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- PDB-5jdu: Crystal structure for human thrombin mutant D189A -

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Basic information

Entry
Database: PDB / ID: 5jdu
TitleCrystal structure for human thrombin mutant D189A
Components
  • Thrombin heavy chain
  • Thrombin light chain
KeywordsHYDROLASE / Serine protease / Coagulation / conformational equilibrium
Function / homology
Function and homology information


positive regulation of lipid kinase activity / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / cytolysis by host of symbiont cells / thrombospondin receptor activity / Defective factor XII causes hereditary angioedema / thrombin / neutrophil-mediated killing of gram-negative bacterium / regulation of blood coagulation / ligand-gated ion channel signaling pathway / Defective F8 cleavage by thrombin ...positive regulation of lipid kinase activity / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / cytolysis by host of symbiont cells / thrombospondin receptor activity / Defective factor XII causes hereditary angioedema / thrombin / neutrophil-mediated killing of gram-negative bacterium / regulation of blood coagulation / ligand-gated ion channel signaling pathway / Defective F8 cleavage by thrombin / Platelet Aggregation (Plug Formation) / negative regulation of platelet activation / negative regulation of astrocyte differentiation / positive regulation of collagen biosynthetic process / negative regulation of cytokine production involved in inflammatory response / positive regulation of blood coagulation / negative regulation of fibrinolysis / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins / fibrinolysis / regulation of cytosolic calcium ion concentration / Intrinsic Pathway of Fibrin Clot Formation / Peptide ligand-binding receptors / positive regulation of release of sequestered calcium ion into cytosol / Regulation of Complement cascade / acute-phase response / Cell surface interactions at the vascular wall / lipopolysaccharide binding / negative regulation of proteolysis / positive regulation of receptor signaling pathway via JAK-STAT / growth factor activity / positive regulation of insulin secretion / platelet activation / response to wounding / Golgi lumen / positive regulation of protein localization to nucleus / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of reactive oxygen species metabolic process / blood coagulation / antimicrobial humoral immune response mediated by antimicrobial peptide / Thrombin signalling through proteinase activated receptors (PARs) / heparin binding / regulation of cell shape / positive regulation of cell growth / G alpha (q) signalling events / collagen-containing extracellular matrix / blood microparticle / cell surface receptor signaling pathway / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / signaling receptor binding / serine-type endopeptidase activity / calcium ion binding / positive regulation of cell population proliferation / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / Thrombin light chain / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. ...Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / Thrombin light chain / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain superfamily / Vitamin K-dependent carboxylation domain. / Gla domain profile. / Domain containing Gla (gamma-carboxyglutamate) residues. / Kringle-like fold / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsPozzi, N. / Chen, Z. / Di Cera, E.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)HL049413 United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)HL073813 United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)HL112303 United States
Citation
Journal: Biochemistry / Year: 2016
Title: Loop Electrostatics Asymmetry Modulates the Preexisting Conformational Equilibrium in Thrombin.
Authors: Pozzi, N. / Zerbetto, M. / Acquasaliente, L. / Tescari, S. / Frezzato, D. / Polimeno, A. / Gohara, D.W. / Di Cera, E. / De Filippis, V.
#1: Journal: JBC / Year: 2004
Title: Molecular dissection of Na+ binding to thrombin
Authors: Pineda, A.O. / Carrell, C.J. / Bush, L.A. / Prasad, S. / Caccia, S. / Chen, Z.W. / Mathews, F.S. / Di Cera, E.
History
DepositionApr 17, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 13, 2016Provider: repository / Type: Initial release
Revision 1.1Aug 10, 2016Group: Database references
Revision 1.2Sep 27, 2017Group: Author supporting evidence / Database references / Derived calculations
Category: citation / pdbx_audit_support / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_mod_residue / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_mod_residue.auth_asym_id / _pdbx_struct_mod_residue.auth_seq_id / _pdbx_struct_mod_residue.label_asym_id / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Thrombin light chain
B: Thrombin heavy chain
C: Thrombin light chain
D: Thrombin heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,0318
Polymers67,0554
Non-polymers9764
Water11,205622
1
A: Thrombin light chain
B: Thrombin heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)33,9523
Polymers33,5272
Non-polymers4241
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2880 Å2
ΔGint-1 kcal/mol
Surface area13030 Å2
MethodPISA
2
C: Thrombin light chain
D: Thrombin heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,0795
Polymers33,5272
Non-polymers5523
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3090 Å2
ΔGint-15 kcal/mol
Surface area13560 Å2
MethodPISA
Unit cell
Length a, b, c (Å)55.429, 81.333, 146.366
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein/peptide / Protein / Sugars , 3 types, 6 molecules ACBD

#1: Protein/peptide Thrombin light chain / / Coagulation factor II


Mass: 3791.204 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: F2 / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P00734, thrombin
#2: Protein Thrombin heavy chain / / Coagulation factor II


Mass: 29736.211 Da / Num. of mol.: 2 / Mutation: D189A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: F2 / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P00734, thrombin
#3: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-6DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a6-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(6+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE

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Non-polymers , 3 types, 624 molecules

#4: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 622 / 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: 2.29 Å3/Da / Density % sol: 46.3 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.9 / Details: 200 mM KCl and 20% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 14, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 1.7→40 Å / Num. obs: 74112 / % possible obs: 99.9 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 8.5 % / Rmerge(I) obs: 0.105 / Net I/σ(I): 18.2
Reflection shellResolution: 1.7→1.74 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.394 / Mean I/σ(I) obs: 3.2 / % possible all: 99.8

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Processing

Software
NameVersionClassification
REFMAC5.5.0109refinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ID 1SHH

1shh


Resolution: 1.7→40 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.953 / SU B: 4.087 / SU ML: 0.062 / Cross valid method: THROUGHOUT / σ(F): -3 / ESU R: 0.101 / ESU R Free: 0.097 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.206 3729 5.1 %RANDOM
Rwork0.18077 ---
obs0.18203 70070 98.86 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å
Displacement parametersBiso mean: 27.943 Å2
Baniso -1Baniso -2Baniso -3
1-0.04 Å20 Å20 Å2
2--0.09 Å20 Å2
3----0.13 Å2
Refinement stepCycle: 1 / Resolution: 1.7→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4456 0 63 622 5141
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0224658
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.3771.9766291
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2845547
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.25423.028218
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.0315826
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.2051542
X-RAY DIFFRACTIONr_chiral_restr0.1040.2661
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0213516
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_it0.6261.52742
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.18224420
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.98631916
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.1884.51869
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.692→1.736 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.28 255 -
Rwork0.247 4654 -
obs--89.69 %
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)
19.0468-0.16-0.02765.85211.5855.7054-0.1282-0.7402-0.0640.5835-0.0587-0.2009-0.07720.52470.1870.1273-0.0174-0.02620.12230.00190.211234.93116.064637.3995
210.3533-4.87513.08245.8842-2.55163.8703-0.10470.43430.5203-0.281-0.1067-0.6369-0.26630.46250.21130.1727-0.07720.02770.1457-0.00450.183733.392722.446723.9664
32.81510.6031.20230.23150.02127.6972-0.00440.6906-0.2687-0.14390.1421-0.1203-0.08560.535-0.13770.2272-0.00310.0760.1775-0.06380.197529.89149.157823.8943
43.04291.40670.37487.91880.45533.3827-0.03560.1197-0.3085-0.44270.0558-0.00040.17830.0316-0.02020.05640.0184-0.01390.0251-0.00980.126122.1532-0.687735.6271
54.69010.71891.41570.95870.36871.4343-0.0167-0.1973-0.2944-0.0107-0.0161-0.03050.1666-0.23350.03280.1153-0.0101-0.00460.049-0.00930.085914.0882-0.522237.6868
64.2768-1.92-1.37933.35830.09162.1093-0.09230.1652-0.3213-0.1917-0.1058-0.24730.25420.0580.19810.142-0.0224-0.040.0996-0.00380.167926.5094-0.541637.2661
74.92240.0609-0.1132.4104-0.5462.75150.0309-0.2886-0.1472-0.016-0.04630.02770.0605-0.24190.01530.08760.0063-0.0220.0492-0.00750.036717.70187.78739.2051
82.3501-0.9425-0.2563.00420.53213.6341-0.07380.0496-0.0246-0.14780.02710.0996-0.10440.01830.04670.0571-0.0303-0.00450.05850.00840.116322.596917.881228.1978
94.82630.3915-0.58351.3964-0.09982.1685-0.1290.22920.3475-0.18030.10740.2344-0.268-0.33630.02160.16130.0186-0.060.0880.00550.12998.220219.7723.7116
1055.5333-0.5975.71050.0351-0.147214.2310.23974.52932.1699-0.1905-0.115-0.049-0.11080.5023-0.12471.27710.00770.16180.61650.15640.303317.336517.665810.6233
112.73060.56960.53821.4538-0.15161.5245-0.06410.1583-0.0315-0.13560.0927-0.069-0.0592-0.077-0.02850.08720.0007-0.00990.02010.00370.05217.939215.31627.5996
123.439-1.87043.91366.9903-5.873813.91050.0669-0.11390.05380.2077-0.0592-0.0568-0.15680.2454-0.00770.067-0.0019-0.00260.0831-0.03220.053216.01514.333148.6786
137.7834-4.32422.12488.0129-2.45016.7010.17770.5004-0.1023-0.6153-0.0848-0.29010.01470.689-0.09280.0631-0.04640.0140.17990.02970.075636.996218.228670.2977
143.38150.23953.63292.34110.70688.5003-0.1045-0.1290.3315-0.0859-0.02110.1416-0.413-0.25950.12560.0542-0.00290.01020.08050.03630.139832.940124.830381.8705
151.3899-0.38480.18833.657-0.69641.8366-0.01170.0883-0.0675-0.1177-0.00140.26520.1645-0.1070.01310.03820.0052-0.01360.10260.00380.040627.68323.259575.8189
160.90570.5969-0.45433.5362-2.70034.0621-0.0160.0021-0.1302-0.3295-0.07830.04920.6323-0.02860.09440.1364-0.0040.00870.1056-0.01780.108827.7379-10.137777.6039
175.7768-1.49892.33523.1232-0.88783.5728-0.02480.1512-0.3407-0.24030.02650.16490.26580.0588-0.00170.07410.0074-0.0130.10170.01310.057219.78469.662164.2258
181.5534-0.00950.73644.0755-1.3643.63550.06880.0686-0.1937-0.2965-0.115-0.13090.4910.18310.04620.07430.04060.02210.1135-0.00030.073336.3064-2.44376.5151
197.9942-2.1693-5.09466.92546.11249.69950.1527-0.42180.2070.14850.0789-0.5252-0.10250.9288-0.23160.076-0.0228-0.03990.19650.06630.149846.392812.436686.984
202.5114-0.71933.22481.3297-0.49066.64850.1571-0.2214-0.10420.0795-0.10.13830.1315-0.4009-0.05710.0363-0.01930.0210.06620.01410.060726.873411.682786.4557
2110.5908-1.926-7.54484.19640.44099.3552-0.1291-0.5268-0.26860.27760.0559-0.12950.2550.48620.07320.0857-0.0045-0.04820.09720.04560.076735.04780.145499.6323
2212.3516-7.9161-6.346810.09972.59537.5091-0.047-0.41260.21810.48750.06270.2341-0.2035-0.0756-0.01570.0705-0.03370.00250.0779-0.01630.067729.618412.172195.7901
232.40851.8703-0.39584.7695-0.99271.67210.0397-0.14280.15170.2394-0.02750.1739-0.1358-0.0416-0.01220.02640.0025-0.00250.060.01280.024732.820912.857785.7998
244.9005-1.3541-3.45072.66391.38455.4251-0.02350.1418-0.16560.025-0.0562-0.14730.23590.1430.07970.05410.0009-0.02110.06860.03740.060936.78250.920786.93
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 8
2X-RAY DIFFRACTION2A9 - 14
3X-RAY DIFFRACTION3B16 - 29
4X-RAY DIFFRACTION4B30 - 50
5X-RAY DIFFRACTION5B51 - 69
6X-RAY DIFFRACTION6B70 - 92
7X-RAY DIFFRACTION7B93 - 121
8X-RAY DIFFRACTION8B122 - 159
9X-RAY DIFFRACTION9B160 - 185
10X-RAY DIFFRACTION10B186 - 188
11X-RAY DIFFRACTION11B189 - 232
12X-RAY DIFFRACTION12B233 - 247
13X-RAY DIFFRACTION13C1 - 8
14X-RAY DIFFRACTION14C9 - 14
15X-RAY DIFFRACTION15D16 - 59
16X-RAY DIFFRACTION16D60 - 68
17X-RAY DIFFRACTION17D69 - 81
18X-RAY DIFFRACTION18D82 - 122
19X-RAY DIFFRACTION19D123 - 131
20X-RAY DIFFRACTION20D132 - 167
21X-RAY DIFFRACTION21D168 - 180
22X-RAY DIFFRACTION22D181 - 185
23X-RAY DIFFRACTION23D186 - 213
24X-RAY DIFFRACTION24D214 - 245

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