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- PDB-4r2g: Crystal Structure of PGT124 Fab bound to HIV-1 JRCSF gp120 core a... -

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Basic information

Entry
Database: PDB / ID: 4r2g
TitleCrystal Structure of PGT124 Fab bound to HIV-1 JRCSF gp120 core and to CD4
Components
  • PGT124 Heavy Chain
  • PGT124 Light Chain
  • Surface protein gp160
  • T-cell surface glycoprotein CD4
KeywordsIMMUNE SYSTEM / Protein-Protein complex / IgG / Anti-HIV antibodies / gp120
Function / homology
Function and homology information


helper T cell enhancement of adaptive immune response / interleukin-16 binding / interleukin-16 receptor activity / cellular response to ionomycin / maintenance of protein location in cell / response to methamphetamine hydrochloride / T cell selection / MHC class II protein binding / cellular response to granulocyte macrophage colony-stimulating factor stimulus / interleukin-15-mediated signaling pathway ...helper T cell enhancement of adaptive immune response / interleukin-16 binding / interleukin-16 receptor activity / cellular response to ionomycin / maintenance of protein location in cell / response to methamphetamine hydrochloride / T cell selection / MHC class II protein binding / cellular response to granulocyte macrophage colony-stimulating factor stimulus / interleukin-15-mediated signaling pathway / CD22 mediated BCR regulation / regulation of T cell activation / positive regulation of monocyte differentiation / response to vitamin D / IgG immunoglobulin complex / Alpha-defensins / Nef Mediated CD4 Down-regulation / Fc epsilon receptor (FCERI) signaling / leukocyte chemotaxis / Other interleukin signaling / Classical antibody-mediated complement activation / T cell receptor complex / immunoglobulin mediated immune response / extracellular matrix structural constituent / enzyme-linked receptor protein signaling pathway / Dectin-2 family / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / macrophage differentiation / positive regulation of calcium ion transport into cytosol / Generation of second messenger molecules / FCGR activation / T cell differentiation / immunoglobulin binding / Co-inhibition by PD-1 / Role of LAT2/NTAL/LAB on calcium mobilization / Binding and entry of HIV virion / Role of phospholipids in phagocytosis / immunoglobulin complex / Scavenging of heme from plasma / antigen binding / coreceptor activity / positive regulation of plasma membrane raft polarization / positive regulation of interleukin-2 production / positive regulation of receptor clustering / symbiont-mediated perturbation of host defense response / positive regulation of T cell proliferation / FCERI mediated Ca+2 mobilization / B cell receptor signaling pathway / FCGR3A-mediated IL10 synthesis / cell surface receptor protein tyrosine kinase signaling pathway / Regulation of Complement cascade / protein tyrosine kinase binding / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / host cell endosome membrane / Cell surface interactions at the vascular wall / T cell activation / FCGR3A-mediated phagocytosis / FCERI mediated MAPK activation / clathrin-coated endocytic vesicle membrane / Vpu mediated degradation of CD4 / Regulation of actin dynamics for phagocytic cup formation / T cell receptor signaling pathway / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / FCERI mediated NF-kB activation / positive regulation of inflammatory response / response to estradiol / MHC class II protein complex binding / transmembrane signaling receptor activity / Downstream TCR signaling / positive regulation of cell growth / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / virus receptor activity / signaling receptor activity / blood microparticle / clathrin-dependent endocytosis of virus by host cell / Potential therapeutics for SARS / response to ethanol / Initial triggering of complement / adaptive immune response / early endosome / cell surface receptor signaling pathway / cell adhesion / viral protein processing / immune response / membrane raft / endoplasmic reticulum lumen / external side of plasma membrane / fusion of virus membrane with host plasma membrane / signaling receptor binding / fusion of virus membrane with host endosome membrane / viral envelope / symbiont entry into host cell / lipid binding / protein kinase binding / endoplasmic reticulum membrane / virion attachment to host cell / host cell plasma membrane / virion membrane
Similarity search - Function
CD4, extracellular / T cell CD4 receptor C-terminal region / CD4, extracellular / T cell CD4 receptor C terminal region / T-cell surface antigen CD4 / Immunoglobulin C2-set / Immunoglobulin C2-set domain / HIV Envelope Protein Gp120; Chain G / Human immunodeficiency virus 1, Gp160, envelope glycoprotein / Immunoglobulin ...CD4, extracellular / T cell CD4 receptor C-terminal region / CD4, extracellular / T cell CD4 receptor C terminal region / T-cell surface antigen CD4 / Immunoglobulin C2-set / Immunoglobulin C2-set domain / HIV Envelope Protein Gp120; Chain G / Human immunodeficiency virus 1, Gp160, envelope glycoprotein / Immunoglobulin / Immunoglobulin domain / : / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Beta Complex / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
T-cell surface glycoprotein CD4 / Immunoglobulin gamma-1 heavy chain / Immunoglobulin lambda constant 3 / Envelope glycoprotein gp160
Similarity search - Component
Biological speciesHuman immunodeficiency virus type 1 group M subtype B
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.283 Å
AuthorsGarces, F. / Wilson, I.A.
CitationJournal: Cell / Year: 2014
Title: Structural evolution of glycan recognition by a family of potent HIV antibodies.
Authors: Fernando Garces / Devin Sok / Leopold Kong / Ryan McBride / Helen J Kim / Karen F Saye-Francisco / Jean-Philippe Julien / Yuanzi Hua / Albert Cupo / John P Moore / James C Paulson / Andrew B ...Authors: Fernando Garces / Devin Sok / Leopold Kong / Ryan McBride / Helen J Kim / Karen F Saye-Francisco / Jean-Philippe Julien / Yuanzi Hua / Albert Cupo / John P Moore / James C Paulson / Andrew B Ward / Dennis R Burton / Ian A Wilson /
Abstract: The HIV envelope glycoprotein (Env) is densely covered with self-glycans that should help shield it from recognition by the human immune system. Here, we examine how a particularly potent family of ...The HIV envelope glycoprotein (Env) is densely covered with self-glycans that should help shield it from recognition by the human immune system. Here, we examine how a particularly potent family of broadly neutralizing antibodies (Abs) has evolved common and distinct structural features to counter the glycan shield and interact with both glycan and protein components of HIV Env. The inferred germline antibody already harbors potential binding pockets for a glycan and a short protein segment. Affinity maturation then leads to divergent evolutionary branches that either focus on a single glycan and protein segment (e.g., Ab PGT124) or engage multiple glycans (e.g., Abs PGT121-123). Furthermore, other surrounding glycans are avoided by selecting an appropriate initial antibody shape that prevents steric hindrance. Such molecular recognition lessons are important for engineering proteins that can recognize or accommodate glycans.
History
DepositionAug 11, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 8, 2014Provider: repository / Type: Initial release
Revision 1.1Oct 15, 2014Group: Derived calculations
Revision 1.2Jun 21, 2017Group: Database references / Source and taxonomy / Structure summary
Category: entity_name_com / entity_src_gen ...entity_name_com / entity_src_gen / struct_ref / struct_ref_seq / struct_ref_seq_dif
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / 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_validate_close_contact / struct_asym / struct_conn / 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.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 3.0Dec 25, 2024Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_nonpoly_scheme / pdbx_validate_close_contact / struct_conn
Item: _atom_site.auth_seq_id / _chem_comp.pdbx_synonyms ..._atom_site.auth_seq_id / _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nonpoly_scheme.pdb_seq_num

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
E: Surface protein gp160
F: T-cell surface glycoprotein CD4
P: PGT124 Light Chain
Q: PGT124 Heavy Chain
B: T-cell surface glycoprotein CD4
C: PGT124 Light Chain
D: PGT124 Heavy Chain
H: T-cell surface glycoprotein CD4
I: PGT124 Light Chain
J: PGT124 Heavy Chain
L: T-cell surface glycoprotein CD4
M: PGT124 Light Chain
N: PGT124 Heavy Chain
O: Surface protein gp160
A: Surface protein gp160
K: Surface protein gp160
hetero molecules


Theoretical massNumber of molelcules
Total (without water)428,76056
Polymers414,76416
Non-polymers13,99740
Water00
1
E: Surface protein gp160
F: T-cell surface glycoprotein CD4
P: PGT124 Light Chain
Q: PGT124 Heavy Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,31015
Polymers103,6914
Non-polymers3,61911
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: T-cell surface glycoprotein CD4
C: PGT124 Light Chain
D: PGT124 Heavy Chain
O: Surface protein gp160
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,08814
Polymers103,6914
Non-polymers3,39810
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
H: T-cell surface glycoprotein CD4
I: PGT124 Light Chain
J: PGT124 Heavy Chain
K: Surface protein gp160
hetero molecules


Theoretical massNumber of molelcules
Total (without water)106,64612
Polymers103,6914
Non-polymers2,9558
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
L: T-cell surface glycoprotein CD4
M: PGT124 Light Chain
N: PGT124 Heavy Chain
A: Surface protein gp160
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,71615
Polymers103,6914
Non-polymers4,02511
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)164.406, 165.438, 229.712
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 2 types, 8 molecules EOAKFBHL

#1: Protein
Surface protein gp160 / Env polyprotein


Mass: 34754.543 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 group M subtype B
Strain: isolate JRCSF / Gene: env / Cell line (production host): 293 FreeStyle / Production host: Homo sapiens (human) / References: UniProt: P20871
#2: Protein
T-cell surface glycoprotein CD4 / T-cell surface antigen T4/Leu-3


Mass: 20419.252 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CD4 / Production host: Escherichia coli (E. coli) / References: UniProt: P01730

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Antibody , 2 types, 8 molecules PCIMQDJN

#3: Antibody
PGT124 Light Chain / Ig lambda chain C region DOT / Ig lambda chain C region NEWM / Ig lambda-3 chain C regions


Mass: 23056.605 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IGL@, IGLC3 / Cell line (production host): 293 FreeStyle / Production host: Homo sapiens (human) / References: UniProt: P0DOY3
#4: Antibody
PGT124 Heavy Chain / Immunoglobulin gamma-1 heavy chain NIE


Mass: 25460.508 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IGH@ / Cell line (production host): 293 FreeStyle / Production host: Homo sapiens (human) / References: UniProt: P0DOX5

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Sugars , 3 types, 32 molecules

#5: Polysaccharide
alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1721.527 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-2DManpa1-2DManpa1-3[DManpa1-2DManpa1-6[DManpa1-3]DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,10,9/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-g1_d2-e1_e2-f1_g3-h1_g6-i1_i2-j1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}}}}}}LINUCSPDB-CARE
#6: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#7: 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.: 26
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
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

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Non-polymers , 2 types, 8 molecules

#8: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#9: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3

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Details

Has protein modificationY

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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: 3.77 Å3/Da / Density % sol: 67.34 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 2.4M ammonium sulphate, 0.1M Tris, 13% glycerol, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 1, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.283→39.647 Å / Num. obs: 94587 / % possible obs: 98.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 6.7 % / Net I/σ(I): 15.7
Reflection shellResolution: 3.283→3.4 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.87 / Mean I/σ(I) obs: 2.2 / Num. unique all: 7664 / % possible all: 95.9

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
PHENIX(phenix.refine: 1.8.1_1168)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.283→39.647 Å / SU ML: 0.45 / Phase error: 26.26 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2625 4720 4.99 %Random
Rwork0.207 ---
all0.2098 94587 --
obs0.2098 94587 98.44 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.283→39.647 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms28246 0 912 0 29158
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01129813
X-RAY DIFFRACTIONf_angle_d1.37340397
X-RAY DIFFRACTIONf_dihedral_angle_d16.06611109
X-RAY DIFFRACTIONf_chiral_restr0.0784717
X-RAY DIFFRACTIONf_plane_restr0.0055058
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.283-3.32030.32671730.28832921X-RAY DIFFRACTION98
3.3203-3.35930.35241520.27942781X-RAY DIFFRACTION93
3.3593-3.40030.36531450.28262979X-RAY DIFFRACTION99
3.4003-3.44330.3741660.31043029X-RAY DIFFRACTION99
3.4433-3.48860.35951550.28772980X-RAY DIFFRACTION100
3.4886-3.53640.29741520.25213006X-RAY DIFFRACTION100
3.5364-3.58680.30011410.24223027X-RAY DIFFRACTION100
3.5868-3.64030.31351600.24822971X-RAY DIFFRACTION100
3.6403-3.69720.30731500.26242973X-RAY DIFFRACTION99
3.6972-3.75780.29391510.22613047X-RAY DIFFRACTION100
3.7578-3.82250.24651640.22113005X-RAY DIFFRACTION100
3.8225-3.8920.29771540.23882982X-RAY DIFFRACTION99
3.892-3.96670.34441510.24272987X-RAY DIFFRACTION99
3.9667-4.04760.26681710.21153013X-RAY DIFFRACTION100
4.0476-4.13560.26341430.19882880X-RAY DIFFRACTION95
4.1356-4.23170.24231590.18382980X-RAY DIFFRACTION98
4.2317-4.33740.2591530.16933026X-RAY DIFFRACTION100
4.3374-4.45450.2291570.16792988X-RAY DIFFRACTION100
4.4545-4.58540.2171620.1623005X-RAY DIFFRACTION99
4.5854-4.73310.21761670.15963024X-RAY DIFFRACTION100
4.7331-4.9020.22881540.1653027X-RAY DIFFRACTION100
4.902-5.09790.21521440.16693035X-RAY DIFFRACTION99
5.0979-5.32940.20921630.1733020X-RAY DIFFRACTION99
5.3294-5.60960.25031570.19342866X-RAY DIFFRACTION94
5.6096-5.960.28131750.20653047X-RAY DIFFRACTION100
5.96-6.41840.26991660.20833052X-RAY DIFFRACTION99
6.4184-7.0610.25241600.20763055X-RAY DIFFRACTION99
7.061-8.07530.24791600.20323001X-RAY DIFFRACTION97
8.0753-10.14570.2141670.183057X-RAY DIFFRACTION97
10.1457-39.64960.28781480.24463103X-RAY DIFFRACTION95

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