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

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Basic information

Entry
Database: PDB / ID: 5aqq
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 / protein carrier chaperone / clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane / Respiratory syncytial virus genome transcription / Lipophagy / 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 / protein carrier chaperone / clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane / Respiratory syncytial virus genome transcription / Lipophagy / GABA synthesis, release, reuptake and degradation / protein targeting to lysosome involved in chaperone-mediated autophagy / adenyl-nucleotide exchange factor activity / clathrin coat disassembly / C3HC4-type RING finger domain binding / positive regulation of smooth muscle cell apoptotic process / negative regulation of NLRP3 inflammasome complex assembly / CHL1 interactions / regulation of protein complex stability / ATP-dependent protein disaggregase activity / membrane organization / Prp19 complex / protein folding chaperone complex / Lysosome Vesicle Biogenesis / cellular response to steroid hormone stimulus / Golgi Associated Vesicle Biogenesis / chaperone-mediated autophagy / non-chaperonin molecular chaperone ATPase / chaperone cofactor-dependent protein refolding / Regulation of HSF1-mediated heat shock response / HSF1-dependent transactivation / response to unfolded protein / regulation of protein-containing complex assembly / Attenuation phase / Protein methylation / ATP metabolic process / heat shock protein binding / protein folding chaperone / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / mRNA Splicing - Major Pathway / lysosomal lumen / cellular response to starvation / AUF1 (hnRNP D0) binds and destabilizes mRNA / spliceosomal complex / G protein-coupled receptor binding / ATP-dependent protein folding chaperone / Late endosomal microautophagy / regulation of protein stability / PKR-mediated signaling / mRNA splicing, via spliceosome / 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 / secretory granule lumen / Interleukin-4 and Interleukin-13 signaling / 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 / ubiquitin protein ligase binding / Neutrophil degranulation / apoptotic process / 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 / Ubiquitin homologues / Nucleotidyltransferase; domain 5 / 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
7-methylquinazolin-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: 2.72 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 1.3Oct 23, 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)168,86616
Polymers167,7566
Non-polymers1,11010
Water1,04558
1
E: HEAT SHOCK COGNATE 71 KDA PROTEIN
F: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,1564
Polymers55,9192
Non-polymers2372
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2140 Å2
ΔGint4 kcal/mol
Surface area21760 Å2
MethodPISA
2
A: HEAT SHOCK COGNATE 71 KDA PROTEIN
B: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,4627
Polymers55,9192
Non-polymers5445
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3060 Å2
ΔGint8.7 kcal/mol
Surface area21750 Å2
MethodPISA
3
C: HEAT SHOCK COGNATE 71 KDA PROTEIN
D: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,2485
Polymers55,9192
Non-polymers3293
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2610 Å2
ΔGint5.3 kcal/mol
Surface area21850 Å2
MethodPISA
Unit cell
Length a, b, c (Å)233.433, 41.332, 205.513
Angle α, β, γ (deg.)90.00, 123.75, 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, 68 molecules

#3: Chemical ChemComp-BBW / 7-methylquinazolin-4-amine


Mass: 159.188 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C9H9N3
#4: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 58 / 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: 49.94 % / 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: 2.72→47.86 Å / Num. obs: 44876 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Biso Wilson estimate: 44.84 Å2 / Rmerge(I) obs: 0.25 / Net I/σ(I): 2.8
Reflection shellResolution: 2.72→2.82 Å / Redundancy: 3.1 % / Rmerge(I) obs: 1.34 / Mean I/σ(I) obs: 1 / % possible all: 99

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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: 2.72→47.86 Å / Cor.coef. Fo:Fc: 0.8796 / Cor.coef. Fo:Fc free: 0.8485 / SU R Cruickshank DPI: 3.306 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 1.78 / SU Rfree Blow DPI: 0.318 / SU Rfree Cruickshank DPI: 0.326
RfactorNum. reflection% reflectionSelection details
Rfree0.2409 2204 4.91 %RANDOM
Rwork0.1952 ---
obs0.1974 44875 99.68 %-
Displacement parametersBiso mean: 57.59 Å2
Baniso -1Baniso -2Baniso -3
1-2.7061 Å20 Å2-24.2271 Å2
2--6.4189 Å20 Å2
3----9.125 Å2
Refine analyzeLuzzati coordinate error obs: 0.368 Å
Refinement stepCycle: LAST / Resolution: 2.72→47.86 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11004 0 74 58 11136
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0111238HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.1115208HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d3912SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes302HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1690HARMONIC5
X-RAY DIFFRACTIONt_it11238HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion2.6
X-RAY DIFFRACTIONt_other_torsion18.57
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion1562SEMIHARMONIC5
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_contact12682SEMIHARMONIC4
LS refinement shellResolution: 2.72→2.79 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.268 149 4.57 %
Rwork0.2444 3108 -
all0.2455 3257 -
obs--98.61 %
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)
12.51110.757-0.99254.36510.16452.72720.1072-0.1850.15780.492-0.14170.1727-0.15220.27970.0345-0.2371-0.0367-0.04030.14140.0957-0.2275393.9504-5.9302164.3019
23.08680.4581-0.46691.183-0.03041.2187-0.00720.480.3235-0.28820.0270.1463-0.0028-0.0587-0.0198-0.148-0.0403-0.07140.17750.1239-0.2232382.2149-3.5074144.725
32.19421.3885-0.10611.49430.04621.56030.2293-0.1755-0.2148-0.00820.02790.31280.09540.0065-0.2572-0.14730.0948-0.12420.16370.1011-0.0596363.9257-26.4932166.5872
41.1918-0.79170.6620.915-0.77535.8838-0.0067-0.24860.05430.22820.06640.036-0.0416-0.0307-0.0597-0.2194-0.02780.00610.25770.02360.0035366.3556-15.847171.1493
53.3015-1.28240.6450-1.17981.805-0.0375-0.330.0487-0.06110.11220.2499-0.0148-0.0392-0.0746-0.2295-0.0862-0.0060.21810.0302-0.0088358.7254-16.8803167.802
64.726-1.2105-1.4515.6798-0.32614.5068-0.11160.0322-0.094-0.11660.0710.03180.311-0.0250.0406-0.17360.15630.10730.30070.0396-0.2134397.18390.643206.9039
72.5689-0.7525-1.02873.2957-0.12782.8693-0.1172-0.5230.06790.60120.16960.07980.00710.2929-0.0524-0.14150.13280.05390.2630.0749-0.3037389.949713.2275219.0321
80.74550.3763-0.09643.1519-0.73590.25220.0495-0.30590.07490.0836-0.0366-0.3242-0.03810.2487-0.013-0.21740.15530.01040.30120.0412-0.2416401.688714.2209208.1556
92.50130.37751.50042.76891.19193.78670.0155-0.01430.0165-0.20710.0487-0.06990.01910.0899-0.0641-0.10360.08670.13340.29470.1437-0.167395.33813.2904189.2029
102.72161.77010.74231.48380.01731.514-0.070.08030.07120.0245-0.0166-0.03080.03640.15620.0866-0.08060.14030.08820.30060.0447-0.2081393.193420.6488196.0861
11-1.8288-0.4533-0.1180.79250.10314.47240.02910.038-0.0711-0.05770.08590.06070.1225-0.2277-0.1149-0.13760.09410.11580.12670.132-0.0476361.807315.178205.5298
12-0.10290.97460.44490.6925-2.84913.9068-0.2360.07020.13090.12080.2210.4238-0.0136-0.06660.015-0.12770.04860.1430.22450.05-0.0747362.55377.6997209.4472
132.2573-0.4007-2.58930.0001-1.15173.719-0.01130.30180.0312-0.2082-0.12390.2370.0232-0.19090.1352-0.16130.07550.05710.21180.1606-0.148378.443217.664192.7227
145.4025-0.4044-1.55352.26240.10792.8914-0.05570.0536-0.1723-0.01350.01920.02380.3105-0.11430.0365-0.06980.0930.06120.12570.0653-0.179389.05029.4701192.6032
151.81450.8897-0.45080.44240.2852-0.35140.1042-0.1199-0.21890.2992-0.00120.10720.0594-0.0343-0.103-0.0070.0930.11350.09570.1343-0.1327363.6123-9.1449223.5927
162.8927-1.0087-0.59930.2974-2.62070.01850.0785-0.0298-0.0290.2505-0.2115-0.1897-0.1528-0.06350.133-0.06590.09450.11370.10960.1321-0.0792369.55433.2192229.5242
172.5082-2.4292-0.19420.3987-1.1373.1467-0.1699-0.2012-0.03140.12160.20110.19820.0907-0.1841-0.0312-0.15950.05830.16320.16670.1863-0.1104358.5637-1.5441220.7105
186.5051.1512-1.55054.48232.40741.489-0.19730.0043-0.1024-0.111-0.15630.45410.15120.09070.3536-0.3439-0.0231-0.09220.2354-0.15710.0615313.26610.5454241.5747
192.0508-1.3717-1.85492.8402-0.53954.62560.0935-0.00710.2286-0.44870.06680.1386-0.06190.1433-0.1603-0.3137-0.0129-0.11510.149-0.17520.0771319.586817.7009232.108
204.8828-0.2266-1.8940.20670.72240.37990.12350.15550.0087-0.08820.06080.59440.0583-0.5507-0.1843-0.3137-0.004-0.13740.1362-0.18550.1292306.94089.4776240.139
211.24020.72950.82661.10050.40791.70330.1251-0.1699-0.05180.3147-0.31220.50870.2251-0.47570.1871-0.3017-0.04190.13810.2625-0.2108-0.0871321.475515.6549256.286
226.60160.41491.12946.38592.38694.59050.0885-0.0688-0.01790.1673-0.0759-0.177-0.05680.0252-0.0126-0.21250.0722-0.07260.224-0.1128-0.2575342.85016.9843246.031
234.7406-0.7648-2.85940.46922.96623.02860.1092-0.4030.22220.3409-0.28710.4694-0.01540.31860.178-0.2169-0.04190.18470.3-0.2108-0.0955326.060916.2434261.1754
245.4241-1.8438-1.90783.0930.59770.70420.1231-0.1777-0.09090.2463-0.03740.5791-0.10570.265-0.0857-0.2413-0.08310.19390.2595-0.1492-0.0729315.07188.2483260.9956
251.5606-0.45731.5682.8484-2.06371.77280.00310.1307-0.0465-0.22140.2989-0.26720.1230.0335-0.302-0.1133-0.0774-0.02130.304-0.0803-0.2372342.59-10.0699232.5715
261.95521.59860.79831.8295-0.73644.5343-0.19790.19670.3327-0.23020.263-0.28840.01-0.0194-0.0652-0.205-0.01490.02320.2736-0.0729-0.1578343.3838-0.1991231.614
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{A|1 - 182}
2X-RAY DIFFRACTION2{A|183 - 381}
3X-RAY DIFFRACTION3{B|150 - 185}
4X-RAY DIFFRACTION4{B|186 - 230}
5X-RAY DIFFRACTION5{B|231 - 260}
6X-RAY DIFFRACTION6{C|0 - 28}
7X-RAY DIFFRACTION7{C|29 - 151}
8X-RAY DIFFRACTION8{C|152 - 182}
9X-RAY DIFFRACTION9{C|183 - 201}
10X-RAY DIFFRACTION10{C|202 - 229}
11X-RAY DIFFRACTION11{C|230 - 249}
12X-RAY DIFFRACTION12{C|250 - 292}
13X-RAY DIFFRACTION13{C|293 - 343}
14X-RAY DIFFRACTION14{C|344 - 381}
15X-RAY DIFFRACTION15{D|150 - 188}
16X-RAY DIFFRACTION16{D|189 - 223}
17X-RAY DIFFRACTION17{D|224 - 261}
18X-RAY DIFFRACTION18{E|1 - 48}
19X-RAY DIFFRACTION19{E|49 - 109}
20X-RAY DIFFRACTION20{E|110 - 182}
21X-RAY DIFFRACTION21{E|183 - 249}
22X-RAY DIFFRACTION22{E|250 - 292}
23X-RAY DIFFRACTION23{E|293 - 343}
24X-RAY DIFFRACTION24{E|344 - 381}
25X-RAY DIFFRACTION25{F|150 - 186}
26X-RAY DIFFRACTION26{F|187 - 261}

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