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- PDB-4ggf: Crystal structure of Mn2+ bound calprotectin -

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Basic information

Entry
Database: PDB / ID: 4ggf
TitleCrystal structure of Mn2+ bound calprotectin
Components(Protein S100- ...) x 2
KeywordsANTIMICROBIAL PROTEIN / S100 / EF-hand
Function / homology
Function and homology information


S100A9 complex / regulation of integrin biosynthetic process / sequestering of zinc ion / calprotectin complex / neutrophil aggregation / positive regulation of peptide secretion / regulation of respiratory burst involved in inflammatory response / modulation of process of another organism / autocrine signaling / Toll-like receptor 4 binding ...S100A9 complex / regulation of integrin biosynthetic process / sequestering of zinc ion / calprotectin complex / neutrophil aggregation / positive regulation of peptide secretion / regulation of respiratory burst involved in inflammatory response / modulation of process of another organism / autocrine signaling / Toll-like receptor 4 binding / chronic inflammatory response / peptidyl-cysteine S-trans-nitrosylation / Metal sequestration by antimicrobial proteins / leukocyte migration involved in inflammatory response / peptide secretion / Regulation of TLR by endogenous ligand / RAGE receptor binding / astrocyte development / MyD88 deficiency (TLR2/4) / arachidonic acid binding / intermediate filament cytoskeleton / IRAK4 deficiency (TLR2/4) / MyD88:MAL(TIRAP) cascade initiated on plasma membrane / response to zinc ion / regulation of toll-like receptor signaling pathway / regulation of cytoskeleton organization / peptidyl-cysteine S-nitrosylation / antioxidant activity / RHO GTPases Activate NADPH Oxidases / endothelial cell migration / defense response to fungus / positive regulation of intrinsic apoptotic signaling pathway / neutrophil chemotaxis / autophagy / positive regulation of neuron projection development / positive regulation of inflammatory response / activation of cysteine-type endopeptidase activity involved in apoptotic process / calcium-dependent protein binding / antimicrobial humoral immune response mediated by antimicrobial peptide / cell-cell signaling / positive regulation of NF-kappaB transcription factor activity / ER-Phagosome pathway / positive regulation of cell growth / microtubule binding / secretory granule lumen / collagen-containing extracellular matrix / response to ethanol / response to lipopolysaccharide / cytoskeleton / defense response to bacterium / inflammatory response / innate immune response / apoptotic process / calcium ion binding / Neutrophil degranulation / extracellular space / extracellular exosome / zinc ion binding / extracellular region / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
S-100/ICaBP type calcium binding protein signature. / S100/Calcium binding protein 7/8-like, conserved site / S100/CaBP-9k-type, calcium binding, subdomain / S-100/ICaBP type calcium binding domain / S-100/ICaBP type calcium binding domain / EF-hand / Recoverin; domain 1 / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. ...S-100/ICaBP type calcium binding protein signature. / S100/Calcium binding protein 7/8-like, conserved site / S100/CaBP-9k-type, calcium binding, subdomain / S-100/ICaBP type calcium binding domain / S-100/ICaBP type calcium binding domain / EF-hand / Recoverin; domain 1 / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
: / Protein S100-A8 / Protein S100-A9
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsDamo, S.M. / Fritz, G.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2013
Title: Molecular basis for manganese sequestration by calprotectin and roles in the innate immune response to invading bacterial pathogens.
Authors: Damo, S.M. / Kehl-Fie, T.E. / Sugitani, N. / Holt, M.E. / Rathi, S. / Murphy, W.J. / Zhang, Y. / Betz, C. / Hench, L. / Fritz, G. / Skaar, E.P. / Chazin, W.J.
History
DepositionAug 6, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 20, 2013Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2013Group: Database references
Revision 1.2Mar 27, 2013Group: Database references
Revision 1.3Sep 13, 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 / pdbx_struct_conn_angle / struct_conn / 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 / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _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: Protein S100-A8
C: Protein S100-A9
K: Protein S100-A8
L: Protein S100-A9
S: Protein S100-A8
T: Protein S100-A9
U: Protein S100-A8
V: Protein S100-A9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)98,04836
Polymers96,3428
Non-polymers1,70628
Water8,791488
1
A: Protein S100-A8
C: Protein S100-A9
K: Protein S100-A8
L: Protein S100-A9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,00718
Polymers48,1714
Non-polymers83714
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12010 Å2
ΔGint-193 kcal/mol
Surface area17080 Å2
MethodPISA
2
S: Protein S100-A8
T: Protein S100-A9
U: Protein S100-A8
V: Protein S100-A9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,04118
Polymers48,1714
Non-polymers87014
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11890 Å2
ΔGint-183 kcal/mol
Surface area17140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)82.027, 217.002, 53.022
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

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Protein S100- ... , 2 types, 8 molecules AKSUCLTV

#1: Protein
Protein S100-A8 / Calgranulin-A / Calprotectin L1L subunit / Cystic fibrosis antigen / CFAG / Leukocyte L1 complex ...Calgranulin-A / Calprotectin L1L subunit / Cystic fibrosis antigen / CFAG / Leukocyte L1 complex light chain / Migration inhibitory factor-related protein 8 / MRP-8 / p8 / S100 calcium-binding protein A8 / Urinary stone protein band A


Mass: 10837.463 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: S100A8, CAGA, CFAG, MRP8 / Plasmid: pET1120 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P05109
#2: Protein
Protein S100-A9 / Calgranulin-B / Calprotectin L1H subunit / Leukocyte L1 complex heavy chain / Migration inhibitory ...Calgranulin-B / Calprotectin L1H subunit / Leukocyte L1 complex heavy chain / Migration inhibitory factor-related protein 14 / MRP-14 / p14 / S100 calcium-binding protein A9


Mass: 13247.955 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: S100A9, CAGB, CFAG, MRP14 / Production host: Escherichia coli (E. coli) / References: UniProt: P06702

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Non-polymers , 5 types, 516 molecules

#3: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Ca
#4: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Mn
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


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


Mass: 18.015 Da / Num. of mol.: 488 / 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: 2.45 Å3/Da / Density % sol: 49.78 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: PEG 3350, lithium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 11, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 1.6→50 Å / Num. all: 126186 / Num. obs: 124149 / % possible obs: 98.4 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 6.7 % / Rmerge(I) obs: 0.112 / Net I/σ(I): 16.81
Reflection shell
Resolution (Å)Diffraction-ID% possible all
1.6-1.7190.6
1.7-1.8199.8
1.8-1.96199.9
1.96-2.14199.9
2.14-2.41100
2.4-2.81100

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.6.0117refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1xk4

1xk4


Resolution: 1.6→47.64 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.955 / SU B: 3.492 / SU ML: 0.059 / Cross valid method: THROUGHOUT / ESU R: 0.083 / ESU R Free: 0.082 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20182 6217 5 %RANDOM
Rwork0.17671 ---
obs0.17796 117923 98.36 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 24.05 Å2
Baniso -1Baniso -2Baniso -3
1-0.05 Å20 Å2-0 Å2
2---1.36 Å20 Å2
3---1.31 Å2
Refinement stepCycle: LAST / Resolution: 1.6→47.64 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6450 0 70 488 7008
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.026944
X-RAY DIFFRACTIONr_bond_other_d0.0010.024765
X-RAY DIFFRACTIONr_angle_refined_deg1.6841.9529361
X-RAY DIFFRACTIONr_angle_other_deg1.047311729
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.5075851
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.07325.496353
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.878151357
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.6341522
X-RAY DIFFRACTIONr_chiral_restr0.1220.2999
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.027723
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021340
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_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free13.51654
X-RAY DIFFRACTIONr_sphericity_bonded17.696548
LS refinement shellResolution: 1.6→1.64 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.303 401 -
Rwork0.289 7071 -
obs--84.75 %
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)
10.45320.0511-0.13171.298-0.07741.6629-0.0025-0.0590.09910.26280.1117-0.1401-0.0130.1709-0.10910.12150.0283-0.05660.1302-0.04330.0648-0.25437.2261.729
22.4713-0.7907-0.06097.9551-2.66353.4002-0.0175-0.06260.09950.30980.12010.406-0.0836-0.1627-0.10260.09780.03890.02170.1051-0.02370.0538-15.59335.094.697
30.7065-0.79690.44492.1994-0.81921.1488-0.0209-0.00230.05480.17750.07310.07240.08450.1064-0.05220.10990.0312-0.01990.0971-0.02090.0358-8.53130.458-2.605
49.8829-9.98815.326319.0769-4.031121.1916-0.2674-0.5204-0.49650.92620.88931.7012-0.4319-1.0582-0.62190.07880.05090.10880.08830.09210.2197-20.42448.527-8.203
56.3437-1.89940.359911.5392-2.603814.7093-0.1362-0.18120.42990.71280.15860.0983-0.9052-0.052-0.02240.13910.0101-0.01260.0498-0.04470.067-5.747.8660.601
61.0299-0.10980.48181.74820.03291.7327-0.0010.05090.059-0.21980.06320.0494-0.11170.0875-0.06220.1025-0.0228-0.00260.0537-0.00450.0809-6.59147.257-19.844
78.94191.9377-1.73523.36040.69031.7613-0.01210.2249-0.1211-0.42860.1201-0.08450.02290.1724-0.1080.1478-0.0013-0.0080.1048-0.01530.0281-3.49135.894-26.734
83.0283-1.071.57312.1135-0.45451.35160.00170.0510.0665-0.05730.0614-0.1915-0.00020.2489-0.06320.05640.0109-0.01190.1267-0.03590.05381.21934.62-12.146
92.3156-1.3831.2161.6558-0.78030.76130.05530.1115-0.115-0.16330.01740.05180.09870.1339-0.07270.12230.0141-0.03370.1047-0.00750.0449-9.28217.272-21.17
101.76290.1758-0.07463.9847-1.95843.74880.0272-0.094-0.19810.05890.10830.25220.116-0.1969-0.13550.0923-0.0194-0.05490.05990.04280.1017-21.20814.228-13.87
114.10343.5571-0.45936.6689-1.13251.60760.0842-0.1847-0.08050.341-0.0270.46670.1267-0.1668-0.05720.1108-0.0039-0.00650.05720.01020.1242-20.51423.933-8.992
121.203-1.95110.67515.3039-2.69731.7867-0.0968-0.0983-0.17720.22240.14860.3534-0.0288-0.0016-0.05180.14470.0336-0.00740.0910.01160.1044-11.72616.492-7.155
132.6245-1.06261.91682.6604-0.8852.25540.0278-0.0813-0.1320.1340.10250.11580.1541-0.0273-0.13030.12730.0488-0.00630.0896-0.00390.0524-1.3065.729-4.168
141.5945-0.2555-0.2671.63230.21591.1443-0.10720.00840.11760.14380.0958-0.24650.03880.15710.01140.10280.05-0.06750.1005-0.01630.06657.72115.145-4.331
151.3837-0.1185-0.34243.1541-1.92434.66660.0110.2680.1945-0.18640.021-0.2372-0.14860.1312-0.0320.08210.0102-0.00280.130.02980.0681-0.30323.313-20.983
1610.3054-3.90090.19266.3768-2.35266.25790.19431.73540.0472-0.3332-0.4781-0.30150.12170.68520.28380.12290.02530.0040.4030.01860.02230.94218.858-26.571
1720.3496-9.4319-7.98848.812610.207921.88060.54830.39570.8886-0.5631-0.2041-0.6269-0.90330.8547-0.34420.1203-0.0025-0.00180.12740.05230.0933-37.59248.203-46.609
181.3748-1.45111.08562.5104-1.39351.2676-0.01910.02490.03870.0480.0232-0.0609-0.03090.0088-0.0040.0950.0068-0.03660.0872-0.00230.057-30.50534.854-34.149
191.8959-2.1162-0.05745.3851-0.48680.7937-0.2052-0.1360.06690.60460.1229-0.1099-0.1456-0.04660.08230.17850.0436-0.0530.1071-0.02860.0245-34.78338.71-20.528
201.8007-1.84090.15543.7783-0.49970.6161-0.0941-0.109-0.1780.38960.11770.2483-0.0847-0.0294-0.02360.1270.0115-0.0010.07540.01930.0947-41.62833.541-26.033
2112.9756-0.7674.96653.8732-1.65318.0699-0.3296-0.23610.83540.49470.1353-0.5702-0.62690.09880.19440.14140.0117-0.06640.045-0.03930.1425-35.34148.116-28.624
221.9235-0.70160.00951.4872-0.25890.20810.02390.0739-0.0016-0.03410.00870.28310.0208-0.0146-0.03260.09250.0091-0.04250.05710.00620.1288-51.68647.678-41.018
232.70470.4748-1.43222.4277-1.32134.53490.12280.1925-0.1961-0.3572-0.00440.46980.12660.0764-0.11840.11550.0316-0.14520.053-0.0390.1846-55.21936.722-48.266
244.3448-1.2979-1.0061.91760.1680.26260.04910.2452-0.1897-0.1735-0.06930.22550.011-0.00690.02020.13560.0251-0.05260.1557-0.02270.0767-40.99934.916-42.063
251.7391-0.8608-0.18762.28310.3240.7159-0.04410.0862-0.3576-0.0317-0.04030.61750.0405-0.07970.08440.0354-0.0075-0.03620.0286-0.00610.2988-56.2917.454-36.815
263.0467-4.38910.007515.13480.15541.5564-0.2537-0.2654-0.4611.18110.14260.37710.1414-0.02560.11110.19190.02240.11850.08150.10740.2413-53.53418.31-21.179
271.082-1.0376-0.1473.00070.04770.5317-0.0192-0.067-0.23760.15370.01970.4551-0.00560.0412-0.00050.04980.0035-0.00270.03140.03790.1851-49.5323.848-30.249
2860.1835-2.4624-7.257310.9357-2.737232.0591-1.3331-2.8954-2.02611.07020.74940.15881.39080.55360.58370.28550.13240.03140.24820.27690.5068-39.5446.181-23.794
292.9876-0.00540.11512.26060.26940.0801-0.0103-0.0166-0.38290.09560.0793-0.00290.06280.0053-0.0690.08120.0084-0.0370.0207-0.00480.2119-37.3256.208-36.521
300.99690.43350.48992.7343-0.29471.21970.06830.227-0.2468-0.23290.0527-0.19660.03010.146-0.1210.06340.0345-0.0240.0774-0.04620.1437-31.59115.849-41.719
313.1531-1.53621.53172.7208-1.54482.01110.00370.28490.0316-0.3605-0.13930.25860.02470.07710.13560.10360.0285-0.1230.0715-0.04230.1815-49.80424.568-46.817
3221.0156-7.3431.26638.6517-0.72755.14590.40221.3776-0.3676-0.7325-0.63370.26010.2999-0.07070.23150.18080.0431-0.11660.1632-0.07020.1478-51.46819.803-52.104
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 43
2X-RAY DIFFRACTION2A44 - 56
3X-RAY DIFFRACTION3A57 - 83
4X-RAY DIFFRACTION4A84 - 89
5X-RAY DIFFRACTION5C4 - 10
6X-RAY DIFFRACTION6C11 - 49
7X-RAY DIFFRACTION7C50 - 70
8X-RAY DIFFRACTION8C71 - 111
9X-RAY DIFFRACTION9K1 - 31
10X-RAY DIFFRACTION10K32 - 46
11X-RAY DIFFRACTION11K47 - 62
12X-RAY DIFFRACTION12K63 - 89
13X-RAY DIFFRACTION13L4 - 37
14X-RAY DIFFRACTION14L38 - 82
15X-RAY DIFFRACTION15L83 - 102
16X-RAY DIFFRACTION16L103 - 112
17X-RAY DIFFRACTION17S1 - 4
18X-RAY DIFFRACTION18S5 - 31
19X-RAY DIFFRACTION19S32 - 50
20X-RAY DIFFRACTION20S51 - 89
21X-RAY DIFFRACTION21T4 - 10
22X-RAY DIFFRACTION22T11 - 49
23X-RAY DIFFRACTION23T50 - 70
24X-RAY DIFFRACTION24T71 - 112
25X-RAY DIFFRACTION25U1 - 43
26X-RAY DIFFRACTION26U44 - 56
27X-RAY DIFFRACTION27U57 - 82
28X-RAY DIFFRACTION28U83 - 87
29X-RAY DIFFRACTION29V4 - 41
30X-RAY DIFFRACTION30V42 - 82
31X-RAY DIFFRACTION31V83 - 103
32X-RAY DIFFRACTION32V104 - 112

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