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- PDB-2vbm: Tailspike protein of bacteriophage Sf6 complexed with tetrasaccharide -

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Basic information

Entry
Database: PDB / ID: 2vbm
TitleTailspike protein of bacteriophage Sf6 complexed with tetrasaccharide
ComponentsTAILSPIKE-PROTEIN
KeywordsVIRAL PROTEIN / VIRAL ADHESION PROTEIN / HYDROLASE / TAILSPIKE / ENDORHAMNOSIDASE / RIGHT-HANDED PARALLEL BETA-HELIX
Function / homology
Function and homology information


endo-1,3-alpha-L-rhamnosidase activity / symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide / virus tail, fiber / symbiont entry into host cell via disruption of host cell envelope / symbiont entry into host / Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / metabolic process / virion attachment to host cell
Similarity search - Function
: / Tailspike protein, C-terminal / Pectate lyase superfamily protein / Pectate lyase superfamily protein / Bacteriophage P22 tailspike, N-terminal / Phage P22 tailspike-like, N-terminal domain superfamily / Head binding / Single-stranded right-handed beta-helix, Pectin lyase-like / Pectate Lyase C-like / Pectin lyase fold ...: / Tailspike protein, C-terminal / Pectate lyase superfamily protein / Pectate lyase superfamily protein / Bacteriophage P22 tailspike, N-terminal / Phage P22 tailspike-like, N-terminal domain superfamily / Head binding / Single-stranded right-handed beta-helix, Pectin lyase-like / Pectate Lyase C-like / Pectin lyase fold / Pectin lyase fold/virulence factor / 3 Solenoid / Mainly Beta
Similarity search - Domain/homology
: / PHOSPHATE ION / Tail spike protein
Similarity search - Component
Biological speciesENTEROBACTERIA PHAGE SF6 (virus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsMueller, J.J. / Barbirz, S. / Freiberg, A. / Seckler, R. / Heinemann, U.
CitationJournal: Structure / Year: 2008
Title: An Intersubunit Active Site between Supercoiled Parallel Beta Helices in the Trimeric Tailspike Endorhamnosidase of Shigella Flexneri Phage Sf6.
Authors: Muller, J.J. / Barbirz, S. / Heinle, K. / Freiberg, A. / Seckler, R. / Heinemann, U.
History
DepositionSep 14, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 22, 2008Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 30, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / pdbx_struct_special_symmetry
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.4May 22, 2019Group: Data collection / Derived calculations / Experimental preparation
Category: exptl_crystal_grow / struct_conn
Item: _exptl_crystal_grow.temp / _struct_conn.pdbx_leaving_atom_flag
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / 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_conn_angle / pdbx_struct_special_symmetry / struct_asym / struct_conn / struct_conn_type / 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.occupancy / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_database_status.status_code_sf / _pdbx_struct_assembly_gen.asym_id_list / _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_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _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_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _pdbx_struct_special_symmetry.label_asym_id / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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.ptnr1_symmetry / _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_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 13, 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
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TAILSPIKE-PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,0167
Polymers55,0321
Non-polymers9846
Water4,468248
1
A: TAILSPIKE-PROTEIN
hetero molecules

A: TAILSPIKE-PROTEIN
hetero molecules

A: TAILSPIKE-PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)168,04921
Polymers165,0973
Non-polymers2,95118
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-y+1,x-y+1,z1
crystal symmetry operation3_565-x+y,-x+1,z1
Buried area25270 Å2
ΔGint-93.71 kcal/mol
Surface area44940 Å2
MethodPISA
Unit cell
Length a, b, c (Å)95.358, 95.358, 182.765
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number146
Space group name H-MH3
Components on special symmetry positions
IDModelComponents
11A-875-

MG

21A-876-

MN

31A-2049-

HOH

DetailsTHE BIOLOGICALLY ACTIVE UNIT IS A TRIMER. THE THREEFOLD AXIS IS THE C-AXIS.

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Components

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Protein / Sugars , 2 types, 2 molecules A

#1: Protein TAILSPIKE-PROTEIN / SF6 TAILSPIKE PROTEIN / TSP


Mass: 55032.414 Da / Num. of mol.: 1
Fragment: RESIDUES 110-623 LACKING THE N-TERMINAL PUTATIVE HEAD-BINDING DOMAIN
Source method: isolated from a genetically manipulated source
Details: ENDO-1,3-ALPHA-L-RHAMNOSIDASE / Source: (gene. exp.) ENTEROBACTERIA PHAGE SF6 (virus) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): D834 / References: UniProt: Q9XJP3
#2: Polysaccharide alpha-L-rhamnopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-L-rhamnopyranose- ...alpha-L-rhamnopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-L-rhamnopyranose-(1-2)-alpha-L-rhamnopyranose


Type: oligosaccharide / Mass: 659.630 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LRhapa1-3DGlcpNAcb1-2LRhapa1-2LRhapa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2211m-1a_1-5][a2122h-1b_1-5_2*NCC/3=O]/1-1-2-1/a2-b1_b2-c1_c3-d1WURCSPDB2Glycan 1.1.0
[][a-L-Rhap]{[(2+1)][a-L-Rhap]{[(2+1)][b-D-GlcpNAc]{[(3+1)][a-L-Rhap]{}}}}LINUCSPDB-CARE

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Non-polymers , 4 types, 253 molecules

#3: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: PO4
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#5: Chemical ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mn
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 248 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsPROTEIN LACKS N-TERMINAL PUTATIVE HEAD-BINDING DOMAIN

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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: 2.9 Å3/Da / Density % sol: 57.7 % / Description: NONE
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: VAPOR DIFFUSION HANGING DROP, 20 DEGR. CELSIUS; DROP: 3 MICROL RESERVOIR AND 3 MICROL PROTEIN SOLUTION; RESERVOIR: 0.1M MES, PH6.5, 16% PEG8000, 20MM MNCL2; PROTEIN: 10MG/ML, 10MM NA- ...Details: VAPOR DIFFUSION HANGING DROP, 20 DEGR. CELSIUS; DROP: 3 MICROL RESERVOIR AND 3 MICROL PROTEIN SOLUTION; RESERVOIR: 0.1M MES, PH6.5, 16% PEG8000, 20MM MNCL2; PROTEIN: 10MG/ML, 10MM NA-PHOSPHATE,PH7.0, OCTASACCHARIDE CONCENTRATION/PROTEIN CONCENTATION 10:1; CRYOCONDITION: 0.1M MES, PH6.5, 25% PEG8000, 20MM MNCL2, 15% ETHYLENGLYCOL

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.9537
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 8, 2005 / Details: MIRRORS
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2→47.7 Å / Num. obs: 39641 / % possible obs: 99.7 % / Redundancy: 4.9 % / Biso Wilson estimate: 17.6 Å2 / Rsym value: 0.06 / Net I/σ(I): 17.4
Reflection shellResolution: 2→2.07 Å / Redundancy: 4 % / Mean I/σ(I) obs: 7 / Rsym value: 0.22 / % possible all: 97.2

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
HKL-2000data reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2VBK

2vbk


Resolution: 2→47.67 Å / Cor.coef. Fo:Fc: 0.925 / Cor.coef. Fo:Fc free: 0.89 / SU B: 7.392 / SU ML: 0.107 / Cross valid method: THROUGHOUT / ESU R: 0.164 / ESU R Free: 0.153 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.232 2110 5.1 %RANDOM
Rwork0.19 ---
obs0.192 39641 99.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 20.2 Å2
Baniso -1Baniso -2Baniso -3
1-0.36 Å20.18 Å20 Å2
2--0.36 Å20 Å2
3----0.54 Å2
Refinement stepCycle: LAST / Resolution: 2→47.67 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3821 0 58 248 4127
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0223961
X-RAY DIFFRACTIONr_bond_other_d0.0010.023514
X-RAY DIFFRACTIONr_angle_refined_deg1.3621.9675400
X-RAY DIFFRACTIONr_angle_other_deg0.7663.0018130
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.7675512
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.97824.762168
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.67615615
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.961520
X-RAY DIFFRACTIONr_chiral_restr0.0850.2632
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.024472
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02773
X-RAY DIFFRACTIONr_nbd_refined0.1810.2700
X-RAY DIFFRACTIONr_nbd_other0.1870.23533
X-RAY DIFFRACTIONr_nbtor_refined0.1680.21996
X-RAY DIFFRACTIONr_nbtor_other0.0950.22315
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1360.2246
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1440.218
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2210.2103
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1490.224
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.82623260
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.10834079
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.0864.51649
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.84361321
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: 2→2.07 Å / Total num. of bins used: 15 /
RfactorNum. reflection
Rfree0.241 208
Rwork0.194 3762
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)
12.4280.1725-0.05251.74540.78412.2717-0.1067-0.10660.2226-0.28170.04720.0742-0.18950.2570.05950.2912-0.0150.03190.34760.07770.09826.309764.8631-38.4
21.77470.319-0.59722.1882-1.43021.6616-0.00590.0186-0.202-0.1163-0.0637-0.1126-0.03510.19450.06960.17340.04130.01010.1915-0.07390.08083.459133.7543-26.4833
33.1980.79830.16121.3986-0.0641.24670.05980.0153-0.0215-0.0737-0.0345-0.03520.01130.0414-0.02530.12470.01380.02040.0979-0.05590.02664.902640.2306-23.6243
42.7408-1.15750.45383.424-0.29961.347-0.13090.0556-0.01920.01580.14480.1926-0.0163-0.1199-0.01390.08660.0157-0.00260.0892-0.03290.0049-7.085242.4863-21.3489
519.52927.46463.17982.94250.88681.72750.1530.3212-0.02550.1604-0.20070.17610.11060.10790.04760.11640.03440.02960.0893-0.0387-0.013317.003538.2584-18.0534
61.0287-0.33960.03660.9767-0.01490.627-0.01740.1293-0.0087-0.166-0.0022-0.045-0.01620.03010.01960.0591-0.00610.01390.0493-0.01750.00275.116446.639-17.8779
71.21890.24390.29370.73870.44790.48550.01220.03290.0692-0.0488-0.0372-0.05630.06450.05010.0250.0175-0.00110.02290.0368-0.0080.034910.259144.6437-7.9003
814.7669-6.81670.48733.36880.27241.12990.04530.0029-0.4552-0.12310.1510.63910.2118-0.1095-0.19630.01890.02760.0481-0.0129-0.03810.017113.627427.1231-3.8909
94.1650.50030.29080.5082-0.44030.5867-0.02070.07410.22340.0023-0.0576-0.0023-0.05160.03220.07820.0423-0.01450.01970.0039-0.0122-0.01659.670449.2592-3.8027
106.7017-0.554-0.68771.46940.29051.3365-0.0653-0.03560.0991-0.12260.0121-0.07050.07130.00150.05320.05680.0020.0211-0.0217-0.0307-0.02173.492735.313-4.3893
110.9550.11570.01750.9190.15140.7035-0.0108-0.0049-0.0349-0.0153-0.0233-0.00060.0158-0.0010.0341-0.0106-0.00510.0122-0.0215-0.0053-0.01031.1543.50655.8079
1213.05223.07921.5693.0252-1.7262.698-0.07910.13090.12370.3090.00760.16680.24120.13740.0714-0.00480.02010.0272-0.0274-0.0215-0.0244-3.386336.5112.5048
132.13640.1559-0.10211.3001-0.02191.02880.01070.01290.0763-0.01880.0221-0.0466-0.0008-0.0328-0.0328-0.01440.00310.0287-0.0422-0.0146-0.0296-2.882844.688412.5048
141.61380.35730.09540.32180.08830.512-0.0801-0.0091-0.05120.02680.0262-0.00560.09690.05590.0539-0.03780.0135-0.0089-0.0221-0.0018-0.01425.835348.005917.837
150.7082-0.5034-0.29841.0997-0.67281.24090.00410.0099-0.04640.1542-0.0198-0.0774-0.1427-0.06840.01570.01990.00070.002-0.017-0.0094-0.0129-4.934349.806520.4161
161.83220.06510.40381.92080.17581.257-0.13450.09120.0538-0.11330.01790.0342-0.03240.01120.1165-0.0006-0.01020.0088-0.0074-0.00520.0097-6.099348.379624.0134
170.83070.1324-0.68724.18473.79975.4195-0.1236-0.1242-0.07570.1858-0.0039-0.05130.4585-0.24220.12750.0744-0.03140.04220.05610.02060.1099-13.38743.952343.3652
1811.73265.579211.03866.07043.103911.7324-0.4757-0.8380.3829-0.3526-0.19390.0852-0.3299-0.9690.66960.02460.02930.02870.0905-0.0477-0.0165-9.996545.162639.7981
192.60262.74380.05555.30220.48542.60730.0119-0.1508-0.0773-0.0032-0.0421-0.0512-0.01860.11710.03020.06430.01310.00840.11170.00820.071-6.265856.514150.5835
201.95080.2287-1.58523.39071.56654.4562-0.13160.0639-0.1269-0.3746-0.01830.0961-0.1317-0.09670.14990.0292-0.0077-0.01490.07110.00320.0569-7.303449.888337.0304
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A114 - 152
2X-RAY DIFFRACTION2A153 - 182
3X-RAY DIFFRACTION3A183 - 219
4X-RAY DIFFRACTION4A220 - 237
5X-RAY DIFFRACTION5A238 - 245
6X-RAY DIFFRACTION6A246 - 288
7X-RAY DIFFRACTION7A289 - 319
8X-RAY DIFFRACTION8A320 - 324
9X-RAY DIFFRACTION9A325 - 340
10X-RAY DIFFRACTION10A341 - 363
11X-RAY DIFFRACTION11A364 - 429
12X-RAY DIFFRACTION12A430 - 438
13X-RAY DIFFRACTION13A439 - 472
14X-RAY DIFFRACTION14A473 - 492
15X-RAY DIFFRACTION15A493 - 517
16X-RAY DIFFRACTION16A518 - 555
17X-RAY DIFFRACTION17A556 - 574
18X-RAY DIFFRACTION18A575 - 580
19X-RAY DIFFRACTION19A581 - 601
20X-RAY DIFFRACTION20A602 - 622

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