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- PDB-5aqp: Fragment-based screening of HSP70 sheds light on the functional r... -

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Basic information

Entry
Database: PDB / ID: 5aqp
TitleFragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues
Components
  • BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
  • HEAT SHOCK COGNATE 71 KDA PROTEIN
KeywordsCHAPERONE / HEAT SHOCK PROTEIN / HSP70 / HSP72 / HSC70 / ATPASE / BAG1 / FRAGMENT
Function / homology
Function and homology information


lumenal side of lysosomal membrane / regulation of protein import / negative regulation of supramolecular fiber organization / chaperone-mediated autophagy translocation complex disassembly / clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane / Lipophagy / Respiratory syncytial virus genome transcription / protein carrier chaperone / GABA synthesis, release, reuptake and degradation / protein targeting to lysosome involved in chaperone-mediated autophagy ...lumenal side of lysosomal membrane / regulation of protein import / negative regulation of supramolecular fiber organization / chaperone-mediated autophagy translocation complex disassembly / clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane / Lipophagy / Respiratory syncytial virus genome transcription / protein carrier chaperone / GABA synthesis, release, reuptake and degradation / protein targeting to lysosome involved in chaperone-mediated autophagy / adenyl-nucleotide exchange factor activity / positive regulation of smooth muscle cell apoptotic process / clathrin coat disassembly / C3HC4-type RING finger domain binding / CHL1 interactions / negative regulation of NLRP3 inflammasome complex assembly / regulation of protein complex stability / ATP-dependent protein disaggregase activity / membrane organization / protein folding chaperone complex / Lysosome Vesicle Biogenesis / cellular response to steroid hormone stimulus / chaperone-mediated autophagy / Golgi Associated Vesicle Biogenesis / non-chaperonin molecular chaperone ATPase / : / Prp19 complex / Regulation of HSF1-mediated heat shock response / HSF1-dependent transactivation / response to unfolded protein / regulation of protein-containing complex assembly / Attenuation phase / ATP metabolic process / Protein methylation / heat shock protein binding / protein folding chaperone / mRNA Splicing - Major Pathway / lysosomal lumen / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / cellular response to starvation / AUF1 (hnRNP D0) binds and destabilizes mRNA / spliceosomal complex / ATP-dependent protein folding chaperone / G protein-coupled receptor binding / Late endosomal microautophagy / regulation of protein stability / mRNA splicing, via spliceosome / PKR-mediated signaling / Chaperone Mediated Autophagy / MHC class II protein complex binding / unfolded protein binding / melanosome / protein folding / Clathrin-mediated endocytosis / protein-folding chaperone binding / protein refolding / protein-macromolecule adaptor activity / Interleukin-4 and Interleukin-13 signaling / secretory granule lumen / blood microparticle / ficolin-1-rich granule lumen / cell surface receptor signaling pathway / protein stabilization / positive regulation of cell migration / cadherin binding / receptor ligand activity / ribonucleoprotein complex / lysosomal membrane / focal adhesion / negative regulation of DNA-templated transcription / apoptotic process / ubiquitin protein ligase binding / Neutrophil degranulation / negative regulation of apoptotic process / nucleolus / enzyme binding / ATP hydrolysis activity / extracellular space / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / nucleus / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
BAG domain / Molecular chaperone regulator BAG / BAG domain superfamily / BAG domain / BAG domain / BAG domain profile. / BAG domains, present in regulator of Hsp70 proteins / Defensin A-like - #30 / Defensin A-like / Heat shock hsp70 proteins family signature 2. ...BAG domain / Molecular chaperone regulator BAG / BAG domain superfamily / BAG domain / BAG domain / BAG domain profile. / BAG domains, present in regulator of Hsp70 proteins / Defensin A-like - #30 / Defensin A-like / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. / Heat shock protein 70, conserved site / Heat shock protein 70kD, peptide-binding domain superfamily / Heat shock protein 70 family / Hsp70 protein / Heat shock protein 70kD, C-terminal domain superfamily / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / ATPase, nucleotide binding domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / ATPase, nucleotide binding domain / Ubiquitin family / Nucleotidyltransferase; domain 5 / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Alpha-Beta Complex / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
quinazolin-4-amine / Heat shock cognate 71 kDa protein / BAG family molecular chaperone regulator 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.08 Å
AuthorsJones, A.M. / Westwood, I.M. / Osborne, J.D. / Matthews, T.P. / Cheeseman, M.D. / Rowlands, M.G. / Jeganathan, F. / Burke, R. / Lee, D. / Kadi, N. ...Jones, A.M. / Westwood, I.M. / Osborne, J.D. / Matthews, T.P. / Cheeseman, M.D. / Rowlands, M.G. / Jeganathan, F. / Burke, R. / Lee, D. / Kadi, N. / Liu, M. / Richards, M. / McAndrew, C. / Yahya, N. / Dobson, S.E. / Jones, K. / Workman, P. / Collins, I. / van Montfort, R.L.M.
CitationJournal: Sci Rep / Year: 2016
Title: A fragment-based approach applied to a highly flexible target: Insights and challenges towards the inhibition of HSP70 isoforms.
Authors: Jones, A.M. / Westwood, I.M. / Osborne, J.D. / Matthews, T.P. / Cheeseman, M.D. / Rowlands, M.G. / Jeganathan, F. / Burke, R. / Lee, D. / Kadi, N. / Liu, M. / Richards, M. / McAndrew, C. / ...Authors: Jones, A.M. / Westwood, I.M. / Osborne, J.D. / Matthews, T.P. / Cheeseman, M.D. / Rowlands, M.G. / Jeganathan, F. / Burke, R. / Lee, D. / Kadi, N. / Liu, M. / Richards, M. / McAndrew, C. / Yahya, N. / Dobson, S.E. / Jones, K. / Workman, P. / Collins, I. / van Montfort, R.L.
History
DepositionSep 22, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 5, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 13, 2017Group: Data collection / Database references / Category: citation / citation_author / diffrn_detector
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name / _diffrn_detector.type
Revision 1.2Jan 10, 2024Group: 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
Revision 1.3Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HEAT SHOCK COGNATE 71 KDA PROTEIN
B: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
C: HEAT SHOCK COGNATE 71 KDA PROTEIN
D: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
E: HEAT SHOCK COGNATE 71 KDA PROTEIN
F: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)170,11530
Polymers167,7566
Non-polymers2,36024
Water10,593588
1
C: HEAT SHOCK COGNATE 71 KDA PROTEIN
D: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,07914
Polymers55,9192
Non-polymers1,16012
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4680 Å2
ΔGint4.6 kcal/mol
Surface area21850 Å2
MethodPISA
2
E: HEAT SHOCK COGNATE 71 KDA PROTEIN
F: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,5108
Polymers55,9192
Non-polymers5926
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2960 Å2
ΔGint-0.5 kcal/mol
Surface area21960 Å2
MethodPISA
3
A: HEAT SHOCK COGNATE 71 KDA PROTEIN
B: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,5268
Polymers55,9192
Non-polymers6086
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3260 Å2
ΔGint11.7 kcal/mol
Surface area22020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)232.951, 40.980, 206.421
Angle α, β, γ (deg.)90.00, 123.19, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein , 2 types, 6 molecules ACEBDF

#1: Protein HEAT SHOCK COGNATE 71 KDA PROTEIN / HEAT SHOCK 70 KDA PROTEIN 8 / LIPOPOLYSACCHARIDE-ASSOCIATED PROTEIN 1 / LAP-1 / LPS-ASSOCIATED PROTEIN 1


Mass: 42406.980 Da / Num. of mol.: 3 / Fragment: NUCLEOTIDE BINDING DOMAIN, UNP RESIDUES 1-381
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX-6P-1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): AI / References: UniProt: P11142, EC: 3.6.3.51
#2: Protein BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1 / BAG-1 / BCL-2-ASSOCIATED ATHANOGENE 1


Mass: 13511.571 Da / Num. of mol.: 3 / Fragment: UNP RESIDUES 222-334
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX-6P-1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): AI / References: UniProt: Q99933

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Non-polymers , 5 types, 612 molecules

#3: Chemical ChemComp-1LQ / quinazolin-4-amine


Mass: 145.161 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C8H7N3
#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#6: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 588 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 2.46 Å3/Da / Density % sol: 49.95 % / Description: NONE
Crystal growpH: 8.5
Details: 16-26% (W/V) PEG3350, 0.1 M K-NA TARTRATE, 0.1 M TRIS.HCL PH 8.5 AND 25% (V/V) GLYCEROL

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.9686
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 29, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9686 Å / Relative weight: 1
ReflectionResolution: 2.08→48.74 Å / Num. obs: 90334 / % possible obs: 90.7 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 35.53 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 6.2
Reflection shellResolution: 2.08→2.12 Å / Redundancy: 1.9 % / Rmerge(I) obs: 1.28 / Mean I/σ(I) obs: 0.8 / % possible all: 53.9

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Processing

Software
NameVersionClassification
BUSTER2.10.2refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1HX1

1hx1


Resolution: 2.08→48.74 Å / Cor.coef. Fo:Fc: 0.9409 / Cor.coef. Fo:Fc free: 0.9268 / SU R Cruickshank DPI: 0.206 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.209 / SU Rfree Blow DPI: 0.163 / SU Rfree Cruickshank DPI: 0.163
RfactorNum. reflection% reflectionSelection details
Rfree0.209 4510 4.99 %RANDOM
Rwork0.1813 ---
obs0.1826 90330 90.69 %-
Displacement parametersBiso mean: 51.25 Å2
Baniso -1Baniso -2Baniso -3
1--6.4589 Å20 Å2-7.1783 Å2
2--9.5885 Å20 Å2
3----3.1296 Å2
Refine analyzeLuzzati coordinate error obs: 0.281 Å
Refinement stepCycle: LAST / Resolution: 2.08→48.74 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11202 0 153 588 11943
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0111514HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.0515559HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d4032SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes318HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1710HARMONIC5
X-RAY DIFFRACTIONt_it11514HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion2.88
X-RAY DIFFRACTIONt_other_torsion16.21
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion1574SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies1HARMONIC1
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact13526SEMIHARMONIC4
LS refinement shellResolution: 2.08→2.13 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2435 204 5.11 %
Rwork0.2147 3792 -
all0.2161 3996 -
obs--54.79 %
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)
11.2092-0.1863-0.512.4609-0.53311.55170.0688-0.1302-0.05010.1833-0.0945-0.0522-0.0380.04270.02570.03380.11440.1621-0.11910.1028-0.0499215.380415.0528133.1723
21.9254-0.7024-0.1581.1373-0.01191.34960.2044-0.00220.2301-0.0377-0.1042-0.3502-0.05170.1612-0.10020.04630.10390.2261-0.12210.11870.011221.071120.128115.063
31.645-0.2748-0.62440.8081-0.18170.74950.01740.25590.0385-0.1737-0.0186-0.06630.1209-0.13720.00120.13230.11930.131-0.07990.0952-0.1114198.143416.4909115.3137
41.55051.56052.19451.02762.1785.98420.1475-0.4679-0.24550.1595-0.1915-0.09880.04670.10940.0440.08590.08110.07520.00290.1536-0.116188.6802-3.6507143.4045
51.08110.11.85391.4562-0.1063.66-0.1934-0.3113-0.09470.2609-0.06190.0805-0.1065-0.18450.25540.06130.11430.1022-0.03020.1029-0.127187.55694.6151140.8087
64.4701-0.5765-2.62334.96540.25232.9119-0.02930.1651-0.3052-0.3981-0.1602-0.05180.2059-0.05450.1895-0.0354-0.04790.0771-0.10440.0069-0.0177218.426-12.378172.3744
70.9720.0381-0.26174.29640.30811.24870.0549-0.11020.06910.2865-0.15460.1756-0.08790.02980.0997-0.0111-0.08430.0595-0.0888-0.0015-0.019214.20131.164983.5388
82.2093-0.236-2.09882.04390.18511.53930.0162-0.22470.1858-0.069-0.1223-0.4317-0.1830.29050.1060.008-0.13110.0779-0.04660.03350.0667226.91470.521273.1164
94.53211.4874-0.39052.17870.68011.4322-0.12810.12560.0908-0.49260.1657-0.2411-0.09380.2023-0.03760.1432-0.08690.1231-0.07650.065-0.1009221.64513.793657.3788
102.1587-0.029-1.54620.6633-0.29072.48980.0282-0.1808-0.0529-0.11350.03270.23920.0971-0.1253-0.06090.154-0.0218-0.1391-0.13270.015-0.018187.70752.457765.1498
112.2512-0.2058-2.25012.0223-0.62134.4761-0.09550.03890.0745-0.18490.1090.11340.02630.0845-0.01350.0145-0.072-0.0898-0.10160.0298-0.0375190.5264-3.1870.2209
123.73481.3651-1.7131.7365-0.58351.7904-0.19220.44440.167-0.59130.15630.1054-0.0483-0.1680.03590.1502-0.0483-0.0572-0.1160.0447-0.1315200.68371.470257.6815
131.9349-0.39791.04312.2764-0.70682.0848-0.1550.4257-0.0386-0.52510.0789-0.1915-0.1530.11250.0760.1829-0.11560.145-0.08480.0067-0.1189216.2859-3.726855.8843
140.9291.04321.5651.86413.25215.88930.0813-0.1165-0.19640.02290.10630.02760.1670.0233-0.18760.01870.0078-0.061-0.11760.07640.027187.3164-21.379883.5659
151.0623-0.1497-0.3452.6915-0.19756.1912-0.0064-0.3122-0.13750.39880.04570.0341-0.05120.1306-0.0394-0.0807-0.0047-0.0240.01940.07530.0006191.4057-9.376393.3223
161.96050.58891.26981.94091.15336.3254-0.0913-0.1261-0.0768-0.23110.02550.28830.0261-0.14570.0658-0.0526-0.0229-0.0656-0.10690.04640.0306182.2892-14.376479.1891
174.2447-0.1265-1.80562.92770.18133.4341-0.1508-0.2223-0.15860.2017-0.15730.11630.2823-0.05090.308-0.1414-0.04330.0034-0.1537-0.20990.1874136.34063.4568161.2938
184.8412-1.5132-0.74416.80220.40741.40990.09780.29760.4165-0.1447-0.12410.0499-0.17280.26770.0262-0.08820.0389-0.0711-0.0554-0.15620.08144.94818.897149.4068
191.1152.59732.9133.3323-1.77884.92040.08020.18130.1115-0.1366-0.0568-0.0097-0.13940.1013-0.0233-0.03080.092-0.0987-0.1536-0.12140.0479142.13323.3187143.3013
203.3902-0.6478-1.83251.28510.41870.93960.19970.15320.1481-0.0502-0.0740.6175-0.1416-0.4217-0.1256-0.1652-0.0022-0.0591-0.1596-0.1830.2183131.166513.1484156.3507
212.9819-0.47980.08084.28431.81580.0841-0.0393-0.28030.22660.05190.02270.157-0.0625-0.34790.0166-0.168-0.0440.15250.1406-0.21040.0304134.318520.0398176.1751
222.78661.5967-1.12712.21791.88961.10.1604-0.22920.13740.0215-0.36720.2831-0.1411-0.05720.20680.02120.0423-0.0531-0.0009-0.0732-0.1052166.029814.9335163.5431
234.0496-1.0174-2.15762.10851.68832.65660.1029-0.73210.3530.3332-0.22790.4390.09850.12490.125-0.0704-0.05220.08980.0099-0.1979-0.1267155.36916.69174.4152
247.0184-0.6692-0.95173.23011.3751.49770.0737-0.4701-0.09680.2440.06790.5893-0.07070.2392-0.1416-0.1445-0.05510.22430.081-0.1934-0.0686139.987612.126177.6306
250.4977-0.51580.47562.3096-3.16516.08030.0310.05170.09320.06850.06730.03980.0632-0.0196-0.09830.024-0.0064-0.03790.0154-0.0096-0.0961167.364-6.0563148.7892
260.583-0.25920.30811.5815-0.40923.7926-0.0157-0.02730.1875-0.04360.05550.0576-0.169-0.1894-0.0399-0.02580.0148-0.03880.0357-0.0145-0.0421163.90644.9619143.9803
271.89321.6079-1.08313.0232-1.19792.4994-0.02320.38710.1359-0.00690.1081-0.13320.01350.0021-0.0849-0.02860.0393-0.02610.0356-0.0332-0.0946171.88022.886148.3299
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{A|0 - 151}
2X-RAY DIFFRACTION2{A|152 - 229}
3X-RAY DIFFRACTION3{A|230 - 381}
4X-RAY DIFFRACTION4{B|150 - 192}
5X-RAY DIFFRACTION5{B|193 - 259}
6X-RAY DIFFRACTION6{C|1 - 41}
7X-RAY DIFFRACTION7{C|42 - 151}
8X-RAY DIFFRACTION8{C|152 - 182}
9X-RAY DIFFRACTION9{C|183 - 229}
10X-RAY DIFFRACTION10{C|230 - 249}
11X-RAY DIFFRACTION11{C|250 - 275}
12X-RAY DIFFRACTION12{C|276 - 343}
13X-RAY DIFFRACTION13{C|344 - 381}
14X-RAY DIFFRACTION14{D|150 - 187}
15X-RAY DIFFRACTION15{D|188 - 223}
16X-RAY DIFFRACTION16{D|224 - 259}
17X-RAY DIFFRACTION17{E|1 - 41}
18X-RAY DIFFRACTION18{E|42 - 89}
19X-RAY DIFFRACTION19{E|90 - 109}
20X-RAY DIFFRACTION20{E|110 - 182}
21X-RAY DIFFRACTION21{E|183 - 229}
22X-RAY DIFFRACTION22{E|230 - 275}
23X-RAY DIFFRACTION23{E|276 - 343}
24X-RAY DIFFRACTION24{E|344 - 381}
25X-RAY DIFFRACTION25{F|148 - 187}
26X-RAY DIFFRACTION26{F|188 - 230}
27X-RAY DIFFRACTION27{F|231 - 259}

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