220.0963-0.03820.460.1389-1.22640.06560.14650.01540.02260.34620.02660.0404-10.5124-23.75117.7685
193.9594-0.62511.58281.3246-0.38626.47230.0490.1844-0.0773-0.0501-0.0326-0.00140.1505-0.3112-0.0164-0.0345-0.09150.0129-0.09070.0032-0.0339-2.7366-31.164331.605
202.62710.7617-4.29811.9392-3.493914.61870.11550.12790.18360.15720.11430.133-0.6274-0.7543-0.2297-0.0572-0.0355-0.0044-0.0511-0.0258-0.0294-0.7824-24.508936.3889
215.3582-0.27913.67373.00630.798412.49120.19320.172-0.1295-0.0967-0.10570.10620.2292-0.4768-0.08750.0592-0.0180.02930.0639-0.0316-0.0332.5467-25.524214.0016
229.4891-4.40032.0884.62411.23466.4955-0.1045-0.11911.14250.59410.17560.1791-1.0655-0.4651-0.0710.39330.01530.09390.11810.07220.1886-2.7698-12.661612.13
235.564-2.19812.9139.8541-4.16979.1623-0.07790.37540.43670.08260.0002-0.2983-0.55990.25130.07770.0567-0.08010.05430.0223-0.0476-0.033911.9051-22.765119.5862
243.5877-0.9347-2.42662.49591.51835.13160.0669-0.32180.01250.11490.0392-0.0476-0.12840.183-0.1061-0.0537-0.0615-0.0215-0.0749-0.0254-0.04178.2594-26.856639.8866
259.6553-2.2609-8.7415.18792.455420.6719-0.0302-0.249-0.4477-0.03940.2297-0.47420.62641.3885-0.1995-0.03450.0118-0.03290.0077-0.07490.096420.0938-32.896432.5272
2618.4986-6.1451-0.69156.1610.38472.44460.35080.48770.8298-0.3917-0.15-0.3884-0.4057-0.0361-0.20080.0391-0.05920.0368-0.0132-0.03090.004916.1133-20.800927.9706
27103.1708-36.147233.91727.7728-15.848123.23180.8859-0.18831.8944-0.7224-0.61740.1613-0.4684-1.4124-0.26850.24460.23130.10.2645-0.00540.3042-5.1515-10.35425.3992
286.76745.7909-3.004111.9781-5.39212.46710.21610.35851.3430.307-0.1680.294-0.6139-0.4512-0.04810.8421-0.1840.24870.5034-0.00470.5581-17.3079-18.018726.4083
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A204 - 217
2X-RAY DIFFRACTION2A218 - 233
3X-RAY DIFFRACTION3A234 - 242
4X-RAY DIFFRACTION4A243 - 258
5X-RAY DIFFRACTION5A259 - 276
6X-RAY DIFFRACTION6A277 - 298
7X-RAY DIFFRACTION7A299 - 332
8X-RAY DIFFRACTION8A333 - 360
9X-RAY DIFFRACTION9A361 - 379
10X-RAY DIFFRACTION10A380 - 404
11X-RAY DIFFRACTION11A405 - 426
12X-RAY DIFFRACTION12A427 - 460
13X-RAY DIFFRACTION13A461 - 467
14X-RAY DIFFRACTION14A468 - 477
15X-RAY DIFFRACTION15B207 - 211
16X-RAY DIFFRACTION16B212 - 239
17X-RAY DIFFRACTION17B240 - 245
18X-RAY DIFFRACTION18B246 - 282
19X-RAY DIFFRACTION19B283 - 311
20X-RAY DIFFRACTION20B312 - 326
21X-RAY DIFFRACTION21B327 - 348
22X-RAY DIFFRACTION22B349 - 366
23X-RAY DIFFRACTION23B367 - 382
24X-RAY DIFFRACTION24B383 - 411
25X-RAY DIFFRACTION25B412 - 424
26X-RAY DIFFRACTION26B425 - 447
27X-RAY DIFFRACTION27B448 - 456
28X-RAY DIFFRACTION28B457 - 474

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