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- PDB-3onw: Structure of a G-alpha-i1 mutant with enhanced affinity for the R... -

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Basic information

Entry
Database: PDB / ID: 3onw
TitleStructure of a G-alpha-i1 mutant with enhanced affinity for the RGS14 GoLoco motif.
Components
  • Guanine nucleotide-binding protein G(i) subunit alpha-1
  • Regulator of G-protein signaling 14
KeywordsSIGNALING PROTEIN / RGS14 GoLoco / Rosetta / protein design / affinity enhancement / Ras-like domain / all-helical domain / GoLoco motif / arginine finger / lipoprotein / transducer / guanine nucleotide dissociation inhibitor / GTP binding / nucleotide binding / ADP-ribosylation
Function / homology
Function and homology information


zygote asymmetric cell division / negative regulation of synaptic plasticity / regulation of G protein-coupled receptor signaling pathway / GTPase activating protein binding / GDP-dissociation inhibitor activity / nucleocytoplasmic transport / spindle organization / positive regulation of neurogenesis / negative regulation of G protein-coupled receptor signaling pathway / platelet-derived growth factor receptor signaling pathway ...zygote asymmetric cell division / negative regulation of synaptic plasticity / regulation of G protein-coupled receptor signaling pathway / GTPase activating protein binding / GDP-dissociation inhibitor activity / nucleocytoplasmic transport / spindle organization / positive regulation of neurogenesis / negative regulation of G protein-coupled receptor signaling pathway / platelet-derived growth factor receptor signaling pathway / negative regulation of MAP kinase activity / G-protein alpha-subunit binding / long-term memory / positive regulation of protein localization to cell cortex / Adenylate cyclase inhibitory pathway / T cell migration / D2 dopamine receptor binding / response to prostaglandin E / G protein-coupled serotonin receptor binding / adenylate cyclase regulator activity / adenylate cyclase-inhibiting serotonin receptor signaling pathway / cellular response to forskolin / regulation of mitotic spindle organization / GTPase activator activity / learning / chromosome segregation / Regulation of insulin secretion / positive regulation of cholesterol biosynthetic process / G protein-coupled receptor binding / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / negative regulation of ERK1 and ERK2 cascade / visual learning / PML body / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / response to peptide hormone / G-protein beta/gamma-subunit complex binding / centriolar satellite / spindle / long-term synaptic potentiation / spindle pole / ADP signalling through P2Y purinoceptor 12 / Adrenaline,noradrenaline inhibits insulin secretion / GDP binding / G alpha (z) signalling events / ADORA2B mediated anti-inflammatory cytokines production / GPER1 signaling / heterotrimeric G-protein complex / mitotic cell cycle / signaling receptor complex adaptor activity / G protein activity / midbody / cell cortex / microtubule binding / G alpha (i) signalling events / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / G alpha (s) signalling events / dendritic spine / response to oxidative stress / microtubule / Extra-nuclear estrogen signaling / postsynaptic density / ciliary basal body / nuclear body / G protein-coupled receptor signaling pathway / lysosomal membrane / cell division / GTPase activity / centrosome / dendrite / protein kinase binding / GTP binding / nucleolus / glutamatergic synapse / magnesium ion binding / Golgi apparatus / extracellular exosome / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
RGS14, RGS domain / : / : / : / GoLoco motif / GoLoco motif / GoLoco/GPR motif profile. / LGN motif, putative GEFs specific for G-alpha GTPases / RGS, subdomain 1/3 / GI Alpha 1, domain 2-like ...RGS14, RGS domain / : / : / : / GoLoco motif / GoLoco motif / GoLoco/GPR motif profile. / LGN motif, putative GEFs specific for G-alpha GTPases / RGS, subdomain 1/3 / GI Alpha 1, domain 2-like / GI Alpha 1, domain 2-like / Regulator of G protein signaling domain / RGS domain / RGS domain profile. / Regulator of G protein signalling domain / RGS, subdomain 2 / RGS domain superfamily / Raf-like Ras-binding domain / Raf-like Ras-binding / Ras-binding domain (RBD) profile. / Raf-like Ras-binding domain / G-protein alpha subunit, group I / Guanine nucleotide binding protein (G-protein), alpha subunit / G protein alpha subunit, helical insertion / G-protein alpha subunit / G-alpha domain profile. / G protein alpha subunit / Ubiquitin-like domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / Regulator of G-protein signaling 14 / Guanine nucleotide-binding protein G(i) subunit alpha-1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.38 Å
AuthorsBosch, D. / Kimple, A.J. / Sammond, D.W. / Miley, M.J. / Machius, M. / Kuhlman, B. / Willard, F.S. / Siderovski, D.P.
Citation
Journal: J.Biol.Chem. / Year: 2011
Title: Structural Determinants of Affinity Enhancement between GoLoco Motifs and G-Protein {alpha} Subunit Mutants.
Authors: Bosch, D.E. / Kimple, A.J. / Sammond, D.W. / Muller, R.E. / Miley, M.J. / Machius, M. / Kuhlman, B. / Willard, F.S. / Siderovski, D.P.
#1: Journal: J.Mol.Biol. / Year: 2007
Title: Structure-based protocol for identifying mutations that enhance protein-protein binding affinities
Authors: Sammond, D.W. / Eletr, Z.M. / Purbeck, C. / Kimple, R.J. / Siderovski, D.P. / Kuhlman, B.
#2: Journal: Nature / Year: 2002
Title: Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits
Authors: Kimple, R.J. / Kimple, M.E. / Betts, L. / Sondek, J. / Siderovski, D.P.
History
DepositionAug 30, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 24, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 6, 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: Guanine nucleotide-binding protein G(i) subunit alpha-1
B: Guanine nucleotide-binding protein G(i) subunit alpha-1
C: Regulator of G-protein signaling 14
D: Regulator of G-protein signaling 14
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,1959
Polymers83,0214
Non-polymers1,1755
Water1,74797
1
A: Guanine nucleotide-binding protein G(i) subunit alpha-1
C: Regulator of G-protein signaling 14
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,0504
Polymers41,5102
Non-polymers5392
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3730 Å2
ΔGint-16 kcal/mol
Surface area17280 Å2
MethodPISA
2
B: Guanine nucleotide-binding protein G(i) subunit alpha-1
D: Regulator of G-protein signaling 14
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,1465
Polymers41,5102
Non-polymers6353
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3770 Å2
ΔGint-17 kcal/mol
Surface area17020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)70.392, 83.679, 190.148
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number17
Space group name H-MP2221

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Components

#1: Protein Guanine nucleotide-binding protein G(i) subunit alpha-1 / Adenylate cyclase-inhibiting G alpha protein


Mass: 37416.637 Da / Num. of mol.: 2 / Mutation: Q147L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GNAI1 / Plasmid: pLICHis / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P63096, EC: 3.6.5.1
#2: Protein/peptide Regulator of G-protein signaling 14 / RGS14


Mass: 4093.621 Da / Num. of mol.: 2 / Source method: obtained synthetically
Details: The RGS14 GoLoco motif peptide was synthesized according to the human RGS14 sequence, identical to that used in PDB entries 1KJY and 2OM2.
References: UniProt: O43566
#3: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#4: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 97 / 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: 3.37 Å3/Da / Density % sol: 63.53 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5
Details: Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (10 mM Tris pH 7.5, 1 mM magnesium chloride, 5% (w/v) glycerol, 5 mM DTT) and well solution (1.9 M ammonium sulfate, 100 ...Details: Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (10 mM Tris pH 7.5, 1 mM magnesium chloride, 5% (w/v) glycerol, 5 mM DTT) and well solution (1.9 M ammonium sulfate, 100 mM sodium acetate pH 5.0, 200 mM magnesium chloride, 10% (w/v) glycerol), VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å
DetectorType: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Nov 30, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.38→28.88 Å / Num. all: 45328 / Num. obs: 45328 / % possible obs: 98.8 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 6 % / Biso Wilson estimate: 59.4 Å2 / Rmerge(I) obs: 0.065 / Net I/σ(I): 27.3
Reflection shellResolution: 2.38→2.4 Å / Redundancy: 6 % / Rmerge(I) obs: 0.761 / Mean I/σ(I) obs: 2.2 / % possible all: 100

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Processing

Software
NameVersionClassification
PHASERphasing
REFMAC5.5.0109refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2OM2 chain A

2om2


Resolution: 2.38→95.07 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.917 / SU B: 15.463 / SU ML: 0.166 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / ESU R: 0.294 / ESU R Free: 0.234 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.26539 1528 3.4 %RANDOM
Rwork0.22825 ---
obs0.22953 43755 98.55 %-
all-43755 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 62.254 Å2
Baniso -1Baniso -2Baniso -3
1--0.02 Å2-0 Å20 Å2
2---0.33 Å2-0 Å2
3---0.35 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.231 Å0.29 Å
Refinement stepCycle: LAST / Resolution: 2.38→95.07 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5643 0 71 97 5811
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0225811
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.0861.9687841
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.155698
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.92524.507284
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.856151065
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.8071536
X-RAY DIFFRACTIONr_chiral_restr0.0740.2872
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.024310
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_it0.4631.53480
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.89725606
X-RAY DIFFRACTIONr_scbond_it1.30332331
X-RAY DIFFRACTIONr_scangle_it2.0864.52235
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.38→2.442 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.28 105 -
Rwork0.3 3186 -
obs--97.77 %
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)
10.3227-0.29360.30822.88620.02621.61190.11620.0044-0.31310.1238-0.10730.55070.4281-0.2337-0.00890.2878-0.0278-0.00610.1292-0.0420.387815.286625.065515.7499
21.0487-0.9937-1.66672.3883.04414.5068-0.16380.2319-0.02930.0663-0.19960.61290.2872-0.56580.36330.3483-0.0775-0.02390.40770.00030.6006-1.943228.356817.5663
36.79333.19192.00077.53721.52942.00710.0171-0.11580.26240.4649-0.05350.30720.1013-0.0250.03630.12160.03350.09340.1529-0.01040.10569.732850.69829.1479
42.9532-0.9222-1.55513.0923-3.9965.92750.0128-0.12970.49770.6006-0.12820.4646-0.2985-0.19870.11550.15390.06830.02230.3094-0.06190.38462.422358.176433.2444
56.8245-0.2028-0.53041.1480.7970.643-0.1371-0.06880.30980.0159-0.07740.39450.0719-0.13510.21450.10540.0008-0.02060.19430.0290.17945.637350.089724.7147
60.2548-0.7694-0.41913.66031.44491.5591-0.03170.0547-0.22560.0937-0.11390.31510.1958-0.14960.14560.2295-0.08220.00380.3289-0.02720.33873.575932.967317.7324
73.0425-1.32170.76132.61410.06560.72880.0124-0.2757-0.30260.38870.06990.04780.1628-0.0032-0.08230.4168-0.01560.01140.24940.04720.291121.813518.73723.5138
82.1870.61850.953410.25441.81520.85980.1448-0.3856-0.22570.1583-0.0991-0.01180.2499-0.1284-0.04580.15170.0130.02110.11250.04690.032625.406236.593318.3056
93.2121-1.3316-0.40724.63680.12371.7552-0.0633-0.2202-0.43590.16340.0407-0.18650.36290.26360.02270.21780.0398-0.02340.08480.02980.09429.364830.653115.4263
104.89191.66410.99346.2531.29065.08140.03510.33660.5812-0.41740.1216-0.2442-0.21240.0579-0.15670.1019-0.00450.04280.03170.03980.111928.721245.19167.8271
112.6522-1.9713-1.537712.19173.65781.7981-0.01380.3743-0.9876-0.4306-0.1204-0.96630.19170.11860.13420.45830.16250.0130.3918-0.18380.645635.699624.61036.324
121.59682.03730.242.654-0.02233.6293-0.16230.0016-0.1369-0.2961-0.0291-0.12360.5165-0.2930.19150.3286-0.005-0.08330.1993-0.14350.252316.983926.23534.0417
136.6096-2.10532.76780.7701-0.79891.22790.16330.2876-0.61210.0628-0.06070.35220.14470.132-0.10260.2413-0.05120.12220.1847-0.02820.322613.861236.673917.2547
143.4675-0.06-0.83332.34481.03111.26960.00350.31690.5604-0.08860.207-0.6419-0.21780.4029-0.21060.0918-0.0765-0.02650.33390.12160.323351.257969.02830.7495
153.3245-0.46391.20730.5034-0.62580.97730.18210.35030.60890.126-0.2637-0.0499-0.1670.43680.08150.485-0.03520.02330.42130.03130.613848.471285.858525.505
1611.69245.1975-1.42379.1806-1.55320.3097-0.11690.8774-0.2072-1.20590.08490.34910.1766-0.03690.0320.36220.0555-0.04880.21650.05870.201327.777276.507617.1556
172.6552-0.16231.0162.14990.7142.0832-0.01930.66990.3863-0.3850.08060.2592-0.1205-0.0585-0.06130.44840.0697-0.0460.38150.0620.372424.543384.494213.5569
181.7003-1.24620.01576.152-2.28081.56090.16040.15910.2062-0.1467-0.11650.5122-0.2541-0.0871-0.04390.21920.0796-0.05630.108-0.00090.229826.410580.067623.8864
190.948-1.5716-1.15793.25021.54312.45340.08580.00840.39980.0584-0.0745-0.6082-0.42670.0223-0.01140.3142-0.0412-0.06710.1970.07080.518539.703487.603127.2962
205.4486-0.65543.46732.10241.22155.5918-0.20620.65310.2134-0.17590.0772-0.145-0.30270.7140.1290.278-0.09580.00970.38250.08820.396357.649471.726229.7334
211.3979-2.18230.25674.01220.51223.3930.23020.31050.1608-0.4337-0.0539-0.28930.11870.2895-0.17640.1396-0.01850.07760.47230.04270.261255.570960.196722.1751
225.50290.331-0.21152.15360.53640.3102-0.02270.2711-0.2884-0.1890.01-0.16160.06150.13510.01270.11130.07130.05320.18660.00010.043241.732355.6829.5925
234.3642-0.5541-0.36015.78130.58933.9304-0.1271-0.3518-0.30670.4132-0.00880.49550.1622-0.21130.13590.0385-0.01220.04570.08010.00690.061731.689959.568539.4525
246.50666.27180.06288.41062.19292.0403-0.15-0.6303-0.40910.0614-0.11510.06290.38590.5290.26510.4950.0971-0.10320.40240.02520.470550.256345.311839.8728
257.68620.06220.79731.18980.44112.9607-0.4158-0.55670.27230.46820.1199-0.50680.15220.48590.29590.2430.0282-0.19530.2357-0.01830.311951.082865.838842.3328
268.79169.94180.722711.37080.78180.06930.3515-0.14330.22860.34-0.42670.1050.03610.06640.07520.12690.04740.04380.620.3350.19240.040771.70629.4461
2711.6889-5.1599-2.86962.40961.35744.559-0.4209-0.9177-0.11110.39120.4562-0.2241-0.0740.5784-0.03540.58930.1223-0.27510.40080.02180.642132.144926.595426.9288
2813.1135-17.8473-2.911826.08753.3330.9541-0.4645-1.6437-0.29010.01590.94231.09260.06840.689-0.47780.67820.2365-0.05371.0321-0.25090.503521.192435.07226.9314
2917.59732.4605-19.34590.4366-2.649121.3258-0.2592-0.8036-0.25340.2067-0.04530.00250.50090.81510.30450.6983-0.00120.08260.36680.11140.30928.134738.364731.6106
303.3497-2.48473.34271.887-2.48813.3976-0.0974-0.16910.18970.0673-0.0179-0.28990.1088-0.03240.11530.55140.0515-0.10510.61710.0020.68429.34350.312339.5055
310.0171-0.17810.71721.9716-8.042532.9303-0.10270.05-0.0191-0.2264-0.5358-0.11081.03611.50160.63850.2783-0.06020.35170.6609-0.43230.872549.96448.398219.9865
3216.2753-9.46891.156116.8565-5.42032.09680.31410.16140.0793-1.1863-0.09510.50280.36650.0384-0.2190.31450.0021-0.04990.3571-0.02240.028442.324658.454519.8942
339.91250.6015-2.98849.0805-9.386410.3009-0.69961.1938-0.4679-0.7820.1846-0.38340.8805-0.42340.5150.53330.00350.12810.42950.0660.227538.409375.038416.1396
3416.77040.5166-0.28186.7059-0.97540.21120.0659-0.0732-0.7477-0.11020.0242-0.21790.08230.0841-0.09010.54240.036-0.0090.59260.03680.387829.692676.24877.871
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A32 - 55
2X-RAY DIFFRACTION2A56 - 71
3X-RAY DIFFRACTION3A72 - 95
4X-RAY DIFFRACTION4A96 - 109
5X-RAY DIFFRACTION5A110 - 155
6X-RAY DIFFRACTION6A156 - 193
7X-RAY DIFFRACTION7A194 - 216
8X-RAY DIFFRACTION8A217 - 237
9X-RAY DIFFRACTION9A238 - 273
10X-RAY DIFFRACTION10A274 - 309
11X-RAY DIFFRACTION11A310 - 320
12X-RAY DIFFRACTION12A321 - 347
13X-RAY DIFFRACTION13A401
14X-RAY DIFFRACTION14B32 - 56
15X-RAY DIFFRACTION15B57 - 75
16X-RAY DIFFRACTION16B76 - 90
17X-RAY DIFFRACTION17B91 - 119
18X-RAY DIFFRACTION18B120 - 158
19X-RAY DIFFRACTION19B159 - 178
20X-RAY DIFFRACTION20B179 - 195
21X-RAY DIFFRACTION21B196 - 219
22X-RAY DIFFRACTION22B220 - 267
23X-RAY DIFFRACTION23B268 - 311
24X-RAY DIFFRACTION24B312 - 317
25X-RAY DIFFRACTION25B318 - 348
26X-RAY DIFFRACTION26B401
27X-RAY DIFFRACTION27C496 - 506
28X-RAY DIFFRACTION28C507 - 513
29X-RAY DIFFRACTION29C514 - 520
30X-RAY DIFFRACTION30C521 - 531
31X-RAY DIFFRACTION31D496 - 501
32X-RAY DIFFRACTION32D502 - 512
33X-RAY DIFFRACTION33D513 - 519
34X-RAY DIFFRACTION34D520 - 529

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