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- PDB-4nhz: Crystal structure of glutathione transferase BBTA-3750 from Brady... -

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Basic information

Entry
Database: PDB / ID: 4nhz
TitleCrystal structure of glutathione transferase BBTA-3750 from Bradyrhizobium sp., Target EFI-507290, with one glutathione bound
ComponentsPutative glutathione S-transferase enzyme with thioredoxin-like domain
KeywordsTRANSFERASE / glutathione s-transferase / Enzyme Function Initiative / EFI / structural genomics
Function / homology
Function and homology information


transferase activity
Similarity search - Function
Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione S-transferase, C-terminal / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 - #10 / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily ...Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione S-transferase, C-terminal / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 - #10 / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / Up-down Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GLUTATHIONE / Putative glutathione S-transferase enzyme with thioredoxin-like domain
Similarity search - Component
Biological speciesBradyrhizobium sp. (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.901 Å
AuthorsPatskovsky, Y. / Vetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Stead, M. / Washington, E. ...Patskovsky, Y. / Vetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Stead, M. / Washington, E. / Scott Glenn, A. / Chowdhury, S. / Evans, B. / Hammonds, J. / Hillerich, B. / Love, J. / Seidel, R.D. / Imker, H.J. / Gerlt, J.A. / Armstrong, R.N. / Almo, S.C. / Enzyme Function Initiative (EFI)
CitationJournal: To be Published
Title: Crystal Structure of Glutathione Transferase Bbta-3750 from Bradyrhizobium Sp., Target Efi-507290
Authors: Patskovsky, Y. / Vetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Stead, M. / Washington, E. / Scott Glenn, A. / Chowdhury, S. / Evans, ...Authors: Patskovsky, Y. / Vetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Stead, M. / Washington, E. / Scott Glenn, A. / Chowdhury, S. / Evans, B. / Hammonds, J. / Hillerich, B. / Love, J. / Seidel, R.D. / Imker, H.J. / Gerlt, J.A. / Armstrong, R.N. / Almo, S.C.
History
DepositionNov 5, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 20, 2013Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2018Group: Structure summary / Category: audit_author / Item: _audit_author.name
Revision 1.2Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _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: Putative glutathione S-transferase enzyme with thioredoxin-like domain
B: Putative glutathione S-transferase enzyme with thioredoxin-like domain
C: Putative glutathione S-transferase enzyme with thioredoxin-like domain
D: Putative glutathione S-transferase enzyme with thioredoxin-like domain
E: Putative glutathione S-transferase enzyme with thioredoxin-like domain
F: Putative glutathione S-transferase enzyme with thioredoxin-like domain
G: Putative glutathione S-transferase enzyme with thioredoxin-like domain
H: Putative glutathione S-transferase enzyme with thioredoxin-like domain
I: Putative glutathione S-transferase enzyme with thioredoxin-like domain
J: Putative glutathione S-transferase enzyme with thioredoxin-like domain
K: Putative glutathione S-transferase enzyme with thioredoxin-like domain
L: Putative glutathione S-transferase enzyme with thioredoxin-like domain
M: Putative glutathione S-transferase enzyme with thioredoxin-like domain
N: Putative glutathione S-transferase enzyme with thioredoxin-like domain
O: Putative glutathione S-transferase enzyme with thioredoxin-like domain
P: Putative glutathione S-transferase enzyme with thioredoxin-like domain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)469,52632
Polymers464,60916
Non-polymers4,91716
Water39,8852214
1
A: Putative glutathione S-transferase enzyme with thioredoxin-like domain
B: Putative glutathione S-transferase enzyme with thioredoxin-like domain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,6914
Polymers58,0762
Non-polymers6152
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4990 Å2
ΔGint-30 kcal/mol
Surface area19100 Å2
MethodPISA
2
C: Putative glutathione S-transferase enzyme with thioredoxin-like domain
D: Putative glutathione S-transferase enzyme with thioredoxin-like domain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,6914
Polymers58,0762
Non-polymers6152
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5050 Å2
ΔGint-28 kcal/mol
Surface area18020 Å2
MethodPISA
3
E: Putative glutathione S-transferase enzyme with thioredoxin-like domain
F: Putative glutathione S-transferase enzyme with thioredoxin-like domain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,6914
Polymers58,0762
Non-polymers6152
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4980 Å2
ΔGint-29 kcal/mol
Surface area18020 Å2
MethodPISA
4
G: Putative glutathione S-transferase enzyme with thioredoxin-like domain
H: Putative glutathione S-transferase enzyme with thioredoxin-like domain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,6914
Polymers58,0762
Non-polymers6152
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5020 Å2
ΔGint-27 kcal/mol
Surface area19280 Å2
MethodPISA
5
I: Putative glutathione S-transferase enzyme with thioredoxin-like domain
J: Putative glutathione S-transferase enzyme with thioredoxin-like domain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,6914
Polymers58,0762
Non-polymers6152
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4920 Å2
ΔGint-30 kcal/mol
Surface area18040 Å2
MethodPISA
6
K: Putative glutathione S-transferase enzyme with thioredoxin-like domain
L: Putative glutathione S-transferase enzyme with thioredoxin-like domain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,6914
Polymers58,0762
Non-polymers6152
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4740 Å2
ΔGint-29 kcal/mol
Surface area18250 Å2
MethodPISA
7
M: Putative glutathione S-transferase enzyme with thioredoxin-like domain
N: Putative glutathione S-transferase enzyme with thioredoxin-like domain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,6914
Polymers58,0762
Non-polymers6152
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5040 Å2
ΔGint-27 kcal/mol
Surface area17980 Å2
MethodPISA
8
O: Putative glutathione S-transferase enzyme with thioredoxin-like domain
P: Putative glutathione S-transferase enzyme with thioredoxin-like domain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,6914
Polymers58,0762
Non-polymers6152
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4930 Å2
ΔGint-29 kcal/mol
Surface area18100 Å2
MethodPISA
Unit cell
Length a, b, c (Å)96.998, 99.359, 108.734
Angle α, β, γ (deg.)89.98, 89.97, 89.99
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.864955, 0.50185, -0.000663), (0.501687, 0.864639, -0.026655), (-0.012804, -0.023388, -0.999645)-24.08704, 6.96658, 27.25647
3given(-0.999992, 0.002796, 0.002824), (0.002793, 0.999996, -0.001048), (-0.002827, -0.00104, -0.999995)-85.22741, 21.14307, 44.21517
4given(0.870674, 0.49186, 0.000344), (-0.491698, 0.870369, 0.026277), (0.012625, -0.023048, 0.999655)60.14551, -18.0436, -16.57843
5given(-0.999923, 0.006429, 0.010598), (0.006394, 0.999974, -0.003315), (-0.010619, -0.003247, -0.999938)-37.01893, -49.53583, 16.90752
6given(0.868094, 0.496363, -0.006089), (-0.496035, 0.86786, 0.027722), (0.019045, -0.021044, 0.999597)-16.92138, -54.93696, 11.92316
7given(0.999996, 0.000513, -0.002917), (0.000511, -1, -0.000699), (-0.002918, 0.000697, -0.999996)48.75589, -62.50098, 98.65948
8given(-0.864635, -0.502397, 0.001992), (0.502276, -0.864324, 0.025731), (-0.011205, 0.023248, 0.999667)-97.61541, -25.34678, -70.58526
9given(0.999946, -0.005693, 0.008671), (-0.00566, -0.999977, -0.003776), (0.008692, 0.003726, -0.999955)-0.49705, 8.19578, 71.42433
10given(-0.868254, -0.496097, -0.004724), (0.495831, -0.868035, 0.025824), (-0.016912, 0.020079, 0.999655)-19.84933, 11.97393, -44.26917
11given(0.868338, -0.49594, 0.005672), (-0.495634, -0.868112, -0.027), (0.018315, 0.020634, -0.999619)43.4778, -47.37777, 2.11219
12given(-0.999931, -0.006602, -0.009718), (0.00657, -0.999973, 0.003398), (-0.00974, 0.003334, 0.999947)-85.38143, -12.4689, 26.24724
13given(0.870742, -0.491738, -0.0013), (-0.4916, -0.870429, -0.026125), (0.011715, 0.023387, -0.999658)-12.77757, -46.09066, 83.02439
14given(-0.999991, -0.003847, -0.00166), (0.003846, -0.999992, 0.000519), (-0.001662, 0.000513, 0.999999)-36.70277, -41.64221, -54.38498
15given(-0.868646, 0.4954, 0.005679), (0.495117, 0.868445, -0.025735), (-0.017681, -0.019543, -0.999653)-80.71918, 6.61231, 54.37889
16given(0.999927, 0.005313, -0.010824), (-0.005278, 0.999981, 0.003289), (0.010841, -0.003232, 0.999936)48.73565, -29.17506, -26.70252

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Components

#1: Protein
Putative glutathione S-transferase enzyme with thioredoxin-like domain


Mass: 29038.074 Da / Num. of mol.: 16
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bradyrhizobium sp. (bacteria) / Strain: BTAI1 / ATCC BAA-1182 / Gene: BBta_3750 / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A5EI34
#2: Chemical
ChemComp-GSH / GLUTATHIONE


Mass: 307.323 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C10H17N3O6S
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2214 / 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: 2.27 Å3/Da / Density % sol: 45.82 %
Crystal growpH: 8.5
Details: Protein in 10 mM HEPES, pH 7.5, 150 mM sodium chloride, 5% glycerol, reservoir: 25% PEG4000, 0.1M TRIS-HCl pH 8.5, 0.2M calcium acetate, 5 mM GSH, cryoprotectant: 20% glycerol, vapor ...Details: Protein in 10 mM HEPES, pH 7.5, 150 mM sodium chloride, 5% glycerol, reservoir: 25% PEG4000, 0.1M TRIS-HCl pH 8.5, 0.2M calcium acetate, 5 mM GSH, cryoprotectant: 20% glycerol, vapor diffusion, sitting drop, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.075
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 18, 2013 / Details: MIRRORS
RadiationMonochromator: ROSENBAUM-ROCK DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.075 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 309970 / % possible obs: 97.2 % / Observed criterion σ(I): -5 / Redundancy: 2 % / Rsym value: 0.047 / Net I/σ(I): 8.8
Reflection shellResolution: 1.9→1.93 Å / Redundancy: 2 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 2.5 / % possible all: 95.1

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Processing

Software
NameVersionClassification
PHASERphasing
REFMAC5.8.0049refinement
HKL-3000data reduction
HKL-3000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4MF7

4mf7


Resolution: 1.901→50 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.955 / SU B: 10.381 / SU ML: 0.141 / Cross valid method: THROUGHOUT / ESU R: 0.156 / ESU R Free: 0.143 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.22542 6282 2 %RANDOM
Rwork0.18577 ---
obs0.18658 303683 97.03 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 31.684 Å2
Baniso -1Baniso -2Baniso -3
1-5.43 Å20.21 Å20.05 Å2
2---2.95 Å20.06 Å2
3----2.49 Å2
Refinement stepCycle: LAST / Resolution: 1.901→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29909 0 314 2214 32437
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.01931319
X-RAY DIFFRACTIONr_bond_other_d0.0010.0229873
X-RAY DIFFRACTIONr_angle_refined_deg1.3811.97742542
X-RAY DIFFRACTIONr_angle_other_deg0.811368791
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.50253776
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.66923.1221483
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.158155095
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.23615260
X-RAY DIFFRACTIONr_chiral_restr0.0790.24375
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.02135575
X-RAY DIFFRACTIONr_gen_planes_other0.0010.027533
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_it5.162.18514978
X-RAY DIFFRACTIONr_mcbond_other5.1572.18514977
X-RAY DIFFRACTIONr_mcangle_it5.6493.64618709
X-RAY DIFFRACTIONr_mcangle_other5.653.64618710
X-RAY DIFFRACTIONr_scbond_it9.5182.86716341
X-RAY DIFFRACTIONr_scbond_other9.5122.86716340
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other10.1734.4923804
X-RAY DIFFRACTIONr_long_range_B_refined10.63911.02537791
X-RAY DIFFRACTIONr_long_range_B_other10.65910.73936934
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.901→1.95 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.361 463 -
Rwork0.356 21472 -
obs--92.83 %
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)
10.71440.1910.14241.67440.32441.6209-0.00070.03820.045-0.16610.01680.0592-0.0394-0.0483-0.01620.01780.0086-0.00170.10720.01680.0644-17.5693-17.50152.5778
20.7804-0.09420.09481.43-0.23111.2551-0.007-0.0482-0.00760.1107-0.0052-0.05850.07590.09650.01210.01610.0015-0.00410.1344-0.00110.0571-16.6324-18.780425.3309
30.7293-0.13850.14531.5369-0.4021.4493-0.0043-0.03320.02980.09990.0001-0.0702-0.0490.05620.00420.0108-0.0206-0.00580.1017-0.0030.0718-67.5775-38.445141.8839
40.6390.0934-0.03951.3340.29731.3901-0.00530.05130.0152-0.1993-0.02310.01720.0104-0.05480.02850.0351-0.0146-0.00560.10720.01270.0809-67.6792-38.172419.1378
50.7779-0.06710.17941.2629-0.25941.2785-0.0015-0.04140.0130.14540.003-0.0372-0.05030.0318-0.00140.0262-0.0304-0.00610.10220.00030.0702-19.106932.213714.4297
60.5515-0.1260.0131.53180.48721.53620.01270.075-0.0073-0.1459-0.03270.0433-0.0038-0.05370.020.0177-0.0151-0.0080.12670.02330.0848-19.261932.445-8.2966
70.723-0.1853-0.0721.63990.28411.49630.0076-0.0475-0.04030.15580.01450.04940.043-0.0426-0.02210.0176-0.0134-0.00180.10870.0160.0827-65.9361-45.135996.2331
80.63830.072-0.06381.3471-0.20941.154-0.01070.05190.0065-0.1278-0.0039-0.0593-0.06390.10460.01460.0186-0.01090.00270.1392-0.00190.0802-64.9345-43.524773.4971
90.6842-0.1341-0.07521.34680.39361.32790.0095-0.042-0.0260.18280.00670.0340.0263-0.037-0.01620.0309-0.019-0.00530.10130.01420.0815-17.52625.532168.8049
100.4589-0.0086-0.00231.745-0.31521.418-0.00560.0619-0.0157-0.117-0.0019-0.0879-0.080.09040.00750.0168-0.0162-0.00030.1198-0.00510.0843-17.435925.311746.0693
110.55180.0519-0.03091.59120.46741.4470.012-0.06330.00850.1579-0.03540.04580.0043-0.05280.02340.01810.00630.00050.13060.02250.1015-67.75754.2642-1.6255
120.85930.0067-0.24281.2284-0.29041.2582-0.00690.0403-0.0002-0.14140.0063-0.04190.04820.02820.00060.02080.0188-0.00120.10020.00160.087-67.54174.5237-24.3629
130.6606-0.1444-0.02221.30170.31411.2936-0.0037-0.0506-0.01350.1922-0.01550.01570.0033-0.03820.01920.03140.0072-0.00020.10770.01080.0632-19.1105-24.484179.6683
140.71640.1454-0.10781.5548-0.37871.4129-0.00470.0329-0.0429-0.1202-0.0031-0.07090.04310.04090.00780.01080.01190.00380.094-0.00140.0558-19.1392-24.185856.9369
150.54790.00890.03381.6496-0.30011.4029-0.0075-0.07130.00460.1008-0.0008-0.08430.06210.08370.00820.01120.0078-0.00450.1194-0.00310.1017-65.928211.441952.7537
160.75920.09490.11971.36750.39441.2920.00010.04790.0267-0.18010.00460.036-0.0268-0.035-0.00470.02550.0096-0.00120.10490.01370.093-66.045411.233330.0287
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A3 - 234
2X-RAY DIFFRACTION2B-9 - 234
3X-RAY DIFFRACTION3C2 - 234
4X-RAY DIFFRACTION4D3 - 234
5X-RAY DIFFRACTION5E3 - 234
6X-RAY DIFFRACTION6F4 - 234
7X-RAY DIFFRACTION7G4 - 234
8X-RAY DIFFRACTION8H-11 - 234
9X-RAY DIFFRACTION9I3 - 234
10X-RAY DIFFRACTION10J4 - 234
11X-RAY DIFFRACTION11K4 - 234
12X-RAY DIFFRACTION12L2 - 234
13X-RAY DIFFRACTION13M4 - 234
14X-RAY DIFFRACTION14N3 - 234
15X-RAY DIFFRACTION15O4 - 234
16X-RAY DIFFRACTION16P3 - 234

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