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- PDB-4x17: JC Mad-1 polyomavirus VP1 in complex with GD1b oligosaccharide -

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Basic information

Entry
Database: PDB / ID: 4x17
TitleJC Mad-1 polyomavirus VP1 in complex with GD1b oligosaccharide
ComponentsMajor capsid protein VP1
KeywordsVIRAL PROTEIN / beta-sandwich / jelly-roll / viral major capsid protein / glycan
Function / homology
Function and homology information


T=7 icosahedral viral capsid / clathrin-dependent endocytosis of virus by host cell / host cell nucleus / virion attachment to host cell / structural molecule activity
Similarity search - Function
Capsid protein VP1,Polyomavirus / Polyomavirus Vp1; Chain A / Capsid protein VP1,Polyomavirus / Polyomavirus capsid protein VP1 superfamily / Polyomavirus coat protein / Double-stranded DNA virus, group I, capsid / Sandwich / Mainly Beta
Similarity search - Domain/homology
: / N-acetyl-alpha-neuraminic acid / Major capsid protein VP1
Similarity search - Component
Biological speciesJC polyomavirus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å
AuthorsStroh, L.J. / Stehle, T.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health United States
CitationJournal: J.Virol. / Year: 2015
Title: The Greater Affinity of JC Polyomavirus Capsid for alpha 2,6-Linked Lactoseries Tetrasaccharide c than for Other Sialylated Glycans Is a Major Determinant of Infectivity.
Authors: Stroh, L.J. / Maginnis, M.S. / Blaum, B.S. / Nelson, C.D. / Neu, U. / Gee, G.V. / O'Hara, B.A. / Motamedi, N. / DiMaio, D. / Atwood, W.J. / Stehle, T.
History
DepositionNov 24, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Apr 22, 2015Provider: repository / Type: Initial release
Revision 1.1May 27, 2015Group: Database references
Revision 1.2Jan 31, 2018Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / 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_conn_angle / 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_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _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.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_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.value / _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.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_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 10, 2024Group: 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 / struct_ncs_dom_lim
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 / _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: Major capsid protein VP1
B: Major capsid protein VP1
C: Major capsid protein VP1
D: Major capsid protein VP1
E: Major capsid protein VP1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)153,96834
Polymers150,3795
Non-polymers3,58929
Water20,9511163
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area31740 Å2
ΔGint-124 kcal/mol
Surface area43900 Å2
MethodPISA
Unit cell
Length a, b, c (Å)149.740, 95.390, 128.880
Angle α, β, γ (deg.)90.00, 110.40, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E

NCS domain segments:

Ens-ID: 1 / Refine code: 4

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11VALVALVALVALAA26 - 299 - 12
21VALVALVALVALBB26 - 299 - 12
31VALVALVALVALCC26 - 299 - 12
41VALVALVALVALDD26 - 299 - 12
51VALVALVALVALEE26 - 299 - 12
12THRTHRASPASPAA31 - 5114 - 34
22THRTHRASPASPBB31 - 5114 - 34
32THRTHRASPASPCC31 - 5114 - 34
42THRTHRASPASPDD31 - 5114 - 34
52THRTHRASPASPEE31 - 5114 - 34
13HISHISPHEPHEAA53 - 5736 - 40
23HISHISPHEPHEBB53 - 5736 - 40
33HISHISPHEPHECC53 - 5736 - 40
43HISHISPHEPHEDD53 - 5736 - 40
53HISHISPHEPHEEE53 - 5736 - 40
14PROPROILEILEAA78 - 8561 - 68
24PROPROILEILEBB78 - 8561 - 68
34PROPROILEILECC78 - 8561 - 68
44PROPROILEILEDD78 - 8561 - 68
54PROPROILEILEEE78 - 8561 - 68
15METMETSERSERAA101 - 12284 - 105
25METMETSERSERBB101 - 12284 - 105
35METMETSERSERCC101 - 12284 - 105
45METMETSERSERDD101 - 12284 - 105
55METMETSERSEREE101 - 12284 - 105
16GLYGLYTHRTHRAA124 - 162107 - 145
26GLYGLYTHRTHRBB124 - 162107 - 145
36GLYGLYTHRTHRCC124 - 162107 - 145
46GLYGLYTHRTHRDD124 - 162107 - 145
56GLYGLYTHRTHREE124 - 162107 - 145
17ASNASNTHRTHRAA173 - 175156 - 158
27ASNASNTHRTHRBB173 - 175156 - 158
37ASNASNTHRTHRCC173 - 175156 - 158
47ASNASNTHRTHRDD173 - 175156 - 158
57ASNASNTHRTHREE173 - 175156 - 158
18GLNGLNLEULEUAA177 - 189160 - 172
28GLNGLNLEULEUBB177 - 189160 - 172
38GLNGLNLEULEUCC177 - 189160 - 172
48GLNGLNLEULEUDD177 - 189160 - 172
58GLNGLNLEULEUEE177 - 189160 - 172
19ALAALATHRTHRAA194 - 205177 - 188
29ALAALATHRTHRBB194 - 205177 - 188
39ALAALATHRTHRCC194 - 205177 - 188
49ALAALATHRTHRDD194 - 205177 - 188
59ALAALATHRTHREE194 - 205177 - 188
110LEULEUTHRTHRAA251 - 263234 - 246
210LEULEUTHRTHRBB251 - 263234 - 246
310LEULEUTHRTHRCC251 - 263234 - 246
410LEULEUTHRTHRDD251 - 263234 - 246
510LEULEUTHRTHREE251 - 263234 - 246
111SERSERVALVALAA266 - 280249 - 263
211SERSERVALVALBB266 - 280249 - 263
311SERSERVALVALCC266 - 280249 - 263
411SERSERVALVALDD266 - 280249 - 263
511SERSERVALVALEE266 - 280249 - 263
112ASNASNASPASPAA207 - 238190 - 221
212ASNASNASPASPBB207 - 238190 - 221
312ASNASNASPASPCC207 - 238190 - 221
412ASNASNASPASPDD207 - 238190 - 221
512ASNASNASPASPEE207 - 238190 - 221
113GLYGLYPROPROAA167 - 171150 - 154
213GLYGLYPROPROBB167 - 171150 - 154
313GLYGLYPROPROCC167 - 171150 - 154
413GLYGLYPROPRODD167 - 171150 - 154
513GLYGLYPROPROEE167 - 171150 - 154
114PHEPHEASPASPAA240 - 249223 - 232
214PHEPHEASPASPBB240 - 249223 - 232
314PHEPHEASPASPCC240 - 249223 - 232
414PHEPHEASPASPDD240 - 249223 - 232
514PHEPHEASPASPEE240 - 249223 - 232
115LEULEUVALVALAA282 - 287265 - 270
215LEULEUVALVALBB282 - 287265 - 270
315LEULEUVALVALCC282 - 287265 - 270
415LEULEUVALVALDD282 - 287265 - 270
515LEULEUVALVALEE282 - 287265 - 270

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.440374, 0.852862, 0.280529), (-0.857054, 0.306256, 0.414326), (0.267449, -0.422887, 0.865816)11.37457, 20.04656, -5.60428
3given(-0.450699, 0.512611, 0.730821), (-0.528674, -0.812945, 0.24418), (0.719287, -0.276315, 0.637398)31.46804, 14.13583, -15.58798
4given(-0.441742, -0.534776, 0.720332), (0.518263, -0.807506, -0.28167), (0.732303, 0.248896, 0.633864)32.44124, -9.09132, -16.53409
5given(0.451564, -0.850837, 0.268637), (0.845839, 0.312389, -0.4324), (0.283982, 0.42248, 0.860735)13.07301, -17.7489, -6.7847

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Components

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Protein , 1 types, 5 molecules ABCDE

#1: Protein
Major capsid protein VP1 / Major structural protein VP1


Mass: 30075.861 Da / Num. of mol.: 5 / Fragment: UNP residues 23-290
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) JC polyomavirus / Plasmid: pET15b / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P03089

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Sugars , 2 types, 3 molecules

#2: Polysaccharide N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-alpha-neuraminic acid


Type: oligosaccharide / Mass: 600.525 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DNeup5Aca2-8DNeup5Aca2-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[Aad21122h-2a_2-6_5*NCC/3=O]/1-1/a8-b2WURCSPDB2Glycan 1.1.0
[][a-D-Neup5Ac]{[(8+2)][a-D-Neup5Ac]{}}LINUCSPDB-CARE
#6: Sugar ChemComp-SIA / N-acetyl-alpha-neuraminic acid / N-acetylneuraminic acid / sialic acid / alpha-sialic acid / O-SIALIC ACID


Type: D-saccharide, alpha linking / Mass: 309.270 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C11H19NO9
IdentifierTypeProgram
DNeup5AcaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-a-D-neuraminic acidCOMMON NAMEGMML 1.0
a-D-Neup5AcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
Neu5AcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 4 types, 1189 molecules

#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: K
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1163 / 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: 2.87 Å3/Da / Density % sol: 57.12 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: 0.1 M HEPES pH 7.5, 0.2 M KSCN, 12% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jul 12, 2013
RadiationMonochromator: Bartels Monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.75→30 Å / Num. obs: 170305 / % possible obs: 99.6 % / Redundancy: 5.7 % / Biso Wilson estimate: 23.1 Å2 / Net I/σ(I): 15.5
Reflection shellResolution: 1.75→1.8 Å / Redundancy: 5.3 % / Mean I/σ(I) obs: 2.4 / % possible all: 96.2

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Processing

Software
NameVersionClassification
REFMAC5.8.0025refinement
Cootmodel building
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3NXD

3nxd


Resolution: 1.75→30 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.958 / SU B: 3.913 / SU ML: 0.063 / Cross valid method: THROUGHOUT / ESU R: 0.09 / ESU R Free: 0.086 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.18149 8546 5 %RANDOM
Rwork0.15988 ---
obs0.16097 161759 99.64 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 19.334 Å2
Baniso -1Baniso -2Baniso -3
1--0.86 Å20 Å2-0.38 Å2
2--0.98 Å20 Å2
3---0.01 Å2
Refinement stepCycle: 1 / Resolution: 1.75→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9948 0 235 1163 11346
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0210591
X-RAY DIFFRACTIONr_bond_other_d0.0010.029828
X-RAY DIFFRACTIONr_angle_refined_deg1.3731.97214429
X-RAY DIFFRACTIONr_angle_other_deg0.749322689
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.38151348
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.00624.421475
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.43151684
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.0331559
X-RAY DIFFRACTIONr_chiral_restr0.0830.21643
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02112017
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022413
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_it0.5831.0395206
X-RAY DIFFRACTIONr_mcbond_other0.5821.0385205
X-RAY DIFFRACTIONr_mcangle_it0.9771.5536508
X-RAY DIFFRACTIONr_mcangle_other0.9771.5536509
X-RAY DIFFRACTIONr_scbond_it0.8741.235385
X-RAY DIFFRACTIONr_scbond_other0.8711.235385
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other1.3861.7827886
X-RAY DIFFRACTIONr_long_range_B_refined5.80810.16312545
X-RAY DIFFRACTIONr_long_range_B_other5.80810.16312545
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Ens-ID: 1 / Number: 2989 / Refine-ID: X-RAY DIFFRACTION

Auth asym-IDTypeRms dev position (Å)Weight position
Amedium positional0.240.5
Bmedium positional0.170.5
Cmedium positional0.170.5
Dmedium positional0.170.5
Emedium positional0.190.5
Amedium thermal0.632
Bmedium thermal0.612
Cmedium thermal0.622
Dmedium thermal0.642
Emedium thermal0.672
LS refinement shellResolution: 1.75→1.795 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.294 601 -
Rwork0.269 11479 -
obs--96.26 %
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)
13.2151-0.93354.17550.4845-1.13717.4986-0.05190.08890.1190.0835-0.0313-0.1387-0.23590.29070.08310.0648-0.0525-0.04420.09220.06140.115263.623314.434624.7261
20.6989-0.28330.1320.8940.00080.6951-0.01910.14180.0477-0.0202-0.0078-0.0608-0.01430.08870.02690.0119-0.0246-0.01430.06920.03410.02657.34616.080918.4334
33.38980.25623.44670.23350.47945.1444-0.1932-0.250.2710.08990.0277-0.0812-0.4509-0.15670.16560.15420.0199-0.06880.06210.00620.141534.4329.924936.6501
40.9871-0.0772-0.12380.2478-0.16610.9798-0.04760.00810.13810.0211-0.0058-0.0648-0.13910.01660.05340.0482-0.0084-0.04090.01440.0260.083338.779924.801328.0996
50.87860.11620.79540.93930.2362.04510.0286-0.18790.06290.16520.00790.0228-0.0482-0.3179-0.03650.04490.0198-0.0080.0866-0.00490.072212.87876.679642.0861
60.5960.00480.22221.0237-0.15590.5584-0.0123-0.02210.06760.07710.0152-0.0265-0.0816-0.0961-0.00290.0190.0178-0.00590.0374-0.00090.025817.432210.230839.5278
71.2097-0.12631.69822.14272.718916.0572-0.0307-0.116-0.08480.17620.0549-0.01360.33770.4012-0.02420.0642-0.038-0.01020.09680.03830.103235.3882-25.105656.1795
81.0493-0.32660.01830.47860.04670.6610.0108-0.0212-0.0685-0.00380.02220.08040.066-0.0748-0.03310.0182-0.0115-0.01930.01570.00760.040822.4866-17.495235.0508
92.6137-0.5392.1781.6553-3.658715.7352-0.0475-0.0163-0.03970.128-0.1088-0.12620.06730.49080.15630.07610.043-0.0340.0514-0.02260.074964.3352-20.77440.6228
100.83110.18070.15860.7003-0.18810.94540.01870.0739-0.063-0.0481-0.01330.03860.08380.0586-0.00540.01490.0131-0.00990.0169-0.01410.016347.707-19.539522.5958
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A24 - 58
2X-RAY DIFFRACTION2A59 - 288
3X-RAY DIFFRACTION3B24 - 59
4X-RAY DIFFRACTION4B60 - 288
5X-RAY DIFFRACTION5C25 - 67
6X-RAY DIFFRACTION6C68 - 288
7X-RAY DIFFRACTION7D24 - 42
8X-RAY DIFFRACTION8D43 - 288
9X-RAY DIFFRACTION9E24 - 43
10X-RAY DIFFRACTION10E44 - 288

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