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- PDB-5fgc: Three dimensional structure of broadly neutralizing human anti - ... -

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Basic information

Entry
Database: PDB / ID: 5fgc
TitleThree dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC33.8
Components
  • Anti-HCV E2 Fab HC33.8 heavy chain
  • Anti-HCV E2 Fab HC33.8 light chain
  • Genome polyprotein
KeywordsVIRAL PROTEIN / Fab fragment / neutralizing antibody / Hepatitis C virus E2
Function / homology
Function and homology information


positive regulation of hexokinase activity / modulation by virus of host cellular process / translocation of peptides or proteins into host cell cytoplasm / Toll-like receptor 2 binding / viral capsid assembly / adhesion receptor-mediated virion attachment to host cell / TBC/RABGAPs / hepacivirin / host cell mitochondrial membrane / host cell lipid droplet ...positive regulation of hexokinase activity / modulation by virus of host cellular process / translocation of peptides or proteins into host cell cytoplasm / Toll-like receptor 2 binding / viral capsid assembly / adhesion receptor-mediated virion attachment to host cell / TBC/RABGAPs / hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / transformation of host cell by virus / positive regulation of cytokinesis / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / negative regulation of protein secretion / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / endoplasmic reticulum-Golgi intermediate compartment membrane / SH3 domain binding / kinase binding / : / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / clathrin-dependent endocytosis of virus by host cell / viral nucleocapsid / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / entry receptor-mediated virion attachment to host cell / RNA helicase activity / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / RNA helicase / induction by virus of host autophagy / ribonucleoprotein complex / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / viral envelope / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / structural molecule activity / host cell plasma membrane / virion membrane / negative regulation of transcription by RNA polymerase II / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding
Similarity search - Function
Hepatitis C virus core protein, chain A superfamily / Hepatitus C virus, Non-structural 5a protein, C-terminal / Hepatitis C virus NS5A, 1B domain superfamily / Hepatitis C virus non-structural protein NS2, C-terminal domain / Hepatitis C virus non-structural protein NS2, N-terminal domain / Hepatitis C virus non-structural protein NS2 / HCV NS5a protein C-terminal region / Hepatitis C virus, Non-structural protein NS4b / Hepatitis C virus, Core protein, N-terminal / Hepatitis C virus non-structural protein NS4b ...Hepatitis C virus core protein, chain A superfamily / Hepatitus C virus, Non-structural 5a protein, C-terminal / Hepatitis C virus NS5A, 1B domain superfamily / Hepatitis C virus non-structural protein NS2, C-terminal domain / Hepatitis C virus non-structural protein NS2, N-terminal domain / Hepatitis C virus non-structural protein NS2 / HCV NS5a protein C-terminal region / Hepatitis C virus, Non-structural protein NS4b / Hepatitis C virus, Core protein, N-terminal / Hepatitis C virus non-structural protein NS4b / Hepatitis C virus capsid protein / Hepatitis C virus, Non-structural protein NS2 / Hepatitis C virus, Non-structural 5a protein / Hepatitis C virus, Non-structural 5a protein, domain 1a / Hepatitis C virus non-structural 5a, 1B domain / NS5A domain 1a superfamily / Hepatitis C virus non-structural 5a protein membrane anchor / Hepatitis C virus non-structural 5a zinc finger domain / Hepatitis C virus non-structural 5a domain 1b / Hepacivirus nonstructural protein 2 (NS2) protease domain profile. / Hepatitis C virus, Non-structural protein NS4a / Hepatitis C virus non-structural protein NS4a / Hepatitis C virus, Core protein, C-terminal / Hepatitis C virus core protein / Hepatitis C virus, Non-structural protein E2/NS1 / Hepatitis C virus non-structural protein E2/NS1 / Hepatitis C virus, Envelope glycoprotein E1 / Hepatitis C virus envelope glycoprotein E1 / RNA dependent RNA polymerase, hepatitis C virus / Viral RNA dependent RNA polymerase / Hepatitis C virus, NS3 protease, Peptidase S29 / Hepatitis C virus NS3 protease / Hepacivirus/Pegivirus NS3 protease domain profile. / DEAD box, Flavivirus / Flavivirus DEAD domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Reverse transcriptase/Diguanylate cyclase domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Immunoglobulins / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / Immunoglobulin-like / Sandwich / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
Hepatitis C virus genotype 1a
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsGirard-Blanc, C. / Rey, F.A. / Krey, T.
Funding support France, 1items
OrganizationGrant numberCountry
ANRS France
CitationJournal: J.Virol. / Year: 2016
Title: Antibody Response to Hypervariable Region 1 Interferes with Broadly Neutralizing Antibodies to Hepatitis C Virus.
Authors: Keck, Z.Y. / Girard-Blanc, C. / Wang, W. / Lau, P. / Zuiani, A. / Rey, F.A. / Krey, T. / Diamond, M.S. / Foung, S.K.
History
DepositionDec 20, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jan 20, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 9, 2016Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Genome polyprotein
B: Anti-HCV E2 Fab HC33.8 light chain
E: Anti-HCV E2 Fab HC33.8 heavy chain


Theoretical massNumber of molelcules
Total (without water)54,4453
Polymers54,4453
Non-polymers00
Water2,090116
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5250 Å2
ΔGint-35 kcal/mol
Surface area20130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)66.050, 49.570, 66.390
Angle α, β, γ (deg.)90.00, 98.50, 90.00
Int Tables number3
Space group name H-MP121

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Components

#1: Protein/peptide Genome polyprotein


Mass: 2295.511 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Hepatitis C virus genotype 1a (isolate H)
References: UniProt: P27958, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases, hepacivirin, nucleoside-triphosphate phosphatase, RNA helicase, RNA-directed RNA polymerase
#2: Antibody Anti-HCV E2 Fab HC33.8 light chain


Mass: 23507.953 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pMT/BiP modified / Cell line (production host): Schneider 2 / Production host: Drosophila (fruit flies)
#3: Antibody Anti-HCV E2 Fab HC33.8 heavy chain


Mass: 28641.520 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pMT/BiP modified / Cell line (production host): Schneider 2 / Production host: Drosophila (fruit flies)
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 116 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 1.97 Å3/Da / Density % sol: 37.7 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 32% PEG 4000 100 mM Tris-HCl pH 8.5 800 mM lithium chloride Crystals obtained using heterologous microseeding.

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.00002 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 6, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00002 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 33283 / % possible obs: 99.7 % / Redundancy: 6.7 % / Biso Wilson estimate: 39.81 Å2 / Net I/σ(I): 16.39
Reflection shellResolution: 1.9→2.02 Å / Redundancy: 6.7 % / Mean I/σ(I) obs: 1.21 / Num. unique all: 33780 / % possible all: 97.8

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Processing

Software
NameVersionClassification
BUSTER2.11.2refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB

Resolution: 1.9→49.57 Å / Cor.coef. Fo:Fc: 0.9441 / Cor.coef. Fo:Fc free: 0.9283 / SU R Cruickshank DPI: 0.156 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.153 / SU Rfree Blow DPI: 0.142 / SU Rfree Cruickshank DPI: 0.145
RfactorNum. reflection% reflectionSelection details
Rfree0.2363 1687 5 %RANDOM
Rwork0.194 ---
obs0.1962 33727 99.88 %-
Displacement parametersBiso mean: 61.65 Å2
Baniso -1Baniso -2Baniso -3
1--10.1055 Å20 Å2-2.6428 Å2
2---5.2892 Å20 Å2
3---15.3946 Å2
Refine analyzeLuzzati coordinate error obs: 0.407 Å
Refinement stepCycle: 1 / Resolution: 1.9→49.57 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3414 0 0 116 3530
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.013500HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.164773HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d1145SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes76HARMONIC2
X-RAY DIFFRACTIONt_gen_planes513HARMONIC5
X-RAY DIFFRACTIONt_it3500HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion3.72
X-RAY DIFFRACTIONt_other_torsion16.24
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion464SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact3876SEMIHARMONIC4
LS refinement shellResolution: 1.9→2.01 Å / Total num. of bins used: 17
RfactorNum. reflection% reflection
Rfree0.2652 144 4.99 %
Rwork0.2417 2741 -
all0.2429 5345 -
obs--98.2 %
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)
110.3056.38985.90950-0.86683.95520.2346-0.1032-0.20710.33030.5076-0.9920.34040.3023-0.74220.3254-0.38280.1579-0.2046-0.2657-0.294521.07857.312753.8593
26.9011-2.2244-5.9443.19063.81877.28170.2387-0.30710.2990.02070.29160.1939-0.49180.5428-0.53030.6061-0.25230.2799-0.4164-0.1253-0.32378.711611.198367.2796
32.31832.8577-7.17842.18183.0103-1.3056-0.0908-0.3061.04220.19250.2577-0.527-0.76890.2701-0.16690.7328-0.45840.2573-0.2682-0.0196-0.17615.945115.005848.2354
41.0899-2.06142.05352.12998.55615.8379-0.1818-0.67090.27760.01880.2620.0262-1.10060.1742-0.08020.14740.07980.1552-0.5172-0.0196-0.50384.09011.791859.1757
51.0038-0.4-1.963510.1073-4.1011-0.603-0.1209-0.11830.3041-0.85570.4847-0.1205-1.2462-0.4214-0.36380.44210.09310.1168-0.613-0.0266-0.53592.30176.323952.6808
6-0.2684-5.07190.62926.19583.17123.59820.15810.5931-0.1823-0.2556-0.0220.3989-0.9547-0.3573-0.13610.56640.27350.1383-0.61310.0752-0.2537-2.379211.959451.8284
73.6205-3.5376-6.35428.2911-0.1825-0.16320.1859-0.0038-0.05440.1457-0.15560.2532-0.5404-0.9258-0.03040.5810.17320.3746-0.69010.0601-0.2891-5.471510.514459.71
84.2686-4.76192.90877.32360.35981.89970.31890.12870.07950.6583-0.01310.1973-0.9270.9068-0.30580.8423-0.15540.3568-0.7511-0.1548-0.52088.277615.884657.8304
92.7238-7.6141-5.445810.49497.084315.99180.3217-0.18480.2172-0.37560.21720.3427-0.2674-0.2772-0.53890.2435-0.00010.0543-0.7347-0.0134-0.5439-0.06336.662767.0567
101.51172.1990.92491.62650.75950.2427-0.1448-0.01190.29460.01860.2735-0.082-1.21450.8188-0.12860.1723-0.21930.1569-0.4269-0.0772-0.492314.94924.347351.0815
11-0.32615.59721.05752.2072-0.87630.44850.07230.32930.3485-0.19440.00030.6275-0.6375-0.0219-0.07260.3159-0.02640.1388-0.396-0.0837-0.33824.46365.554374.5962
122.2168-0.603-1.384300.77828.29040.54-0.5009-0.01510.5324-0.47920.4836-0.80350.1761-0.0609-0.335-0.17510.043-0.3227-0.0527-0.47081.4004-9.623887.7622
132.13940.8079-0.83441.53410.55225.02060.1129-0.2207-0.22340.5178-0.190.21540.22130.5390.077-0.3586-0.0602-0.0385-0.27260.0161-0.41444.8536-20.128583.4373
149.4978-5.29122.865813.0375-6.59895.0330.35310.11310.2651-0.5624-0.1981-0.4452-0.61690.8912-0.15490.0389-0.31440.05820.0157-0.0258-0.366611.5821-4.973684.2274
154.4428-4.43366.147103.973510.68-0.0551-0.62970.04020.42320.2796-0.05310.55590.8704-0.2245-0.1624-0.2006-0.09380.26160.0725-0.276714.2868-18.172294.3319
16-1.81791.1845.243301.824611.22520.3708-0.19650.06030.1421-0.3713-0.0626-0.3781.0420.0005-0.2091-0.1649-0.01420.25810.0315-0.275615.576-16.969283.561
172.7781-3.27270.667412.6393-2.75254.20050.3322-0.1897-0.0106-0.2188-0.22880.0595-0.4470.4418-0.1034-0.1235-0.1018-0.0053-0.141-0.018-0.31175.4013-11.392979.6131
183.02671.8124-3.12655.2075-6.64180.86140.2903-0.1505-0.43721.1502-0.5537-0.21430.59171.19520.26350.237-0.0251-0.19510.20790.2035-0.215112.2645-30.56793.2555
192.927-2.069-0.2191.1076-1.58146.44250.2746-0.62330.11710.822-0.02650.0486-0.71230.6016-0.2481-0.0001-0.3396-0.02570.0048-0.0198-0.38577.5421-9.801393.6905
207.067-0.2894-4.66232.7833-4.9673-1.46670.0302-0.7882-0.70760.245-0.06181.1072-0.28190.51260.03160.0178-0.2283-0.1088-0.09370.1748-0.31984.7883-26.857495.155
213.16592.9427-5.739312.14036.42861.8689-0.1089-0.109-0.07430.959-0.56480.681-0.3157-0.48470.6737-0.1102-0.00790.0945-0.1047-0.0105-0.1257-2.2379-11.513248.5388
221.65396.1344-6.08170-5.57677.33730.33980.4741-1.0008-0.1251-0.1447-0.31440.21310.6366-0.1951-0.13330.09990.0021-0.132-0.0251-0.144516.8289-23.781752.1055
2313.1385-8.09124.1578.3493-2.18086.5219-0.4338-0.3924-0.3049-0.11370.60530.5834-0.3301-0.5963-0.1715-0.1344-0.0223-0.0126-0.0741-0.0055-0.13160.1649-10.803242.1055
240.011.7162-0.224301.00992.5563-0.22320.1338-0.1761-0.15170.3190.2256-1.0903-0.2142-0.09580.1093-0.0023-0.0044-0.08170.0239-0.18134.9061-5.284141.6086
252.03796.41725.41377.26554.77541.57270.0012-0.0762-0.22771.10050.1846-0.24120.20570.8411-0.18580.3399-0.01280.04230.0356-0.0553-0.25213.4926-6.325460.2682
262.3524-0.4054-2.69463.82930.72978.0956-0.1040.1181-0.0531-0.15390.3282-0.0995-1.03830.5279-0.22420.021-0.16940.0185-0.1466-0.0208-0.346613.7475-5.145940.6548
271.8415-6.1647-0.89765.1005-1.85787.34840.28060.8094-0.4507-0.2519-0.105-0.04970.00751.1788-0.1756-0.2893-0.06240.0514-0.1709-0.0358-0.39214.3955-12.132341.2782
282.2721.01221.216401.93034.69730.06210.9677-0.3285-0.0556-0.05920.39910.11490.5038-0.0029-0.0561-0.0446-0.0433-0.1242-0.0398-0.10354.0458-14.204938.8787
295.5925-5-1.8179.7180.94856.8701-0.256-0.027-0.01280.52720.1968-0.2304-0.28750.74830.0592-0.0665-0.00210.0534-0.0216-0.0153-0.207214.8059-13.853752.1995
301.8081-6.25934.10822.656-1.65692.18380.17171.0246-0.1749-0.4224-0.128-0.5845-0.9004-0.6701-0.04370.75010.12210.0343-0.12010.0616-0.31986.79597.431738.9337
314.1876-2.1007-2.27394.32990.7027-0.7726-0.3806-0.12331.1879-0.0020.309-0.9553-1.31190.79370.07160.7567-0.26910.2158-0.24260.07540.028511.60829.676942.1247
329.19480.93530.15299.49957.21776.0377-0.0884-0.38010.06710.1165-0.16140.6233-1.0355-0.53320.2498-0.02020.12940.0744-0.28220.0618-0.31961.3428-3.275150.5829
33-0.04193.6624-0.10592.038-3.42533.29440.18830.2119-0.20950.5585-0.151-0.09280.3390.4671-0.03730.10940.11170.0414-0.1774-0.0019-0.249511.7334-23.104460.435
343.878-3.071-2.3896.11321.11983.663-0.0518-0.552-0.2978-0.08170.02160.6490.4690.32720.0302-0.2061-0.0499-0.0848-0.1867-0.0169-0.25641.1444-22.668879.05
351.67423.4568-5.239202.36749.2843-0.28550.02070.958-1.07440.2540.1520.4758-0.08920.03150.20380.1014-0.059-0.29290.0134-0.25973.9688-19.689665.4866
3610.10038.34262.54140-1.61549.7584-0.25890.44540.3040.33670.17950.214-0.2069-1.12770.0795-0.28250.0258-0.1261-0.0793-0.0549-0.1169-10.2948-16.096273.4636
372.3546-0.29720.59434.123-1.54893.35120.5068-0.45350.1611-0.5397-0.20250.0807-0.19120.3381-0.3043-0.2513-0.0249-0.0717-0.2606-0.0425-0.35583.5994-17.261576.2141
382.7616-2.95893.82274.845-0.94591.08090.0522-0.0018-0.68180.0753-0.10351.07490.6981-1.19270.0513-0.2942-0.1377-0.1279-0.3291-0.0226-0.1699-9.394-22.348876.712
3910.1422-3.7266-6.84481.2094-9.45520.6047-0.1550.6281-0.723-1.0303-0.45390.48760.6101-0.36990.60890.05990.089-0.1279-0.4279-0.1307-0.39280.5576-27.036861.8833
40-1.366-1.08134.089115.5052-4.14716.43550.0724-0.2884-0.61860.18610.02380.44310.1388-0.0996-0.0962-0.5213-0.1074-0.0696-0.5773-0.0509-0.2976-7.124-27.103878.4953
412.1034-6.41014.41047.1334-4.672213.56670.15220.41971.0333-0.82630.2806-0.2287-1.0277-1.0914-0.43280.5095-0.08070.1382-0.22370.103-0.36249.2943.572135.3054
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{B|1 - 5}
2X-RAY DIFFRACTION2{B|6 - 24}
3X-RAY DIFFRACTION3{B|25 - 31}
4X-RAY DIFFRACTION4{B|32 - 41}
5X-RAY DIFFRACTION5{B|42 - 50}
6X-RAY DIFFRACTION6{B|51 - 55}
7X-RAY DIFFRACTION7{B|56 - 61}
8X-RAY DIFFRACTION8{B|62 - 74}
9X-RAY DIFFRACTION9{B|75 - 85}
10X-RAY DIFFRACTION10{B|86 - 102}
11X-RAY DIFFRACTION11{B|103 - 108}
12X-RAY DIFFRACTION12{B|109 - 119}
13X-RAY DIFFRACTION13{B|120 - 141}
14X-RAY DIFFRACTION14{B|142 - 146}
15X-RAY DIFFRACTION15{B|147 - 154}
16X-RAY DIFFRACTION16{B|155 - 162}
17X-RAY DIFFRACTION17{B|163 - 184}
18X-RAY DIFFRACTION18{B|185 - 190}
19X-RAY DIFFRACTION19{B|191 - 208}
20X-RAY DIFFRACTION20{B|209 - 212}
21X-RAY DIFFRACTION21{E|1 - 9}
22X-RAY DIFFRACTION22{E|10 - 18}
23X-RAY DIFFRACTION23{E|19 - 29}
24X-RAY DIFFRACTION24{E|30 - 38}
25X-RAY DIFFRACTION25{E|39 - 45}
26X-RAY DIFFRACTION26{E|46 - 63}
27X-RAY DIFFRACTION27{E|64 - 73}
28X-RAY DIFFRACTION28{E|74 - 82}
29X-RAY DIFFRACTION29{E|83 - 97}
30X-RAY DIFFRACTION30{E|98 - 107}
31X-RAY DIFFRACTION31{E|108 - 113}
32X-RAY DIFFRACTION32{E|114 - 119}
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38X-RAY DIFFRACTION38{E|202 - 214}
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