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- PDB-3n3k: The catalytic domain of USP8 in complex with a USP8 specific inhibitor -

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Basic information

Entry
Database: PDB / ID: 3n3k
TitleThe catalytic domain of USP8 in complex with a USP8 specific inhibitor
Components
  • Ubiquitin
  • Ubiquitin carboxyl-terminal hydrolase 8
KeywordsHYDROLASE / PROTEASE / THIOL PROTEASE / UBL CONJUGATION PATHWAY / DEUBIQUITINATING ENZYME / DUB / ZINC RIBBON / INHIBITOR / UBIQUITIN / Isopeptide bond / Nucleus / Phosphoprotein / Structural Genomics / Structural Genomics Consortium / SGC
Function / homology
Function and homology information


negative regulation of lysosomal protein catabolic process / : / : / protein modification process => GO:0036211 / endosome organization / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / protein K48-linked deubiquitination / K48-linked deubiquitinase activity / protein K63-linked deubiquitination / K63-linked deubiquitinase activity ...negative regulation of lysosomal protein catabolic process / : / : / protein modification process => GO:0036211 / endosome organization / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / protein K48-linked deubiquitination / K48-linked deubiquitinase activity / protein K63-linked deubiquitination / K63-linked deubiquitinase activity / positive regulation of amyloid fibril formation / mitotic cytokinesis / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / Viral mRNA Translation / protein deubiquitination / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Maturation of protein E / Maturation of protein E / cytosolic ribosome / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / cellular response to dexamethasone stimulus / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / Regulation of innate immune responses to cytosolic DNA / NF-kB is activated and signals survival / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLK / InlB-mediated entry of Listeria monocytogenes into host cell / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / Translesion synthesis by POLI / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / TCF dependent signaling in response to WNT / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / activated TAK1 mediates p38 MAPK activation / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / Regulation of signaling by CBL / NOTCH3 Activation and Transmission of Signal to the Nucleus / Vpu mediated degradation of CD4
Similarity search - Function
: / USP8 WW domain / USP8 dimerisation domain / USP8 dimerisation domain / : / Rhodanese-like domain / Rhodanese domain profile. / Rhodanese-like domain superfamily / Rhodanese-like domain / Ubiquitin specific protease (USP) domain signature 2. ...: / USP8 WW domain / USP8 dimerisation domain / USP8 dimerisation domain / : / Rhodanese-like domain / Rhodanese domain profile. / Rhodanese-like domain superfamily / Rhodanese-like domain / Ubiquitin specific protease (USP) domain signature 2. / Ubiquitin specific protease (USP) domain signature 1. / Ubiquitin specific protease, conserved site / Peptidase C19, ubiquitin carboxyl-terminal hydrolase / Ubiquitin carboxyl-terminal hydrolase / Ubiquitin specific protease domain / Ubiquitin specific protease (USP) domain profile. / Cysteine proteinases / Cathepsin B; Chain A / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Papain-like cysteine peptidase superfamily / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-C / Ubiquitin carboxyl-terminal hydrolase 8 / Ubiquitin-60S ribosomal protein L40
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / molecular replacement / Resolution: 2.6 Å
AuthorsWalker, J.R. / Avvakumov, G.V. / Xue, S. / Li, Y. / Allali-Hassani, A. / Lam, R. / Ernst, A. / Sidhu, S. / Weigelt, J. / Bountra, C. ...Walker, J.R. / Avvakumov, G.V. / Xue, S. / Li, Y. / Allali-Hassani, A. / Lam, R. / Ernst, A. / Sidhu, S. / Weigelt, J. / Bountra, C. / Arrowsmith, C.H. / Edwards, A.M. / Bochkarev, A. / Dhe-Paganon, S. / Structural Genomics Consortium / Structural Genomics Consortium (SGC)
Citation
Journal: Science / Year: 2013
Title: A strategy for modulation of enzymes in the ubiquitin system.
Authors: Ernst, A. / Avvakumov, G. / Tong, J. / Fan, Y. / Zhao, Y. / Alberts, P. / Persaud, A. / Walker, J.R. / Neculai, A.M. / Neculai, D. / Vorobyov, A. / Garg, P. / Beatty, L. / Chan, P.K. / ...Authors: Ernst, A. / Avvakumov, G. / Tong, J. / Fan, Y. / Zhao, Y. / Alberts, P. / Persaud, A. / Walker, J.R. / Neculai, A.M. / Neculai, D. / Vorobyov, A. / Garg, P. / Beatty, L. / Chan, P.K. / Juang, Y.C. / Landry, M.C. / Yeh, C. / Zeqiraj, E. / Karamboulas, K. / Allali-Hassani, A. / Vedadi, M. / Tyers, M. / Moffat, J. / Sicheri, F. / Pelletier, L. / Durocher, D. / Raught, B. / Rotin, D. / Yang, J. / Moran, M.F. / Dhe-Paganon, S. / Sidhu, S.S.
#1: Journal: J.Biol.Chem. / Year: 2006
Title: Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8).
Authors: Avvakumov, G.V. / Walker, J.R. / Xue, S. / Finerty, P.J. / Mackenzie, F. / Newman, E.M. / Dhe-Paganon, S.
History
DepositionMay 20, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 23, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Feb 27, 2013Group: Database references
Revision 1.3Mar 14, 2018Group: Database references / Category: struct_ref_seq_dif / Item: _struct_ref_seq_dif.details
Revision 1.4Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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_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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin carboxyl-terminal hydrolase 8
B: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,7513
Polymers54,6862
Non-polymers651
Water2,018112
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2830 Å2
ΔGint-13 kcal/mol
Surface area19010 Å2
MethodPISA
Unit cell
Length a, b, c (Å)69.983, 69.983, 181.549
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number169
Space group name H-MP61

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Components

#1: Protein Ubiquitin carboxyl-terminal hydrolase 8 / Ubiquitin thioesterase 8 / Ubiquitin-specific-processing protease 8 / Deubiquitinating enzyme 8 / ...Ubiquitin thioesterase 8 / Ubiquitin-specific-processing protease 8 / Deubiquitinating enzyme 8 / Ubiquitin isopeptidase Y / hUBPy


Mass: 45418.457 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KIAA0055, UBPY, USP8 / Plasmid: PET28-LIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: P40818, EC: 3.1.2.15
#2: Protein Ubiquitin


Mass: 9267.615 Da / Num. of mol.: 1
Mutation: Q2R, F4V, T9M, K11R, T14I, Q62H, K63N, E64H, T66A, H68Y, V70L, R72K
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RPS27A, UBA52, UBA80, UBB, UBC, UBCEP1, UBCEP2, UBQ / Plasmid: PET28ALIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: P62988, UniProt: P0CG48*PLUS
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 112 / Source method: isolated from a natural source / Formula: H2O

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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: 2.35 Å3/Da / Density % sol: 47.59 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.3
Details: 24% PEG3350, 0.1 M BIS-TRIS, 0.2 M AMMONIUM ACETATE, 1 MM DTT, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.97949
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: May 13, 2010
RadiationMonochromator: double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97949 Å / Relative weight: 1
ReflectionResolution: 2.6→37 Å / Num. all: 15464 / Num. obs: 15464 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 11.6 % / Rsym value: 0.161 / Net I/σ(I): 17.14
Reflection shellResolution: 2.6→2.69 Å / Redundancy: 11.6 % / Mean I/σ(I) obs: 5.89 / Num. unique all: 1555 / Rsym value: 0.537 / % possible all: 100

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.5.0102refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: molecular replacement
Starting model: PDB entries 2GFO, 3MTN

2gfo

3mtn


Resolution: 2.6→34.99 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.891 / SU B: 22.248 / SU ML: 0.216 / Cross valid method: THROUGHOUT / ESU R Free: 0.318 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24237 769 5 %RANDOM
Rwork0.17777 ---
obs0.18083 14633 99.95 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 33.151 Å2
Baniso -1Baniso -2Baniso -3
1--0.36 Å2-0.18 Å20 Å2
2---0.36 Å20 Å2
3---0.54 Å2
Refinement stepCycle: LAST / Resolution: 2.6→34.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3463 0 1 112 3576
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0223567
X-RAY DIFFRACTIONr_angle_refined_deg1.0181.9554809
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.4655432
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.47724.4175
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.93315653
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.6921520
X-RAY DIFFRACTIONr_chiral_restr0.0770.2518
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0212694
X-RAY DIFFRACTIONr_mcbond_it0.3641.52149
X-RAY DIFFRACTIONr_mcangle_it0.71223456
X-RAY DIFFRACTIONr_scbond_it0.99531418
X-RAY DIFFRACTIONr_scangle_it1.6914.51353
LS refinement shellResolution: 2.6→2.669 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.321 60 -
Rwork0.244 1063 -
obs--99.73 %
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)
116.38495.6546-5.72041.5276-2.15981.46990.2789-0.04960.41180.1332-0.04750.1841-0.1510.008-0.23150.33030.15190.11210.1695-0.14680.3937-1.14651.5572-3.7201
24.01351.1889-0.10783.32413.03284.50770.0870.08760.35740.12670.03190.0178-0.061-0.0432-0.1190.1632-0.01-0.04350.01830.01560.18348.9978-1.7997-7.6277
30.78070.22030.08390.66880.40380.2257-0.0471-0.00430.1012-0.0497-0.03020.118-0.03720.00810.07730.1441-0.0194-0.01650.10840.01340.13424.7383-14.0659-9.9334
43.79532.3612-1.27224.281-1.76023.25540.00810.0950.68010.03410.17440.5249-0.2221-0.2922-0.18240.09320.0362-0.03250.1235-0.03080.2494-13.6241-10.6837-10.9981
51.60360.8427-0.11441.3572-0.39531.30240.0189-0.13490.11420.1409-0.09750.0841-0.1003-0.11770.07860.14370.0102-0.00180.1137-0.02830.1476-0.2384-11.1329-4.0012
62.2451-0.04290.97850.65810.18891.29320.10040.02760.0670.0862-0.13660.0660.0048-0.00320.03620.1392-0.01150.01280.14-0.01120.1268-3.2934-21.9525-5.4593
72.58270.9577-0.99462.55541.76422.1665-0.3078-0.09780.0826-0.0671-0.33460.81780.1835-0.28240.64240.2439-0.0311-0.09710.2039-0.03590.332-23.9573-33.1261-14.7982
87.40821.93613.891112.68976.43244.23160.29470.5707-0.1829-0.5411-0.31690.2395-0.14520.00510.02210.16380.017-0.05090.42760.03420.11-17.8908-37.7292-26.2561
91.18251.00110.34390.90510.49480.724-0.0545-0.01920.1262-0.0385-0.02170.11160.0365-0.08720.07630.1206-0.02170.00490.11870.01690.1477-12.9963-27.1293-18.6016
100.83820.874-0.54110.9287-0.50110.5179-0.11750.0354-0.1186-0.12970.0647-0.05930.107-0.01110.05280.14710.005-0.01950.11880.00270.2059-1.2369-41.9922-16.9596
112.48222.6004-1.33993.0376-1.10050.9350.07-0.15810.09540.203-0.03260.01070.10220.2127-0.03740.19230.023-0.02590.11480.02070.2012-9.269-51.2953-8.5887
120.36940.32720.11870.37480.15330.06070.0568-0.0656-0.13550.1002-0.04-0.02680.0614-0.0256-0.01680.1799-0.0304-0.03650.14540.04310.18810.553-38.6458-11.5713
130.83060.8091-0.44681.2843-0.43471.6109-0.01390.2273-0.0269-0.13510.06760.05790.13220.177-0.05370.1120.0477-0.00510.1672-0.04220.14636.1921-32.9898-23.0112
141.1296-0.2461.11640.79490.0571.3224-0.03540.09490.0489-0.00010.0049-0.1324-0.13640.0590.03050.114-0.01040.00640.12990.0040.132411.9015-20.8227-15.2498
151.28360.34920.39710.66620.45930.3507-0.0410.10650.0139-0.05330.0681-0.1028-0.04730.1066-0.02710.1155-0.03820.00330.16370.03010.151713.6018-19.695-16.5907
160.155-0.4847-0.82181.30350.23574.81-0.17380.0507-0.01190.37650.16530.07240.3472-0.57550.00850.1915-0.0650.05530.20130.02830.1362-15.195-32.8535-3.8824
1710.12763.0022-5.78921.4037-2.67236.21740.46280.1299-0.54510.2898-0.17550.1012-0.161-0.2828-0.28730.2629-0.18380.06550.3442-0.020.2032-14.2239-35.5263-6.667
1811.28991.885-13.38980.4311-2.281913.5672-0.14320.2113-0.57690.1882-0.4286-0.0250.0608-0.15560.57180.1991-0.31270.12170.6812-0.07650.1499-16.8659-39.05027.2872
1910.3961-2.91912.5634.15992.58924.2051-0.03040.02180.0655-0.1371-0.1820.1630.0018-0.14790.21240.2463-0.1168-0.04230.10170.02030.2117-10.4171-43.5057-1.7781
202.83193.1525-1.04945.11291.14043.1510.341-0.2544-0.19150.5105-0.2009-0.40780.11760.1349-0.14010.1702-0.1151-0.04180.20840.01110.1209-6.3424-33.96153.5473
214.87570.30760.70866.52150.03597.29420.4436-0.90480.22950.1994-0.39150.37190.0892-0.1317-0.05220.1913-0.10540.11640.275-0.03840.0837-14.1122-30.67339.6865
221.00551.2236-0.62631.69430.50083.50210.0328-0.06210.08010.1502-0.17260.0184-0.0991-0.38310.13980.21580.0095-0.0660.2544-0.06850.2268-15.466-29.4622-1.1608
2318.64241.39985.6305-3.23581.2593-0.22980.0285-0.12970.5963-0.0821-0.138-0.14370.24320.00430.10951.2872-0.1435-0.23930.14340.32430.54781.8325-37.66510.5635
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A756 - 763
2X-RAY DIFFRACTION2A764 - 775
3X-RAY DIFFRACTION3A776 - 805
4X-RAY DIFFRACTION4A806 - 820
5X-RAY DIFFRACTION5A821 - 862
6X-RAY DIFFRACTION6A863 - 886
7X-RAY DIFFRACTION7A887 - 901
8X-RAY DIFFRACTION8A902 - 910
9X-RAY DIFFRACTION9A911 - 932
10X-RAY DIFFRACTION10A933 - 971
11X-RAY DIFFRACTION11A972 - 990
12X-RAY DIFFRACTION12A991 - 1020
13X-RAY DIFFRACTION13A1021 - 1049
14X-RAY DIFFRACTION14A1050 - 1079
15X-RAY DIFFRACTION15A1080 - 1110
16X-RAY DIFFRACTION16B1 - 8
17X-RAY DIFFRACTION17B9 - 17
18X-RAY DIFFRACTION18B18 - 27
19X-RAY DIFFRACTION19B28 - 38
20X-RAY DIFFRACTION20B39 - 46
21X-RAY DIFFRACTION21B47 - 62
22X-RAY DIFFRACTION22B63 - 69
23X-RAY DIFFRACTION23B70 - 74

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