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- PDB-7qzr: Structure of native leukocyte myeloperoxidase in complex with the... -

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Basic information

Entry
Database: PDB / ID: 7qzr
TitleStructure of native leukocyte myeloperoxidase in complex with the Staphyloccal Peroxidase Inhibitor SPIN from Staphylococcus aureus
Components
  • (Myeloperoxidase heavy ...) x 2
  • Exported protein
  • Myeloperoxidase light chain
KeywordsOXIDOREDUCTASE / Phagocytosis Innate Immune Response Inhibitor Complex
Function / homology
Function and homology information


myeloperoxidase / hypochlorous acid biosynthetic process / Events associated with phagocytolytic activity of PMN cells / phagocytic vesicle lumen / response to gold nanoparticle / response to yeast / respiratory burst involved in defense response / low-density lipoprotein particle remodeling / response to food / azurophil granule ...myeloperoxidase / hypochlorous acid biosynthetic process / Events associated with phagocytolytic activity of PMN cells / phagocytic vesicle lumen / response to gold nanoparticle / response to yeast / respiratory burst involved in defense response / low-density lipoprotein particle remodeling / response to food / azurophil granule / defense response to fungus / response to mechanical stimulus / removal of superoxide radicals / secretory granule / hydrogen peroxide catabolic process / defense response / peroxidase activity / azurophil granule lumen / heparin binding / response to oxidative stress / response to lipopolysaccharide / lysosome / defense response to bacterium / intracellular membrane-bounded organelle / chromatin binding / heme binding / Neutrophil degranulation / negative regulation of apoptotic process / extracellular space / extracellular exosome / extracellular region / nucleoplasm / nucleus / metal ion binding
Similarity search - Function
Haem peroxidase, animal-type / Haem peroxidase domain superfamily, animal type / Animal haem peroxidase / Animal heme peroxidase superfamily profile. / Peroxidases proximal heme-ligand signature. / Haem peroxidase superfamily
Similarity search - Domain/homology
HEME C / DI(HYDROXYETHYL)ETHER / PHOSPHATE ION / Exported protein / Myeloperoxidase
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.18 Å
AuthorsPfanzagl, V. / Brito, J.A.
Funding support Austria, 1items
OrganizationGrant numberCountry
Austrian Science FundP33997 Austria
CitationJournal: J.Biol.Chem. / Year: 2022
Title: The staphylococcal inhibitory protein SPIN binds to human myeloperoxidase with picomolar affinity but only dampens halide oxidation.
Authors: Leitgeb, U. / Furtmuller, P.G. / Hofbauer, S. / Brito, J.A. / Obinger, C. / Pfanzagl, V.
History
DepositionJan 31, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 26, 2022Provider: repository / Type: Initial release
Revision 1.1Nov 9, 2022Group: Database references / Category: citation / Item: _citation.journal_volume
Revision 2.0Dec 7, 2022Group: Advisory / Atomic model
Category: atom_site / atom_site_anisotrop / pdbx_validate_close_contact
Item: _atom_site_anisotrop.id
Revision 3.0Dec 21, 2022Group: Atomic model / Category: atom_site / atom_site_anisotrop / Item: _atom_site_anisotrop.id
Revision 4.0Nov 15, 2023Group: Atomic model / Data collection
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp_atom / chem_comp_bond
Item: _atom_site_anisotrop.id
Revision 4.1Jan 31, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Myeloperoxidase light chain
B: Myeloperoxidase heavy chain
C: Myeloperoxidase light chain
D: Myeloperoxidase heavy chain
E: Exported protein
F: Exported protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)160,75024
Polymers155,1016
Non-polymers5,64918
Water9,476526
1
A: Myeloperoxidase light chain
B: Myeloperoxidase heavy chain
E: Exported protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)80,60015
Polymers77,5513
Non-polymers3,04912
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19150 Å2
ΔGint-80 kcal/mol
Surface area25990 Å2
MethodPISA
2
C: Myeloperoxidase light chain
D: Myeloperoxidase heavy chain
F: Exported protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)80,1509
Polymers77,5513
Non-polymers2,6006
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area18410 Å2
ΔGint-78 kcal/mol
Surface area25920 Å2
MethodPISA
Unit cell
Length a, b, c (Å)112.085, 112.085, 249.949
Angle α, β, γ (deg.)90, 90, 90
Int Tables number96
Space group name H-MP43212

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Components

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Protein , 2 types, 4 molecules ACEF

#1: Protein Myeloperoxidase light chain


Mass: 12894.465 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: myeloperoxidase light chain / Source: (natural) Homo sapiens (human) / References: UniProt: P05164
#4: Protein Exported protein / Myeloperoxidase inhibitor SPIN / Peroxidase inhibitor


Mass: 11318.837 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria)
Gene: spn, BN1321_100004, BSG37_02260, BTN44_10620, DD547_00397, DQU54_02285, E3A28_06620, E3K14_02150, E4U00_13265, E5491_02175, ELP52_13680, EP54_01735, EQ90_14250, FA040_13280, G6X35_08925, G6X37_ ...Gene: spn, BN1321_100004, BSG37_02260, BTN44_10620, DD547_00397, DQU54_02285, E3A28_06620, E3K14_02150, E4U00_13265, E5491_02175, ELP52_13680, EP54_01735, EQ90_14250, FA040_13280, G6X35_08925, G6X37_02280, G6Y24_06940, GO788_14115, GO793_01255, GO814_02200, GO942_04205, GQX37_09010, GZ145_13040, HMPREF3211_00419, NCTC10654_00513, NCTC10702_00804, QU38_03305, RK64_02670, SAHC1335_03340, SAMEA1029536_02387, SAMEA103891420_01955, SAMEA103891454_02159, SAMEA2076468_01149, SAMEA2076503_02336, SAMEA2077334_02539, SAMEA2078260_02478, SAMEA2078588_01351, SAMEA2079501_02481, SAMEA2080344_01411, SAMEA2081063_02581, SAMEA4008569_02671, SAMEA70146418_02739
Production host: Escherichia coli (E. coli) / References: UniProt: A0A0D1H8K9

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Myeloperoxidase heavy ... , 2 types, 2 molecules BD

#2: Protein Myeloperoxidase heavy chain


Mass: 53337.266 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: myeloperoxidase heavy chain / Source: (natural) Homo sapiens (human) / References: UniProt: P05164
#3: Protein Myeloperoxidase heavy chain


Mass: 53337.266 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: myeloperoxidase heavy chain / Source: (natural) Homo sapiens (human) / References: UniProt: P05164

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Sugars , 2 types, 6 molecules

#5: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#6: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1056.964 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-3-4/a4-b1_a6-f1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE

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Non-polymers , 7 types, 538 molecules

#7: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H34FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#9: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#10: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca / Feature type: SUBJECT OF INVESTIGATION
#11: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#12: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#13: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 526 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.53 Å3/Da / Density % sol: 51.43 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 9
Details: 8% (w/V) PEG 20000, 0.1 M BICINE pH 9, 0.5% (V/V) Dioxane

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Data collection

DiffractionMean temperature: 213.15 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.873 Å
DetectorType: DECTRIS PILATUS3 X 2M / Detector: PIXEL / Date: Nov 18, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.873 Å / Relative weight: 1
ReflectionResolution: 2.18→19.814 Å / Num. obs: 68945 / % possible obs: 92.9 % / Redundancy: 7.63 %
Details: Some remarks regarding the mmCIF items written, the PDB Exchange Dictionary (PDBx/mmCIF) Version 5.0 supporting the data files in the current PDB archive (dictionary version 5.325, last ...Details: Some remarks regarding the mmCIF items written, the PDB Exchange Dictionary (PDBx/mmCIF) Version 5.0 supporting the data files in the current PDB archive (dictionary version 5.325, last updated 2020-04-13: http://mmcif.wwpdb.org/dictionaries/mmcif_pdbx_v50.dic/Index/) and the actual quantities provided by MRFANA (https://github.com/githubgphl/MRFANA) from the autoPROC package (https://www.globalphasing.com/autoproc/). In general, the mmCIF categories here should provide items that are currently used in the PDB archive. If there are alternatives, the one recommended by the PDB developers has been selected. The distinction between *_all and *_obs quantities is not always clear: often only one version is actively used within the PDB archive (or is the one recommended by PDB developers). The intention of distinguishing between classes of reflections before and after some kind of observation criterion was applied, can in principle be useful - but such criteria change in various ways throughout the data processing steps (rejection of overloaded or too partial reflections, outlier/misfit rejections during scaling etc) and there is no retrospect computation of data scaling/merging statistics for the reflections used in the final refinement (where another observation criterion might have been applied). Typical data processing will usually only provide one version of statistics at various stages and these are given in the recommended item here, irrespective of the "_all" and "_obs" connotation, see e.g. the use of _reflns.pdbx_Rmerge_I_obs, _reflns.pdbx_Rrim_I_all and _reflns.pdbx_Rpim_I_all. Please note that all statistics related to "merged intensities" (or "merging") are based on inverse-variance weighting of the individual measurements making up a symmetry-unique reflection. This is standard for several decades now, even if some of the dictionary definitions seem to suggest that a simple "mean" or "average" intensity is being used instead. R-values are always given for all symmetry-equivalent reflections following Friedel's law, i.e. Bijvoet pairs are not treated separately (since we want to describe the overall mean intensity and not the mean I(+) and I(-) here). The Rrim metric is identical to the Rmeas R-value and only differs in name. _reflns.pdbx_number_measured_all is the number of measured intensities just before the final merging step (at which point no additional rejection takes place). _reflns.number_obs is the number of symmetry-unique observations, i.e. the result of merging those measurements via inverse-variance weighting. _reflns.pdbx_netI_over_sigmaI is based on the merged intensities (_reflns.number_obs) as expected. _reflns.pdbx_redundancy is synonymous with "multiplicity". The per-shell item _reflns_shell.number_measured_all corresponds to the overall value _reflns.pdbx_number_measured_all. The per-shell item _reflns_shell.number_unique_all corresponds to the overall value _reflns.number_obs. The per-shell item _reflns_shell.percent_possible_all corresponds to the overall value _reflns.percent_possible_obs. The per-shell item _reflns_shell.meanI_over_sigI_obs corresponds to the overall value given as _reflns.pdbx_netI_over_sigmaI. But be aware of the incorrect definition of the former in the current dictionary!
CC1/2: 0.988 / CC1/2 anomalous: -0.08 / Rmerge(I) obs: 0.28 / Rpim(I) all: 0.1049 / Rrim(I) all: 0.2998 / AbsDiff over sigma anomalous: 0.728 / Baniso tensor eigenvalue 1: 23 Å2 / Baniso tensor eigenvalue 2: 23 Å2 / Baniso tensor eigenvalue 3: 38.4 Å2 / Baniso tensor eigenvector 1 ortho1: 1 / Baniso tensor eigenvector 1 ortho2: 0 / Baniso tensor eigenvector 1 ortho3: 0 / Baniso tensor eigenvector 2 ortho1: 0 / Baniso tensor eigenvector 2 ortho2: 1 / Baniso tensor eigenvector 2 ortho3: 0 / Baniso tensor eigenvector 3 ortho1: 0 / Baniso tensor eigenvector 3 ortho2: 0 / Baniso tensor eigenvector 3 ortho3: 1 / Aniso diffraction limit 1: 2.179 Å / Aniso diffraction limit 2: 2.179 Å / Aniso diffraction limit 3: 2.486 Å / Aniso diffraction limit axis 1 ortho1: 1 / Aniso diffraction limit axis 1 ortho2: 0 / Aniso diffraction limit axis 1 ortho3: 0 / Aniso diffraction limit axis 2 ortho1: 0 / Aniso diffraction limit axis 2 ortho2: 1 / Aniso diffraction limit axis 2 ortho3: 0 / Aniso diffraction limit axis 3 ortho1: 0 / Aniso diffraction limit axis 3 ortho2: 0 / Aniso diffraction limit axis 3 ortho3: 1 / Net I/σ(I): 6.19 / Num. measured all: 525797 / Observed signal threshold: 1.2 / Orthogonalization convention: pdb / % possible anomalous: 92.6 / % possible ellipsoidal: 92.9 / % possible ellipsoidal anomalous: 92.6 / % possible spherical: 82.4 / % possible spherical anomalous: 82 / Redundancy anomalous: 4 / Signal type: local
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. measured obsNum. unique allNum. unique obsCC1/2CC1/2 anomalousRpim(I) allRrim(I) allAbsDiff over sigma anomalous% possible anomalous% possible ellipsoidal% possible ellipsoidal anomalous% possible spherical% possible spherical anomalousRedundancy anomalous% possible all
6.422-19.8148.950.091614.783085030850344634460.997-0.3230.03180.09720.5711001001001001005.12100
5.085-6.4228.510.143812.012936529365344934490.99-0.0850.05210.15320.70599.999.999.999.999.94.6499.9
4.434-5.0858.780.130113.133024030240344634460.993-0.1430.04630.13840.6699.910099.910099.94.72100
4.02-4.4348.940.150312.533082730827344734470.991-0.0990.05330.15980.69399.999.999.999.999.94.7799.9
3.726-4.029.290.190611.313201232012344734470.987-0.1020.06620.20210.7221001001001001004.94100
3.501-3.7269.360.24639.753227632276344934490.982-0.1380.08550.26110.7411001001001001004.94100
3.323-3.5019.230.31218.323180931809344734470.976-0.0930.10850.3310.76499.999.999.999.999.94.8699.9
3.176-3.3239.120.40396.853141131411344634460.964-0.1130.14050.42830.7610099.810099.81004.7999.8
3.05-3.1768.80.49375.783036730367344934490.946-0.0640.17440.52450.76310099.910099.91004.6299.9
2.943-3.058.170.57784.862816128161344534450.924-0.1140.21260.61690.75599.899.899.899.899.84.2999.8
2.85-2.9437.550.66553.962602326023344834480.891-0.0420.25520.71450.74199.699.999.699.999.63.9599.9
2.767-2.857.20.7593.372480424804344734470.855-0.0560.29750.81750.72599.599.999.599.999.53.7799.9
2.693-2.7677.010.82933.082416424164344834480.831-0.0540.32870.89470.74999.599.899.599.899.53.6699.8
2.625-2.6936.790.92052.642342723427344834480.769-0.020.37010.99540.74299.599.399.599.399.53.5499.3
2.563-2.6256.560.99842.42262822628344734470.726-0.0440.41041.08310.7397.797.397.797.397.73.4197.3
2.505-2.5636.331.11162.142179421794344534450.649-0.0070.46891.21060.74295.79595.79595.73.2895
2.451-2.5055.911.15761.872040120401345034500.643-0.0110.50411.2670.72795.395.395.393.293.73.0895.3
2.397-2.4515.551.22851.691914119141344634460.59-0.0130.55421.35280.72993.394.193.385.4862.8994.1
2.327-2.3975.191.13351.691788817888344734470.537-0.0260.53991.26070.74773.173.673.159.960.52.6973.6
2.18-2.3275.281.21991.571820918209344834480.51200.5821.3550.75148.648.448.623.5242.7148.4

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Processing

Software
NameVersionClassification
autoPROC1.0.5 20210716data processing
Aimless0.7.4data scaling
STARANISO2.3.77data scaling
BUSTER2.10.4refinement
autoPROCdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5UZU

5uzu


Resolution: 2.18→19.81 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.899 / Cross valid method: THROUGHOUT / SU R Blow DPI: 0.336 / SU Rfree Blow DPI: 0.228
RfactorNum. reflection% reflectionSelection details
Rfree0.2438 3513 -RANDOM
Rwork0.2038 ---
obs0.2059 68945 82.4 %-
Displacement parametersBiso mean: 32.35 Å2
Baniso -1Baniso -2Baniso -3
1-0.0188 Å20 Å20 Å2
2--0.0188 Å20 Å2
3----0.0376 Å2
Refine analyzeLuzzati coordinate error obs: 0.29 Å
Refinement stepCycle: LAST / Resolution: 2.18→19.81 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10274 0 372 526 11172
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.00821382HARMONIC2
X-RAY DIFFRACTIONt_angle_deg0.9838609HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d6428SINUSOIDAL2
X-RAY DIFFRACTIONt_gen_planes3370HARMONIC5
X-RAY DIFFRACTIONt_it10930HARMONIC10
X-RAY DIFFRACTIONt_nbd1SEMIHARMONIC5
X-RAY DIFFRACTIONt_chiral_improper_torsion1428SEMIHARMONIC5
X-RAY DIFFRACTIONt_ideal_dist_contact16181SEMIHARMONIC4
X-RAY DIFFRACTIONt_omega_torsion3.26
X-RAY DIFFRACTIONt_other_torsion14.98
LS refinement shellResolution: 2.18→2.26 Å
RfactorNum. reflection% reflection
Rfree0.2809 68 -
Rwork0.2776 --
obs0.2777 1379 17.17 %
Refinement TLS params.

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)
11.7776-0.64150.71720.20011.93254.1293-0.00240.26780.08760.26780.0760.25450.08760.2545-0.0736-0.0586-0.0388-0.0461-0.03130.0213-0.086626.63516.223243.0429
20.2227-0.0838-0.00810.59370.04790.326-0.00750.0132-0.02370.0132-0.00080.0044-0.02370.00440.0084-0.0654-0.0049-0.0278-0.03270.0191-0.03895.6501-4.866723.0563
30.2836-0.0757-0.01750.35920.01740.2680.04460.03870.01190.0387-0.02180.0570.01190.057-0.0229-0.0465-0.0132-0.025-0.03230.0199-0.02668.0376-16.134823.3097
40.251-0.1515-0.11320.49090.07550.5332-0.0238-0.00430.0669-0.00430.0121-0.01770.0669-0.01770.0117-0.064-0.0137-0.0079-0.0610.0278-0.00770.827-52.689543.6447
50.5579-0.0428-0.13840.72940.01030.47610.0169-0.0182-0.0125-0.0182-0.03420.044-0.01250.0440.0173-0.0624-0.0024-0.0166-0.06150.0376-0.0432.513-41.387244.4916
62.7038-1.0024-1.16521.88811.34042.3146-0.0393-0.2156-0.0283-0.21560.09110.4019-0.02830.4019-0.0518-0.25010.04790.018-0.07150.0250.132629.8472-63.649337.933
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{ E|* }E33 - 102
2X-RAY DIFFRACTION2{ B|* }B279 - 744
3X-RAY DIFFRACTION2{ B|* }B1000 - 7000
4X-RAY DIFFRACTION3{ A|* }A167 - 271
5X-RAY DIFFRACTION3{ A|* }A5000
6X-RAY DIFFRACTION4{ D|* }D279 - 743
7X-RAY DIFFRACTION4{ D|* }D1000 - 4000
8X-RAY DIFFRACTION5{ C|* }C167 - 271
9X-RAY DIFFRACTION5{ C|* }C5000
10X-RAY DIFFRACTION6{ F|* }F35 - 103

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