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- PDB-4dt7: Crystal structure of thrombin bound to the activation domain QEDQ... -

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Basic information

Entry
Database: PDB / ID: 4dt7
TitleCrystal structure of thrombin bound to the activation domain QEDQVDPRLIDGKMTRRGDS of protein C
Components
  • Thrombin heavy chain
  • Thrombin light chain
  • Vitamin K-dependent protein C
KeywordsHYDROLASE / Serine protease
Function / homology
Function and homology information


protein C (activated) / positive regulation of establishment of endothelial barrier / negative regulation of coagulation / negative regulation of blood coagulation / 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 ...protein C (activated) / positive regulation of establishment of endothelial barrier / negative regulation of coagulation / negative regulation of blood coagulation / 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 / regulation of blood coagulation / neutrophil-mediated killing of gram-negative bacterium / ligand-gated ion channel signaling pathway / Defective F8 cleavage by thrombin / Platelet Aggregation (Plug Formation) / negative regulation of astrocyte differentiation / negative regulation of platelet activation / 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 / acute-phase response / Regulation of Complement cascade / negative regulation of proteolysis / Cell surface interactions at the vascular wall / lipopolysaccharide binding / Post-translational protein phosphorylation / positive regulation of receptor signaling pathway via JAK-STAT / growth factor activity / positive regulation of insulin secretion / platelet activation / negative regulation of inflammatory response / response to wounding / positive regulation of protein localization to nucleus / Golgi lumen / antimicrobial humoral immune response mediated by antimicrobial peptide / 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 / 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 / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell surface receptor signaling pathway / blood microparticle / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / serine-type endopeptidase activity / signaling receptor binding / calcium ion binding / positive regulation of cell population proliferation / negative regulation of apoptotic process / Golgi apparatus / endoplasmic reticulum / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Peptidase S1A, coagulation factor VII/IX/X/C/Z / Coagulation factor-like, Gla domain superfamily / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / Thrombin light chain / Coagulation Factor Xa inhibitory site / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. ...Peptidase S1A, coagulation factor VII/IX/X/C/Z / Coagulation factor-like, Gla domain superfamily / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / Thrombin light chain / Coagulation Factor Xa inhibitory site / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / 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. / Epidermal growth factor-like domain. / Kringle-like fold / EGF-like domain profile. / EGF-like domain signature 2. / EGF-like domain signature 1. / EGF-like domain / 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
ACETATE ION / DI(HYDROXYETHYL)ETHER / Prothrombin / Vitamin K-dependent protein C
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsPozzi, N. / Barranco-Medina, S. / Chen, Z. / Di Cera, E.
Citation
Journal: Blood / Year: 2012
Title: Exposure of R169 controls protein C activation and autoactivation.
Authors: Pozzi, N. / Barranco-Medina, S. / Chen, Z. / Di Cera, E.
#1: Journal: J.Biol.Chem. / 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. / Mahews, F.S. / Di Cera, E.
History
DepositionFeb 20, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 9, 2012Provider: repository / Type: Initial release
Revision 1.1Aug 15, 2012Group: Database references
Revision 1.2Sep 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_PDB_ins_code / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_PDB_ins_code / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_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_PDB_ins_code / _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: Thrombin light chain
B: Thrombin heavy chain
C: Thrombin light chain
D: Thrombin heavy chain
E: Vitamin K-dependent protein C
F: Vitamin K-dependent protein C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,84811
Polymers71,5786
Non-polymers2705
Water5,873326
1
A: Thrombin light chain
B: Thrombin heavy chain
E: Vitamin K-dependent protein C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)35,9776
Polymers35,7893
Non-polymers1883
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3940 Å2
ΔGint-21 kcal/mol
Surface area13280 Å2
MethodPISA
2
C: Thrombin light chain
D: Thrombin heavy chain
F: Vitamin K-dependent protein C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)35,8715
Polymers35,7893
Non-polymers822
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3970 Å2
ΔGint-26 kcal/mol
Surface area13440 Å2
MethodPISA
Unit cell
Length a, b, c (Å)46.395, 84.272, 66.363
Angle α, β, γ (deg.)90.00, 94.59, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein/peptide , 2 types, 4 molecules ACEF

#1: Protein/peptide Thrombin light chain


Mass: 3704.126 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: F2, Human / Production host: Escherichia coli (E. coli) / References: UniProt: P00734, thrombin
#3: Protein/peptide Vitamin K-dependent protein C / Anticoagulant protein C / Autoprothrombin IIA / Blood coagulation factor XIV / Vitamin K-dependent ...Anticoagulant protein C / Autoprothrombin IIA / Blood coagulation factor XIV / Vitamin K-dependent protein C light chain / Vitamin K-dependent protein C heavy chain / Activation peptide


Mass: 2320.541 Da / Num. of mol.: 2 / Fragment: UNP residues 204-223 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P04070, protein C (activated)

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Protein , 1 types, 2 molecules BD

#2: Protein Thrombin heavy chain


Mass: 29764.219 Da / Num. of mol.: 2 / Mutation: S195A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: F2, Human / Production host: Escherichia coli (E. coli) / References: UniProt: P00734, thrombin

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Non-polymers , 4 types, 331 molecules

#4: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#5: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#6: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 326 / 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: 1.84 Å3/Da / Density % sol: 33.04 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 0.1 M Tris, pH 8.5, 0.2 M Na acetate, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Jul 28, 2011
RadiationMonochromator: Mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.9→40 Å / Num. all: 39759 / Num. obs: 38884 / % possible obs: 97.8 % / Observed criterion σ(F): -0.7 / Observed criterion σ(I): -0.7 / Redundancy: 3.6 % / Rsym value: 0.083 / Net I/σ(I): 13.4
Reflection shell
Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. unique allRsym valueDiffraction-ID% possible all
1.9-1.932.62.416060.34181.1
1.93-1.972.92.918860.32195.5
1.97-2.012.93.419700.274197
2.01-2.053418770.256197.7
2.05-2.093.14.719610.228197.9
2.09-2.143.25.619270.2198.7

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Processing

Software
NameVersionClassification
CrystalCleardata collection
MOLREPfrom ccp4phasing
REFMAC5.5.0109refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1SHH

1shh


Resolution: 1.9→35.7 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.938 / SU B: 8.189 / SU ML: 0.109 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.19 / ESU R Free: 0.158 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21773 1953 5 %RANDOM
Rwork0.17554 ---
obs0.1777 36856 97.26 %-
all-37894 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 30.42 Å2
Baniso -1Baniso -2Baniso -3
1--0.02 Å20 Å20 Å2
2--0.05 Å20 Å2
3----0.03 Å2
Refinement stepCycle: LAST / Resolution: 1.9→35.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4737 0 17 326 5080
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0224866
X-RAY DIFFRACTIONr_angle_refined_deg1.2491.9656562
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.3075578
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.36623.418237
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.26215868
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.1091544
X-RAY DIFFRACTIONr_chiral_restr0.0940.2677
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0213716
X-RAY DIFFRACTIONr_mcbond_it0.4931.52915
X-RAY DIFFRACTIONr_mcangle_it0.92524686
X-RAY DIFFRACTIONr_scbond_it1.52931951
X-RAY DIFFRACTIONr_scangle_it2.4554.51876
LS refinement shellResolution: 1.9→1.953 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.298 130 -
Rwork0.242 2203 -
obs-2203 79.19 %
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)
16.93593.73551.47895.4710.50173.45870.0626-0.48230.71690.5159-0.13960.6221-0.2317-0.73840.07710.10760.01940.00080.29070.04420.1635-2.5914-3.384739.1819
212.4121-4.3165-6.555314.27366.619415.0561-0.18380.1215-0.3843-0.0141-0.00560.83960.117-0.98760.18940.0565-0.0588-0.03620.25010.110.1251-4.689-13.345738.4527
34.89290.01483.79844.4439-2.09677.1767-0.01590.1513-0.3576-0.21840.0987-0.00240.31920.116-0.08280.1153-0.02160.02440.0287-0.0090.055411.385-17.519540.8434
42.3012-0.2495-1.86763.54080.98722.0038-0.20860.2283-0.1502-0.31130.18080.10540.3085-0.30350.02790.2085-0.1159-0.08120.21330.03020.05965.8136-7.593125.8531
52.6368-2.17528.41832.0011-6.762227.04230.04040.0429-0.1152-0.32250.13890.2448-0.40610.1829-0.17930.6602-0.0259-0.14480.53570.14910.29877.22184.44713.674
61.15542.0499-0.01974.0259-0.45950.4662-0.0273-0.06380.17660.10060.14870.4058-0.1439-0.2995-0.12150.06020.07920.00530.21240.08830.09915.74537.854230.3246
72.74970.9893-0.37761.2544-0.31120.5153-0.01550.34930.1848-0.17520.14970.2358-0.0218-0.377-0.13420.18870.0111-0.00530.29680.09620.14354.60467.144721.0786
87.83451.0758-2.89993.8995-1.28413.3719-0.0441-0.20780.050.28080.0188-0.2247-0.20860.28290.02530.0785-0.0226-0.00420.0346-0.01570.034819.397712.011929.3454
91.8088-0.36880.00141.4901-0.89942.264-0.06340.03850.14820.10780.1220.0467-0.1633-0.2192-0.05860.0523-0.01130.00640.05080.0230.0526.9074-2.127236.3181
103.16140.39680.73861.74660.44894.4044-0.2090.16930.1096-0.2676-0.1049-0.20220.09720.26340.31390.11170.01310.04350.0340.04190.078120.2364-7.711127.7597
113.3215-0.01720.2642.3939-0.70272.0024-0.12030.1073-0.0546-0.0973-0.0737-0.39680.21770.4220.1940.10340.01190.03480.10850.02630.094624.2979-5.854930.804
121.63050.2245-0.67141.7896-1.04912.6556-0.0435-0.0142-0.0202-0.02480.0214-0.13560.05930.08780.02220.0152-0.0106-0.01510.01670.01040.031515.5257-3.699134.7362
1313.8376-4.62921.430510.1781-0.92824.6579-0.2168-0.35430.51220.47060.27330.206-0.5662-0.2606-0.05650.2533-0.00650.06430.10180.00230.11439.53914.369739.6727
147.3901-0.6935-0.85399.46432.80138.93130.02780.465-0.1999-0.4272-0.04080.2160.1162-0.2420.0130.0267-0.0023-0.01060.07430.01340.02470.8822-21.9384-9.3001
1523.413314.7560.177732.0148-1.125317.2701-0.1324-0.18140.7443-0.6802-0.52080.4461-0.1564-0.60480.65310.07490.0871-0.01310.1710.03030.1166-2.5212-14.2743-10.9007
168.89071.3796-5.85942.6238-1.03515.56460.01420.03180.540.1456-0.00130.0313-0.30940.0057-0.0130.09120.004-0.05350.01550.00840.103715.1256-10.1271-9.1158
172.2932-0.63881.00441.83670.69241.8573-0.0549-0.1866-0.00790.28520.10660.1721-0.0841-0.1805-0.05170.10230.05280.06120.06940.0030.06435.9794-23.25857.3513
184.2422-0.8020.90643.612-0.06122.09860.0324-0.2144-0.21940.2854-0.03050.24320.1912-0.2468-0.00180.0415-0.0240.02510.03950.02430.09497.265-34.13774.8459
195.5502-2.6740.95881.3514-0.32010.6012-0.1689-0.5109-0.13830.12740.20030.0739-0.0749-0.2397-0.03140.2160.02560.0280.13330.06310.15228.5286-35.113912.4254
200.9763-3.2278-2.079810.79726.92864.4580.27160.2464-0.08790.1908-0.76380.28910.0383-0.62540.49220.8712-0.1386-0.12730.8392-0.08920.8331-5.9876-21.762311.6366
213.2732-1.06751.24451.8384-0.99481.76370.0827-0.135-0.37280.00070.01870.20680.204-0.0806-0.10140.05-0.01290.00460.0247-0.01480.09249.5261-37.32211.7489
221.873-0.1669-0.96971.78720.37833.089-0.05360.0251-0.0823-0.00140.0001-0.05350.0840.11450.05350.00590.0007-0.00830.00740.00530.047217.4849-21.961-2.9089
235.5255-1.1735-0.94662.1760.6061.1384-0.0786-0.1739-0.13280.14630.0397-0.17650.11550.15740.03890.04670.0048-0.01050.03140.01370.029324.2885-22.07233.1286
242.2082-0.02740.58371.8423-0.2142.07550.0171-0.04030.0390.1066-0.01-0.1919-0.06660.1153-0.00710.0121-0.0038-0.00390.0092-0.00080.029620.3236-22.5998-0.104
2516.99098.4874-4.860512.1463-5.777110.7271-0.14940.6392-0.5038-0.70190.12740.19950.3945-0.13380.0220.10910.0368-0.03120.0449-0.01950.084715.2328-39.8349-7.7949
2610.2581-2.0248-2.936812.3195-4.79833.2728-0.27931.1123-1.5309-0.9576-0.13690.30860.5906-0.37480.41620.6478-0.1145-0.08910.5315-0.14520.64455.257-46.1178-7.4535
275.29334.6576-2.240514.6914-4.0973.1123-0.3260.0315-0.0988-1.2581-0.0329-1.37040.18160.70850.35890.2398-0.01440.05120.3120.02260.250526.56852.88720.2686
283.5849-6.45365.394614.0991-5.034921.4713-0.1358-0.08820.05960.8926-0.0342-0.42450.76550.7960.170.3377-0.1019-0.03380.4230.1660.292725.084-30.598613.8058
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 6
2X-RAY DIFFRACTION2A7 - 12
3X-RAY DIFFRACTION3A13 - 15
4X-RAY DIFFRACTION4B16 - 34
5X-RAY DIFFRACTION5B35 - 43
6X-RAY DIFFRACTION6B44 - 59
7X-RAY DIFFRACTION7B60 - 92
8X-RAY DIFFRACTION8B93 - 107
9X-RAY DIFFRACTION9B108 - 144
10X-RAY DIFFRACTION10B145 - 172
11X-RAY DIFFRACTION11B173 - 194
12X-RAY DIFFRACTION12B195 - 232
13X-RAY DIFFRACTION13B233 - 246
14X-RAY DIFFRACTION14C1 - 8
15X-RAY DIFFRACTION15C9 - 12
16X-RAY DIFFRACTION16C13 - 15
17X-RAY DIFFRACTION17D16 - 37
18X-RAY DIFFRACTION18D38 - 59
19X-RAY DIFFRACTION19D60 - 73
20X-RAY DIFFRACTION20D74 - 81
21X-RAY DIFFRACTION21D82 - 123
22X-RAY DIFFRACTION22D124 - 147
23X-RAY DIFFRACTION23D150 - 175
24X-RAY DIFFRACTION24D176 - 232
25X-RAY DIFFRACTION25D233 - 241
26X-RAY DIFFRACTION26D242 - 247
27X-RAY DIFFRACTION27E34 - 41
28X-RAY DIFFRACTION28F34 - 42

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