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- PDB-3qhe: Crystal structure of the complex between the armadillo repeat dom... -

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Basic information

Entry
Database: PDB / ID: 3qhe
TitleCrystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68
Components
  • Adenomatous polyposis coli protein
  • KH domain-containing, RNA-binding, signal transduction-associated protein 1
Keywordssignaling protein/splicing / Armadillo repeat superhelix / Regulation of Wnt signaling / tumor suppressor protein / adaptor protein / RNA-binding protein / signaling protein-splicing protein complex / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI / signaling protein-splicing complex
Function / homology
Function and homology information


regulation of RNA export from nucleus / Grb2-Sos complex / APC truncation mutants are not K63 polyubiquitinated / PTK6 Regulates Proteins Involved in RNA Processing / positive regulation of RNA export from nucleus / regulation of microtubule-based movement / negative regulation of cell cycle G1/S phase transition / gamma-catenin binding / regulation of attachment of spindle microtubules to kinetochore / positive regulation of pseudopodium assembly ...regulation of RNA export from nucleus / Grb2-Sos complex / APC truncation mutants are not K63 polyubiquitinated / PTK6 Regulates Proteins Involved in RNA Processing / positive regulation of RNA export from nucleus / regulation of microtubule-based movement / negative regulation of cell cycle G1/S phase transition / gamma-catenin binding / regulation of attachment of spindle microtubules to kinetochore / positive regulation of pseudopodium assembly / negative regulation of cyclin-dependent protein serine/threonine kinase activity / positive regulation of protein localization to centrosome / bicellular tight junction assembly / pattern specification process / negative regulation of microtubule depolymerization / catenin complex / beta-catenin destruction complex / APC truncation mutants have impaired AXIN binding / AXIN missense mutants destabilize the destruction complex / Truncations of AMER1 destabilize the destruction complex / heart valve development / regulation of microtubule-based process / microtubule plus-end binding / poly(A) binding / Beta-catenin phosphorylation cascade / Signaling by GSK3beta mutants / CTNNB1 S33 mutants aren't phosphorylated / CTNNB1 S37 mutants aren't phosphorylated / CTNNB1 S45 mutants aren't phosphorylated / CTNNB1 T41 mutants aren't phosphorylated / protein kinase regulator activity / Wnt signalosome / Disassembly of the destruction complex and recruitment of AXIN to the membrane / cell fate specification / poly(U) RNA binding / endocardial cushion morphogenesis / regulation of alternative mRNA splicing, via spliceosome / molecular function inhibitor activity / negative regulation of G1/S transition of mitotic cell cycle / mitotic spindle assembly checkpoint signaling / Apoptotic cleavage of cellular proteins / dynein complex binding / regulation of RNA splicing / mitotic cytokinesis / positive regulation of translational initiation / bicellular tight junction / lateral plasma membrane / signaling adaptor activity / SH2 domain binding / protein tyrosine kinase binding / adherens junction / Deactivation of the beta-catenin transactivating complex / negative regulation of canonical Wnt signaling pathway / beta-catenin binding / Degradation of beta-catenin by the destruction complex / kinetochore / SH3 domain binding / Wnt signaling pathway / G1/S transition of mitotic cell cycle / ruffle membrane / mRNA processing / positive regulation of protein catabolic process / G2/M transition of mitotic cell cycle / Ovarian tumor domain proteases / insulin receptor signaling pathway / cell migration / nervous system development / lamellipodium / T cell receptor signaling pathway / positive regulation of cold-induced thermogenesis / protein-containing complex assembly / microtubule binding / regulation of apoptotic process / spermatogenesis / microtubule / proteasome-mediated ubiquitin-dependent protein catabolic process / regulation of cell cycle / cell adhesion / positive regulation of cell migration / positive regulation of apoptotic process / protein domain specific binding / negative regulation of cell population proliferation / negative regulation of DNA-templated transcription / mRNA binding / centrosome / ubiquitin protein ligase binding / DNA damage response / protein-containing complex binding / protein kinase binding / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / Golgi apparatus / protein-containing complex / DNA binding / RNA binding / nucleoplasm / identical protein binding / nucleus / membrane / plasma membrane
Similarity search - Function
Sam68, tyrosine-rich domain / KHDRBS, Qua1 domain / Qua1 domain / Tyrosine-rich domain of Sam68 / Adenomatous polyposis coli protein repeat / SAMP / EB-1 binding / Adenomatous polyposis coli protein basic domain / Adenomatous polyposis coli protein, 15 residue repeat / Adenomatous polyposis coli (APC) family ...Sam68, tyrosine-rich domain / KHDRBS, Qua1 domain / Qua1 domain / Tyrosine-rich domain of Sam68 / Adenomatous polyposis coli protein repeat / SAMP / EB-1 binding / Adenomatous polyposis coli protein basic domain / Adenomatous polyposis coli protein, 15 residue repeat / Adenomatous polyposis coli (APC) family / Adenomatous polyposis coli protein / Adenomatous polyposis coli, N-terminal dimerisation domain / APC, N-terminal coiled-coil domain superfamily / Adenomatous polyposis coli (APC) repeat / APC repeat / SAMP Motif / EB-1 Binding Domain / APC basic domain / APC 15 residue motif / Adenomatous polyposis coli tumour suppressor protein / Armadillo-associated region on APC / Unstructured region on APC between 1st and 2nd catenin-bdg motifs / Unstructured region on APC between 1st two creatine-rich regions / Unstructured region on APC between APC_crr and SAMP / Unstructured region on APC between SAMP and APC_crr / Unstructured region on APC between APC_crr regions 5 and 6 / Coiled-coil N-terminus of APC, dimerisation domain / Adenomatous polyposis coli (APC) repeat / : / KHDC4/BBP-like, KH-domain type I / KH domain-containing BBP-like / Type-1 KH domain profile. / Armadillo/plakoglobin ARM repeat profile. / Armadillo/beta-catenin-like repeat / K Homology domain, type 1 superfamily / Armadillo/beta-catenin-like repeats / Armadillo / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / K Homology domain / K homology RNA-binding domain / Armadillo-like helical / Alpha Horseshoe / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
Adenomatous polyposis coli protein / KH domain-containing, RNA-binding, signal transduction-associated protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsMorishita, E.C.J. / Murayama, K. / Kato-Murayama, M. / Ishizuku-Katsura, Y. / Tomabechi, Y. / Terada, T. / Handa, N. / Shirouzu, M. / Akiyama, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: Structure / Year: 2011
Title: Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of sam68
Authors: Morishita, E.C. / Murayama, K. / Kato-Murayama, M. / Ishizuka-Katsura, Y. / Tomabechi, Y. / Hayashi, T. / Terada, T. / Handa, N. / Shirouzu, M. / Akiyama, T. / Yokoyama, S.
History
DepositionJan 25, 2011Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Nov 2, 2011Provider: repository / Type: Initial release
Revision 1.1Nov 1, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Adenomatous polyposis coli protein
B: KH domain-containing, RNA-binding, signal transduction-associated protein 1
C: Adenomatous polyposis coli protein
D: KH domain-containing, RNA-binding, signal transduction-associated protein 1


Theoretical massNumber of molelcules
Total (without water)87,9914
Polymers87,9914
Non-polymers00
Water4,720262
1
A: Adenomatous polyposis coli protein
B: KH domain-containing, RNA-binding, signal transduction-associated protein 1


Theoretical massNumber of molelcules
Total (without water)43,9962
Polymers43,9962
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1720 Å2
ΔGint-7 kcal/mol
Surface area15200 Å2
MethodPISA
2
C: Adenomatous polyposis coli protein
D: KH domain-containing, RNA-binding, signal transduction-associated protein 1


Theoretical massNumber of molelcules
Total (without water)43,9962
Polymers43,9962
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1950 Å2
ΔGint-7 kcal/mol
Surface area15310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)148.223, 148.223, 63.379
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number169
Space group name H-MP61

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Components

#1: Protein Adenomatous polyposis coli protein / APC / Protein APC / Deleted in polyposis 2.5


Mass: 37502.219 Da / Num. of mol.: 2 / Fragment: Armadillo repeat domain, residues 396-732
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Description: E. coli cell-free system / Plasmid: pCR2.1 / Production host: cell free synthsis (unknown) / References: UniProt: P25054
#2: Protein KH domain-containing, RNA-binding, signal transduction-associated protein 1 / Src-associated in mitosis 68 kDa protein / Sam68 / GAP-associated tyrosine phosphoprotein p62 / p21 ...Src-associated in mitosis 68 kDa protein / Sam68 / GAP-associated tyrosine phosphoprotein p62 / p21 Ras GTPase-activating protein-associated p62 / p68


Mass: 6493.303 Da / Num. of mol.: 2 / Fragment: Tyrosine-rich domain, residues 365-419
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Description: E. coli cell-free system / Plasmid: pCR2.1 / Production host: cell free synthsis (unknown) / References: UniProt: Q07666
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 262 / 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: 2.28 Å3/Da / Density % sol: 46.15 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 100mM BIS-TRIS (pH 5.5), 150mM NaCl, 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Mar 30, 2010
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→64.18 Å / Num. all: 31344 / Num. obs: 31344 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 11.2 % / Rmerge(I) obs: 0.095 / Rsym value: 0.091 / Net I/σ(I): 7.1
Reflection shellResolution: 2.4→2.53 Å / Redundancy: 10.8 % / Rmerge(I) obs: 0.388 / Mean I/σ(I) obs: 2 / Num. unique all: 4539 / Rsym value: 0.37 / % possible all: 100

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.5.0102refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3AU3

3au3


Resolution: 2.4→64.18 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.908 / SU B: 14.657 / SU ML: 0.157 / Cross valid method: THROUGHOUT / ESU R Free: 0.239 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS; ASN709-LEU710 and LEU710-ILE711 C-N bonds in chain C, 0.91A and 1.05A, respectively, lie outside of the accepted range for the peptide bond ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS; ASN709-LEU710 and LEU710-ILE711 C-N bonds in chain C, 0.91A and 1.05A, respectively, lie outside of the accepted range for the peptide bond (1.30-1.45). depositors said that it was hard to build them suitably because these residues are in a region of poor density.
RfactorNum. reflection% reflectionSelection details
Rfree0.23046 1578 5 %RANDOM
Rwork0.18695 ---
all0.18915 31322 --
obs0.18915 29744 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 32.716 Å2
Baniso -1Baniso -2Baniso -3
1-0.17 Å20.09 Å20 Å2
2--0.17 Å20 Å2
3----0.26 Å2
Refinement stepCycle: LAST / Resolution: 2.4→64.18 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5100 0 0 262 5362
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0215185
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.0911.9577007
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.3255654
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.66524.591220
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.13815942
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.9081530
X-RAY DIFFRACTIONr_chiral_restr0.0720.2820
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.023786
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.4051.53282
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.825235
X-RAY DIFFRACTIONr_scbond_it1.50831903
X-RAY DIFFRACTIONr_scangle_it2.5244.51772
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.4→2.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.259 118 -
Rwork0.196 2180 -
obs--100 %
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)
112.92195.0391-0.44836.05910.42923.4143-0.19310.56110.1772-0.5990.2430.0215-0.28730.1637-0.04990.31530.046-0.08080.20090.08880.129934.2271123.2103-17.8859
216.3804-9.468121.200127.565111.039852.0089-0.44910.0111-0.2392-0.51550.76660.2194-1.32620.8229-0.31750.5640.2592-0.08930.5180.32160.620330.5282132.8954-15.2446
33.4802-0.6402-0.74364.4473-0.29683.4360.12030.0643-0.2075-0.2176-0.0440.34580.2932-0.1936-0.07630.1686-0.0133-0.1250.21390.05340.230325.3739115.1394-8.7447
41.48280.56840.35783.18470.24511.61890.05250.080.0129-0.17110.02330.18020.0111-0.0619-0.07580.15490.0081-0.02180.16180.04010.16737.2305120.9559-4.1588
51.3087-0.3219-0.29288.94690.21762.60580.0917-0.072-0.04420.0778-0.05650.0633-0.041-0.1071-0.03520.13840.0076-0.01760.1820.03670.182436.6392120.08235.5129
62.9416-0.4619-0.55037.293.94336.35240.07370.0527-0.0423-0.21780.1273-0.038-0.03370.213-0.2010.1330.0218-0.03570.15310.08360.177346.0904114.28986.6286
70.4509-0.51710.06772.3280.03971.77710.0607-0.04070.07330.0727-0.01510.1812-0.127-0.1396-0.04560.1463-0.0132-0.00260.1620.02610.21442.6437116.645516.6754
833.4326-18.0476-4.54459.74912.04434.9194-1.3343-1.5974-1.52280.74420.92450.8252-0.93070.29690.40980.5899-0.08180.2320.54670.00390.660926.9979122.499125.0302
94.0014-0.5928-0.39932.71990.18883.95880.0097-0.20960.18290.1693-0.0056-0.0638-0.04540.0632-0.00410.2151-0.0258-0.00840.15840.03840.217545.944112.843726.4079
1021.74455.86485.6277.0891-3.80697.4779-0.0398-1.59951.64040.8182-0.09930.6912-0.5857-1.25140.13910.2909-0.02480.04360.4897-0.14780.382433.4733108.499932.9297
115.2778-1.07540.37642.9731-1.32122.7209-0.0492-0.0967-0.13240.00580.0175-0.08350.06950.05280.03170.1809-0.03060.01680.1620.01880.193544.4838104.61428.9115
1211.93753.0921-9.49055.4837-2.31219.78970.1061-1.06480.02340.83230.0854-0.2674-0.29410.7265-0.19150.2484-0.0329-0.06630.24710.03090.138446.4535104.565240.6974
1313.43091.69514.18433.68820.6575.12340.07890.1236-0.2638-0.04570.0077-0.2262-0.04220.0706-0.08660.197-0.03260.03040.13610.05720.215239.318696.596731.6382
1412.9335-5.82591.0979.10893.899313.39950.5994-0.05590.1737-0.8319-0.1382-0.180.1969-0.5571-0.46120.3788-0.0309-0.02220.2430.06940.428732.5679109.63819.2276
152.22962.8946-5.371611.8863-5.849513.26660.3355-0.07340.3054-0.03130.08890.5553-0.88870.2977-0.42440.31630.0724-0.07230.3190.08560.53837.2743108.49821.7159
166.78172.72-4.25245.8743-3.50017.4581-0.06690.120.4620.06930.09480.1201-0.2586-0.4732-0.0280.1880.0501-0.02110.2585-0.01930.106-4.261194.524128.0151
1724.713310.24592.43734.24851.020.4998-0.8612.1471-0.2461-0.33750.8314-0.09380.2687-0.3490.02961.337-0.35110.2711.6767-0.15610.2562-11.376985.915528.1442
1810.95585.33510.34725.23111.37531.6999-0.23490.37320.5224-0.29160.0670.1878-0.1441-0.12750.16790.2533-0.0115-0.01360.19520.0530.10357.604795.906718.8843
198.415-5.56831.097417.6408-7.078517.5995-0.0294-0.21241.478-0.3976-0.0986-1.4383-0.5861.2530.1280.2941-0.0564-0.06130.22890.01170.392618.6731107.558625.7926
2031.0818-1.43471.17754.1212-9.653522.7775-0.5229-1.14361.58820.84080.2106-0.1954-1.9299-0.37780.31230.42520.0815-0.15590.14-0.09960.401710.9877107.162930.2959
211.81580.39280.3850.8617-0.04582.1106-0.0566-0.06650.10130.00930.0111-0.0516-0.015-0.14030.04550.16620.0095-0.01660.18470.01340.13059.659491.373329.4775
223.8204-0.0478-0.21382.34140.59685.2905-0.0005-0.0172-0.09230.0847-0.0062-0.01320.0944-0.1450.00670.1530.0213-0.00780.15940.0370.139216.78986.275533.8381
235.9668-2.4678-3.54747.45254.82558.6085-0.11660.037-0.46060.1971-0.04310.1930.4493-0.30890.15970.1459-0.0211-0.04890.20340.06330.189917.951179.311337.8503
243.4331-1.06260.46932.22050.4922.28450.0434-0.0238-0.25790.03810.058-0.08880.11780.0307-0.10140.1648-0.0258-0.02520.17390.01130.18526.660878.182138.288
254.798-0.80720.66675.6338-1.48864.50710.06550.2877-0.141-0.11510.0336-0.11480.20560.1983-0.09910.1509-0.0115-0.0650.2542-0.03370.294534.178573.950439.957
265.58770.23721.26676.3566-2.20994.52070.1971-0.0833-0.5261-0.062-0.0291-0.40680.52020.3974-0.16810.12250.013-0.08150.22-0.05420.236244.736174.989244.2651
277.37570.58162.093617.7048-6.9699.4762-0.0066-0.100400.48030.0346-0.158-0.27710.2244-0.0280.1406-0.0278-0.10650.232-0.07110.196148.29883.810448.9938
288.6985-1.48235.08896.5828-3.458917.2530.17640.0309-0.27840.21390.0356-0.07810.42490.4009-0.2120.089-0.04220.01960.1238-0.01070.231626.962490.788734.9721
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A401 - 440
2X-RAY DIFFRACTION2A441 - 445
3X-RAY DIFFRACTION3A446 - 473
4X-RAY DIFFRACTION4A474 - 533
5X-RAY DIFFRACTION5A534 - 553
6X-RAY DIFFRACTION6A554 - 579
7X-RAY DIFFRACTION7A580 - 622
8X-RAY DIFFRACTION8A623 - 627
9X-RAY DIFFRACTION9A628 - 665
10X-RAY DIFFRACTION10A666 - 672
11X-RAY DIFFRACTION11A673 - 694
12X-RAY DIFFRACTION12A695 - 704
13X-RAY DIFFRACTION13A705 - 731
14X-RAY DIFFRACTION14B379 - 388
15X-RAY DIFFRACTION15C402 - 411
16X-RAY DIFFRACTION16C412 - 425
17X-RAY DIFFRACTION17C426 - 439
18X-RAY DIFFRACTION18C440 - 458
19X-RAY DIFFRACTION19C459 - 464
20X-RAY DIFFRACTION20C465 - 470
21X-RAY DIFFRACTION21C471 - 526
22X-RAY DIFFRACTION22C527 - 559
23X-RAY DIFFRACTION23C560 - 581
24X-RAY DIFFRACTION24C582 - 622
25X-RAY DIFFRACTION25C623 - 661
26X-RAY DIFFRACTION26C662 - 706
27X-RAY DIFFRACTION27C707 - 731
28X-RAY DIFFRACTION28D379 - 389

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