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- PDB-7z1b: Nanobody H11-A10 and F2 bound to RBD -

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Basic information

Entry
Database: PDB / ID: 7z1b
TitleNanobody H11-A10 and F2 bound to RBD
Components
  • Nanobody A10
  • Nanobody F2
  • Spike protein S1
KeywordsANTIVIRAL PROTEIN / spike / nanobody / high affinity
Function / homology
Function and homology information


Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell ...Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated endocytosis of virus by host cell / membrane fusion / Attachment and Entry / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / receptor ligand activity / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / identical protein binding / membrane / plasma membrane
Similarity search - Function
Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / Spike glycoprotein, betacoronavirus / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus / Betacoronavirus spike glycoprotein S1, receptor binding / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like ...Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / Spike glycoprotein, betacoronavirus / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus / Betacoronavirus spike glycoprotein S1, receptor binding / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like / Betacoronavirus-like spike glycoprotein S1, N-terminal / Spike glycoprotein S2, coronavirus, heptad repeat 1 / Spike glycoprotein S2, coronavirus, heptad repeat 2 / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile. / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile. / Spike glycoprotein S2 superfamily, coronavirus / Spike glycoprotein S2, coronavirus / Coronavirus spike glycoprotein S2 / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal
Similarity search - Domain/homology
Biological speciesSevere acute respiratory syndrome coronavirus 2
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsMikolajek, H. / Naismith, J.H.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Wellcome Trust100209/Z/12/Z) United Kingdom
Engineering and Physical Sciences Research CouncilEP/S025243/1 United Kingdom
CitationJournal: Proc Natl Acad Sci U S A / Year: 2022
Title: Correlation between the binding affinity and the conformational entropy of nanobody SARS-CoV-2 spike protein complexes.
Authors: Halina Mikolajek / Miriam Weckener / Z Faidon Brotzakis / Jiandong Huo / Evmorfia V Dalietou / Audrey Le Bas / Pietro Sormanni / Peter J Harrison / Philip N Ward / Steven Truong / Lucile ...Authors: Halina Mikolajek / Miriam Weckener / Z Faidon Brotzakis / Jiandong Huo / Evmorfia V Dalietou / Audrey Le Bas / Pietro Sormanni / Peter J Harrison / Philip N Ward / Steven Truong / Lucile Moynie / Daniel K Clare / Maud Dumoux / Joshua Dormon / Chelsea Norman / Naveed Hussain / Vinod Vogirala / Raymond J Owens / Michele Vendruscolo / James H Naismith /
Abstract: Camelid single-domain antibodies, also known as nanobodies, can be readily isolated from naïve libraries for specific targets but often bind too weakly to their targets to be immediately useful. ...Camelid single-domain antibodies, also known as nanobodies, can be readily isolated from naïve libraries for specific targets but often bind too weakly to their targets to be immediately useful. Laboratory-based genetic engineering methods to enhance their affinity, termed maturation, can deliver useful reagents for different areas of biology and potentially medicine. Using the receptor binding domain (RBD) of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein and a naïve library, we generated closely related nanobodies with micromolar to nanomolar binding affinities. By analyzing the structure-activity relationship using X-ray crystallography, cryoelectron microscopy, and biophysical methods, we observed that higher conformational entropy losses in the formation of the spike protein-nanobody complex are associated with tighter binding. To investigate this, we generated structural ensembles of the different complexes from electron microscopy maps and correlated the conformational fluctuations with binding affinity. This insight guided the engineering of a nanobody with improved affinity for the spike protein.
History
DepositionFeb 24, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 23, 2022Provider: repository / Type: Initial release
Revision 1.1Oct 5, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Spike protein S1
B: Nanobody F2
F: Nanobody A10
C: Spike protein S1
D: Nanobody F2
E: Nanobody A10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,2908
Polymers106,8476
Non-polymers4422
Water2,756153
1
A: Spike protein S1
B: Nanobody F2
F: Nanobody A10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,6454
Polymers53,4243
Non-polymers2211
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Spike protein S1
D: Nanobody F2
E: Nanobody A10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,6454
Polymers53,4243
Non-polymers2211
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)58.490, 120.860, 171.950
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
12B
22D
13F
23E

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11THRTHRLYSLYSAA333 - 5284 - 199
21THRTHRLYSLYSCD333 - 5284 - 199
12GLNGLNSERSERBB1 - 1251 - 125
22GLNGLNSERSERDE1 - 1251 - 125
13GLNGLNSERSERFC1 - 1271 - 127
23GLNGLNSERSEREF1 - 1271 - 127

NCS ensembles :
ID
1
2
3

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Components

#1: Protein Spike protein S1


Mass: 23716.580 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: S, 2 / Production host: Homo sapiens (human) / References: UniProt: P0DTC2
#2: Antibody Nanobody F2


Mass: 14833.442 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli)
#3: Antibody Nanobody A10


Mass: 14873.572 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli)
#4: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6 / Feature type: SUBJECT OF INVESTIGATION
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 153 / Source method: isolated from a natural source / Formula: H2O
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: 2.84 Å3/Da / Density % sol: 56.75 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1 M Sodium citrate, pH 5.5, 20 % Peg 3000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 16, 2020
RadiationMonochromator: M / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 2.3→57.01 Å / Num. obs: 55151 / % possible obs: 100 % / Redundancy: 13.4 % / CC1/2: 0.998 / Rmerge(I) obs: 0.129 / Net I/σ(I): 12
Reflection shellResolution: 2.3→2.36 Å / Mean I/σ(I) obs: 1.2 / Num. unique obs: 4029 / CC1/2: 0.565

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
xia2data reduction
xia2data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6ZBP

6zbp


Resolution: 2.3→57.01 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.899 / SU B: 17.161 / SU ML: 0.189 / Cross valid method: THROUGHOUT / ESU R: 0.26 / ESU R Free: 0.213 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24331 2631 4.8 %RANDOM
Rwork0.19774 ---
obs0.19993 52466 99.98 %-
Solvent computationIon probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1.1 Å / Solvent model: MASK
Displacement parametersBiso mean: 64.563 Å2
Baniso -1Baniso -2Baniso -3
1-0.93 Å20 Å2-0 Å2
2---3.82 Å20 Å2
3---2.88 Å2
Refinement stepCycle: 1 / Resolution: 2.3→57.01 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7115 0 28 153 7296
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0127385
X-RAY DIFFRACTIONr_bond_other_d0.0010.0186624
X-RAY DIFFRACTIONr_angle_refined_deg1.4971.65510037
X-RAY DIFFRACTIONr_angle_other_deg1.2371.58315190
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.4735908
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.5821.155407
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.296151116
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.9751554
X-RAY DIFFRACTIONr_chiral_restr0.060.2919
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.028566
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021950
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_it3.1840.9443623
X-RAY DIFFRACTIONr_mcbond_other3.1850.9443622
X-RAY DIFFRACTIONr_mcangle_it4.6891.3974522
X-RAY DIFFRACTIONr_mcangle_other4.6891.3974523
X-RAY DIFFRACTIONr_scbond_it4.1851.3213762
X-RAY DIFFRACTIONr_scbond_other4.1851.3213763
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other6.0941.8615512
X-RAY DIFFRACTIONr_long_range_B_refined11.88511.2357787
X-RAY DIFFRACTIONr_long_range_B_other11.8911.1327777
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A60920.09
12C60920.09
21B39320.07
22D39320.07
31F38050.1
32E38050.1
LS refinement shellResolution: 2.3→2.36 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.346 182 -
Rwork0.344 3842 -
obs--99.98 %
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)
11.5286-1.0601-0.00582.55311.04113.18080.10510.46360.1195-0.578-0.0546-0.1545-0.08090.0674-0.05050.5074-0.05160.01720.57330.02350.559-21.974-26.607-6.378
24.99410.5246-0.72157.80372.91142.55480.0545-0.35310.05920.585-0.0707-0.18620.10970.02520.01620.3819-0.0083-0.02070.43730.01090.477-24.794-23.7297.81
31.6422-0.1856-0.1544.06121.44072.06810.0222-0.14710.19130.2930.005-0.2327-0.1141-0.054-0.02720.39730.0009-0.02950.45760.02440.4976-24.399-15.05511.202
411.8641-1.0499-0.01691.8831-1.64891.5536-0.08320.9537-0.16520.0067-0.081-0.04350.0661-0.06650.16420.6043-0.0113-0.02980.6869-0.05720.6283-33.137-30.674-14.273
55.1724-0.23480.24532.9756-3.93796.7956-0.458-1.15980.24640.29110.5893-0.018-0.2105-0.7305-0.13130.61340.2072-0.09270.947-0.04140.5371-23.888-54.39418.613
64.4023-6.9869-0.958511.39181.85312.8895-0.1564-0.032-0.20460.31350.17130.25450.2682-0.4281-0.01490.5389-0.01040.01370.64920.03230.67-29.247-53.95813.999
74.681-2.53021.10125.4722-2.02473.83510.0170.0625-0.1422-0.16750.0321-0.0440.41580.1688-0.04920.4168-0.0050.03230.4844-0.00890.517-21.743-52.0127.396
81.4821-0.47350.78877.4384-4.02924.59640.0113-0.0854-0.11590.23870.0321-0.0190.15460.016-0.04340.39230.0032-0.00310.4734-0.0070.487-18.49-47.00311.971
90.88130.4845-0.62932.50980.35034.670.082-0.43190.02120.6009-0.0685-0.4786-0.16070.6717-0.01350.81590.0654-0.1210.78710.03030.691-14.487-48.7150.774
102.302-0.0083-1.25532.62791.94996.61170.03480.06440.0704-0.0403-0.14350.0565-0.04340.00520.10870.57970.060.0160.5310.06080.5772-22.417-49.82139.583
111.81390.48920.11564.42150.9122.1941-0.0646-0.1459-0.21150.1792-0.04520.46780.1354-0.26110.10980.63280.10820.01940.58410.09890.5889-27.521-59.3435.302
121.0478-0.2485-1.51580.94741.94827.80410.0305-0.33080.08770.37160.0368-0.19790.1030.4294-0.06730.71540.0734-0.07390.59970.03530.6413-17.366-48.99147.117
138.73682.7077-2.25365.5484-2.56418.5519-0.0488-0.03680.39620.44930.49171.0365-0.4266-0.4979-0.44290.74610.1691-0.01210.6327-0.03740.8644-20.341-19.82730.32
147.4911.7853-5.49528.8635-5.516812.26380.03880.27990.06730.2442-0.0862-0.0487-0.04870.20570.04740.6050.0151-0.12510.6129-0.07740.5566-13.725-27.88234.27
1512.36726.7731-3.52866.0272-5.35477.59210.3106-0.86270.30520.8202-0.2804-0.0716-0.99491.0131-0.03010.9085-0.0488-0.07760.8291-0.15720.5342-10.018-22.43542.025
161.88490.551-1.40866.679-4.29927.22860.1317-0.27260.3460.60640.06580.2741-0.65330.1346-0.19740.5920.0182-0.09840.6107-0.10910.617-14.17-24.74933.593
173.83092.09572.7477.6225.52737.45750.03060.3615-0.13350.30950.3636-0.45370.43050.4245-0.39420.83190.0374-0.04150.54090.05980.6971-21.479-91.91424.749
182.03891.4614-0.28091.12880.13071.44860.29-0.28260.18320.1609-0.17650.10280.0203-0.0453-0.11350.7837-0.05290.00380.79930.02240.7678-20.361-76.06334.435
193.0623-0.4920.42617.48161.13194.81730.07740.1103-0.0252-0.5112-0.09240.0614-0.0778-0.01640.0150.7206-0.0097-0.02210.54380.0620.6928-27.675-84.17921.931
201.47130.5937-0.11978.4313.20471.3244-0.01560.1269-0.1083-0.73720.0509-0.1468-0.1853-0.0846-0.03520.845-0.0151-0.01420.58350.08710.6072-23.921-77.83720.071
219.3989-1.0957.411310.0602-4.02119.8558-0.1059-0.3299-0.6278-0.35810.2529-1.16680.191-0.2274-0.14690.70410.00070.0780.6408-0.06020.7838-14.742-77.72824.066
226.1816-4.1605-1.74327.6153-0.84731.34150.2210.51950.0182-0.4923-0.06710.25450.0457-0.2292-0.15391.0346-0.26690.12451.1859-0.24971.0323-22.539-95.79514.641
231.66351.130.28047.66151.32162.8019-0.10760.16610.13930.0050.2842-1.2186-0.25470.4703-0.17660.6832-0.024-0.0530.6367-0.09831.0441-9.64711.81618.089
242.45610.15420.80217.85352.33483.81550.00550.07890.09310.14740.2134-0.6171-0.31810.199-0.2190.599-0.0125-0.04860.5085-0.05920.7336-17.84811.26920.926
253.2743.44672.74538.55614.0712.63240.1348-0.16820.16130.57820.049-1.02730.14870.0771-0.18380.707-0.0357-0.12570.6839-0.06460.8389-13.0173.61523.062
263.87412.38621.13868.32993.44232.2398-0.17370.0168-0.33540.17270.4903-0.9153-0.05710.3337-0.31660.6594-0.0472-0.06070.73-0.08920.8689-5.30812.18520.911
271.8961-56.920116.94862090.1819-619.8333183.8224-8.70690.9817-1.20742.151221.289619.4129-12.6735-7.9485-12.58273.2377-3.49712.77089.6456-2.12183.7253-8.3932.52338.685
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A333 - 393
2X-RAY DIFFRACTION2A394 - 417
3X-RAY DIFFRACTION3A418 - 515
4X-RAY DIFFRACTION4A516 - 528
5X-RAY DIFFRACTION5B1 - 14
6X-RAY DIFFRACTION6B15 - 28
7X-RAY DIFFRACTION7B29 - 88
8X-RAY DIFFRACTION8B89 - 125
9X-RAY DIFFRACTION9C333 - 392
10X-RAY DIFFRACTION10C393 - 417
11X-RAY DIFFRACTION11C418 - 498
12X-RAY DIFFRACTION12C499 - 528
13X-RAY DIFFRACTION13D1 - 28
14X-RAY DIFFRACTION14D29 - 53
15X-RAY DIFFRACTION15D54 - 71
16X-RAY DIFFRACTION16D72 - 125
17X-RAY DIFFRACTION17E1 - 25
18X-RAY DIFFRACTION18E26 - 32
19X-RAY DIFFRACTION19E33 - 87
20X-RAY DIFFRACTION20E88 - 113
21X-RAY DIFFRACTION21E114 - 117
22X-RAY DIFFRACTION22E118 - 128
23X-RAY DIFFRACTION23F1 - 44
24X-RAY DIFFRACTION24F45 - 87
25X-RAY DIFFRACTION25F88 - 113
26X-RAY DIFFRACTION26F114 - 117
27X-RAY DIFFRACTION27F118 - 128

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