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- PDB-2c0i: Src family kinase Hck with bound inhibitor A-420983 -

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Basic information

Entry
Database: PDB / ID: 2c0i
TitleSrc family kinase Hck with bound inhibitor A-420983
ComponentsTYROSINE-PROTEIN KINASE HCK
KeywordsTRANSFERASE / TYROSINE-PROTEIN KINASE / ATP-BINDING / KINASE / LIPOPROTEIN / MYRISTATE / NUCLEOTIDE-BINDING / PALMITATE / PHOSPHORYLATION / SH2 DOMAIN / SH3 DOMAIN
Function / homology
Function and homology information


leukocyte degranulation / innate immune response-activating signaling pathway / leukocyte migration involved in immune response / respiratory burst after phagocytosis / regulation of podosome assembly / FLT3 signaling through SRC family kinases / regulation of phagocytosis / regulation of DNA-binding transcription factor activity / Nef and signal transduction / positive regulation of actin filament polymerization ...leukocyte degranulation / innate immune response-activating signaling pathway / leukocyte migration involved in immune response / respiratory burst after phagocytosis / regulation of podosome assembly / FLT3 signaling through SRC family kinases / regulation of phagocytosis / regulation of DNA-binding transcription factor activity / Nef and signal transduction / positive regulation of actin filament polymerization / Fc-gamma receptor signaling pathway involved in phagocytosis / mesoderm development / FCGR activation / type II interferon-mediated signaling pathway / transport vesicle / Signaling by CSF3 (G-CSF) / phosphotyrosine residue binding / FCGR3A-mediated IL10 synthesis / cell surface receptor protein tyrosine kinase signaling pathway / lipopolysaccharide-mediated signaling pathway / peptidyl-tyrosine phosphorylation / integrin-mediated signaling pathway / cell projection / regulation of actin cytoskeleton organization / non-membrane spanning protein tyrosine kinase activity / FCGR3A-mediated phagocytosis / Regulation of signaling by CBL / non-specific protein-tyrosine kinase / negative regulation of inflammatory response to antigenic stimulus / Inactivation of CSF3 (G-CSF) signaling / caveola / cytoplasmic side of plasma membrane / cytokine-mediated signaling pathway / Signaling by CSF1 (M-CSF) in myeloid cells / regulation of cell shape / protein autophosphorylation / regulation of inflammatory response / protein tyrosine kinase activity / cell differentiation / cytoskeleton / lysosome / protein phosphorylation / cell adhesion / defense response to Gram-positive bacterium / intracellular signal transduction / inflammatory response / signaling receptor binding / focal adhesion / intracellular membrane-bounded organelle / positive regulation of cell population proliferation / lipid binding / negative regulation of apoptotic process / Golgi apparatus / ATP binding / nucleus / plasma membrane / cytosol
Similarity search - Function
Tyrosine-protein kinase HCK, SH2 domain / SH2 domain / SHC Adaptor Protein / SH3 Domains / : / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain ...Tyrosine-protein kinase HCK, SH2 domain / SH2 domain / SHC Adaptor Protein / SH3 Domains / : / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH3 type barrels. / Src homology 3 domains / SH2 domain superfamily / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Roll / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-L1G / Tyrosine-protein kinase HCK
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsBorhani, D.W. / Burchat, A. / Calderwood, D.J. / Hirst, G.C. / Li, B. / Loew, A.
Citation
Journal: Bioorg.Med.Chem.Lett. / Year: 2006
Title: Discovery of A-770041, a Src-Family Selective Orally Active Lck Inhibitor that Prevents Organ Allograft Rejection.
Authors: Burchat, A. / Borhani, D.W. / Calderwood, D.J. / Hirst, G.C. / Li, B. / Stachlewitz, R.F.
#1: Journal: Bioorg.Med.Chem.Lett. / Year: 2004
Title: A-420983: A Potent, Orally Active Inhibitor of Lck with Efficacy in a Model of Transplant Rejection
Authors: Borhani, D.W. / Calderwood, D.J. / Friedman, M.M. / Hirst, G.C. / Li, B. / Leung, A.K.W. / Mcrae, B. / Ratnofsky, S. / Ritter, K. / Waegell, W.
History
DepositionSep 3, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 20, 2006Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Mar 6, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / struct_conn
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 1.3May 8, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method
Revision 1.4Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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_auth_asym_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_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
Revision 1.5Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TYROSINE-PROTEIN KINASE HCK
B: TYROSINE-PROTEIN KINASE HCK
hetero molecules


Theoretical massNumber of molelcules
Total (without water)105,2686
Polymers104,0002
Non-polymers1,2684
Water4,918273
1
A: TYROSINE-PROTEIN KINASE HCK
hetero molecules


Theoretical massNumber of molelcules
Total (without water)52,6343
Polymers52,0001
Non-polymers6342
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: TYROSINE-PROTEIN KINASE HCK
hetero molecules


Theoretical massNumber of molelcules
Total (without water)52,6343
Polymers52,0001
Non-polymers6342
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)49.078, 73.124, 179.485
Angle α, β, γ (deg.)90.00, 95.97, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22B

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ARGARGPROPRO5AA59 - 5058 - 454
21ARGARGPROPRO5BB59 - 5058 - 454
12L1GL1GL1GL1G4AC1506
22L1GL1GL1GL1G4BE1506

NCS ensembles :
ID
1
2

NCS oper: (Code: given
Matrix: (0.944154, 0.025026, -0.328552), (0.023364, -0.999687, -0.009006), (-0.328675, -0.000827, -0.944443)
Vector: 13.27254, 136.66725, 89.18681)

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Components

#1: Protein TYROSINE-PROTEIN KINASE HCK / HAEMATOPOETIC CELL KINASE HCK / P59-HCK/P60-HCK HEMOPOIETIC CELL KINASE


Mass: 52000.227 Da / Num. of mol.: 2 / Fragment: SH3-SH2-SH1, RESIDUES 80-525 / Mutation: YES
Source method: isolated from a genetically manipulated source
Details: SRC NUMBERING USED. ADD 20 TO THE RESIDUE NUMBERS IN THIS ENTRY TO OBTAIN ACTUAL HUMAN HCK RESIDUE NUMBERS. RESIDUE Y501 (HCK Y521) IS PHOSPHORYLATED
Source: (gene. exp.) HOMO SAPIENS (human) / Cell: LYMPHOCYTE / Plasmid: PBC HCK002 / Cell line (production host): SF9 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: P08631, EC: 2.7.1.112
#2: Chemical ChemComp-L1G / N-(4-{4-AMINO-1-[4-(4-METHYLPIPERAZIN-1-YL)-TRANS-CYCLOHEXYL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE


Mass: 593.722 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C33H39N9O2
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 273 / Source method: isolated from a natural source / Formula: H2O
Compound detailsENGINEERED RESIDUE IN CHAIN A, GLN 502 TO GLU ENGINEERED RESIDUE IN CHAIN A, GLN 503 TO GLU ...ENGINEERED RESIDUE IN CHAIN A, GLN 502 TO GLU ENGINEERED RESIDUE IN CHAIN A, GLN 503 TO GLU ENGINEERED RESIDUE IN CHAIN A, GLN 504 TO ILE ENGINEERED RESIDUE IN CHAIN B, GLN 502 TO GLU ENGINEERED RESIDUE IN CHAIN B, GLN 503 TO GLU ENGINEERED RESIDUE IN CHAIN B, GLN 504 TO ILE
Has protein modificationY
Sequence detailsTHE PROTEIN CRYSTALLIZED INCLUDED EIGHT NON-NATIVE N-TERMINAL RESIDUES: GLY-ALA-MET-GLY-SER-GLY-ILE- ...THE PROTEIN CRYSTALLIZED INCLUDED EIGHT NON-NATIVE N-TERMINAL RESIDUES: GLY-ALA-MET-GLY-SER-GLY-ILE-ARG. Q502E, Q503E, Q504I TRIPLE MUTANT TO INCREASE THE PHOSPHORYLATION OF Y501 (ALL SRC NUMBERING).

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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: 3.1 Å3/Da / Density % sol: 59.9 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8
Details: HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-420983 [100 MM STOCK SOLUTION OF THE BIS-MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-420983 CONCENTRATION OF 1 MM. HCK/A- ...Details: HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-420983 [100 MM STOCK SOLUTION OF THE BIS-MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-420983 CONCENTRATION OF 1 MM. HCK/A-420983 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1, 5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1.0332
DetectorType: MARRESEARCH / Detector: CCD / Date: Feb 7, 2002
RadiationMonochromator: SI(111) DOUBLE MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 2.3→15 Å / Num. obs: 50423 / % possible obs: 88.9 % / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Biso Wilson estimate: 54.7 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 13.8
Reflection shellResolution: 2.3→2.38 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 3.3 / % possible all: 75.5

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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 1AD5

1ad5


Resolution: 2.3→19.96 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.91 / SU B: 15.259 / SU ML: 0.192 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.341 / ESU R Free: 0.261 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE ACTIVATION LOOP (RESIDUES A386-A398 AND B386-B398) IS DISORDERED IN BOTH HCK MOLECULES (CHAINS A AND B). HCK CHAIN A IS SLIGHTLY BETTER ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE ACTIVATION LOOP (RESIDUES A386-A398 AND B386-B398) IS DISORDERED IN BOTH HCK MOLECULES (CHAINS A AND B). HCK CHAIN A IS SLIGHTLY BETTER ORDERED THAN CHAIN B. SIMILARLY, THE LIGAND A1506 IS BETTER ORDERED THAN B1506. SEVEN N-TERMINAL RESIDUES (FROM THE EXPRESSION VECTOR, GLY-ALA -MET-GLY-SER-GLY-ILE) ARE DISORDERED IN BOTH CHAINS. RESIDUE ARG-59 IS NON-NATIVE (EXPRESSION VECTOR).
RfactorNum. reflection% reflectionSelection details
Rfree0.274 2513 5 %RANDOM
Rwork0.222 ---
obs0.224 47904 89.9 %-
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: 50.47 Å2
Baniso -1Baniso -2Baniso -3
1-2.22 Å20 Å2-0.98 Å2
2---0.51 Å20 Å2
3----1.91 Å2
Refinement stepCycle: LAST / Resolution: 2.3→19.96 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6992 0 90 273 7355
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0227293
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.4061.979872
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2425870
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.71923.86329
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.268151291
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.0961546
X-RAY DIFFRACTIONr_chiral_restr0.0840.21043
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.025504
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.210.23325
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3080.24920
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1680.2419
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.1270.211
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1820.241
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2420.211
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5961.54473
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.0227037
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.50133302
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.2894.52835
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
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1736medium positional0.220.5
21A44medium positional0.070.5
22B44medium positional0.070.5
11A1762loose positional0.485
11A1736medium thermal0.662
21A44medium thermal0.462
22B44medium thermal0.462
11A1762loose thermal1.4110
LS refinement shellResolution: 2.3→2.36 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.385 151 -
Rwork0.281 3304 -
obs--84.89 %
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)
12.49630.82170.49264.7991-1.0462.3706-0.0354-0.0205-0.00630.3438-0.1342-0.135-0.60010.00440.1696-0.0840.0136-0.1004-0.10190.00960.00346.37793.01479.9315
21.8262-0.92041.8072.2471-2.29695.2061-0.43890.24530.28020.5987-0.2851-0.4461-1.17330.75770.724-0.0426-0.1898-0.18670.04330.15330.131625.853985.547230.8572
30.5805-0.20230.97190.7682-0.74432.76570.0694-0.0511-0.0452-0.07470.03880.13050.3146-0.2141-0.1082-0.2519-0.00510.0219-0.08770.0076-0.02053.754161.317323.0513
41.8963-1.1929-0.2745.6305-1.49674.14780.1808-0.07750.0320.0316-0.17660.03880.55410.0106-0.00410.31910.00190.0915-0.04380.0233-0.099418.463143.787177.792
52.1241-0.6057-0.45563.3178-1.06264.5336-0.0243-0.06210.04970.0939-0.0579-0.15670.49180.5310.0822-0.15310.08080.0335-0.00490.0261-0.064629.797151.454651.5889
60.31160.1053-0.431.1229-0.60784.90970.013-0.01510.01990.4387-0.04960.2024-0.9261-0.50070.03660.13590.1210.0435-0.0087-0.0399-0.010710.739475.240466.2431
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A59 - 115
2X-RAY DIFFRACTION1A223 - 228
3X-RAY DIFFRACTION2A116 - 222
4X-RAY DIFFRACTION2A495 - 505
5X-RAY DIFFRACTION2A1507
6X-RAY DIFFRACTION3A229 - 494
7X-RAY DIFFRACTION3A1506
8X-RAY DIFFRACTION4B59 - 115
9X-RAY DIFFRACTION4B223 - 228
10X-RAY DIFFRACTION5B116 - 222
11X-RAY DIFFRACTION5B495 - 505
12X-RAY DIFFRACTION5B1507
13X-RAY DIFFRACTION6B229 - 494
14X-RAY DIFFRACTION6B1506

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