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- PDB-3prm: Structural analysis of a viral OTU domain protease from the Crime... -

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Basic information

Entry
Database: PDB / ID: 3prm
TitleStructural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic Fever virus in complex with human ubiquitin
Components
  • Polyubiquitin-B (Fragment)
  • RNA-directed RNA polymerase L
KeywordsHYDROLASE/HYDROLASE / ubiquitin hydrolase / deubiquitinase / hydrolase / cysteine protease / viral protein / HYDROLASE-HYDROLASE complex
Function / homology
Function and homology information


RNA-templated viral transcription / negative stranded viral RNA replication / Maturation of protein E / Maturation of protein E / 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 ...RNA-templated viral transcription / negative stranded viral RNA replication / Maturation of protein E / Maturation of protein E / 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 / Constitutive Signaling by NOTCH1 HD Domain Mutants / NOTCH2 Activation and Transmission of Signal to the Nucleus / Endosomal Sorting Complex Required For Transport (ESCRT) / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of FZD by ubiquitination / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / InlA-mediated entry of Listeria monocytogenes into host cells / Pexophagy / Regulation of innate immune responses to cytosolic DNA / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Activated NOTCH1 Transmits Signal to the Nucleus / Translesion synthesis by REV1 / NF-kB is activated and signals survival / Regulation of PTEN localization / Translesion synthesis by POLK / Regulation of BACH1 activity / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Regulation of activated PAK-2p34 by proteasome mediated degradation / InlB-mediated entry of Listeria monocytogenes into host cell / IKK complex recruitment mediated by RIP1 / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / TNFR1-induced NF-kappa-B signaling pathway / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / Regulation of NF-kappa B signaling / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Negative regulators of DDX58/IFIH1 signaling / NOTCH3 Activation and Transmission of Signal to the Nucleus / TNFR2 non-canonical NF-kB pathway / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Recognition of DNA damage by PCNA-containing replication complex / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Negative regulation of FGFR3 signaling / Peroxisomal protein import / Termination of translesion DNA synthesis / Degradation of AXIN / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Regulation of TNFR1 signaling / Defective CFTR causes cystic fibrosis / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Hedgehog ligand biogenesis / Negative regulation of FGFR2 signaling / Negative regulation of FGFR4 signaling / Stabilization of p53 / EGFR downregulation / Negative regulation of FGFR1 signaling / Negative regulation of NOTCH4 signaling / Iron uptake and transport / G2/M Checkpoints / Translesion Synthesis by POLH
Similarity search - Function
: / RNA-directed RNA polymerase, nairovirus / Cathepsin B; Chain A - #80 / OTU-like cysteine protease / OTU domain / OTU domain profile. / RNA-dependent RNA polymerase, bunyaviral / Bunyavirus RNA dependent RNA polymerase / RNA-directed RNA polymerase, negative-strand RNA virus / RdRp of negative ssRNA viruses with segmented genomes catalytic domain profile. ...: / RNA-directed RNA polymerase, nairovirus / Cathepsin B; Chain A - #80 / OTU-like cysteine protease / OTU domain / OTU domain profile. / RNA-dependent RNA polymerase, bunyaviral / Bunyavirus RNA dependent RNA polymerase / RNA-directed RNA polymerase, negative-strand RNA virus / RdRp of negative ssRNA viruses with segmented genomes catalytic domain profile. / Cathepsin B; Chain A / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Papain-like cysteine peptidase superfamily / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin domain signature. / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Ubiquitin-like domain superfamily / Roll / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Ubiquitin B / Polyubiquitin-C / RNA-directed RNA polymerase L / RNA-directed RNA polymerase L
Similarity search - Component
Biological speciesCrimean-Congo hemorrhagic fever virus
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.3 Å
AuthorsCapodagli, G.C. / McKercher, M.A. / Baker, E.A. / Masters, E.M. / Brunzelle, J.S. / Pegan, S.D.
CitationJournal: J.Virol. / Year: 2011
Title: Structural analysis of a viral ovarian tumor domain protease from the crimean-congo hemorrhagic Fever virus in complex with covalently bonded ubiquitin.
Authors: Capodagli, G.C. / McKercher, M.A. / Baker, E.A. / Masters, E.M. / Brunzelle, J.S. / Pegan, S.D.
History
DepositionNov 30, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 26, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 2.0Feb 22, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Polymer sequence / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / database_2 / entity / entity_name_com / entity_poly / entity_poly_seq / entity_src_gen / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_assembly_gen / pdbx_struct_mod_residue / pdbx_unobs_or_zero_occ_atoms / struct_asym / struct_conn / struct_ref / struct_ref_seq / struct_ref_seq_dif / struct_site
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.group_PDB / _atom_site.label_alt_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.label_seq_id / _atom_site.occupancy / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_poly.nstd_monomer / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_seq_type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_mod_residue.details / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_id / _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_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_ref.db_code / _struct_ref.pdbx_db_accession / _struct_ref_seq.pdbx_db_accession / _struct_site.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: RNA-directed RNA polymerase L
B: Polyubiquitin-B (Fragment)
C: RNA-directed RNA polymerase L
D: Polyubiquitin-B (Fragment)


Theoretical massNumber of molelcules
Total (without water)58,4284
Polymers58,4284
Non-polymers00
Water3,963220
1
A: RNA-directed RNA polymerase L
B: Polyubiquitin-B (Fragment)


Theoretical massNumber of molelcules
Total (without water)29,2142
Polymers29,2142
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2290 Å2
ΔGint-11 kcal/mol
Surface area11410 Å2
MethodPISA
2
C: RNA-directed RNA polymerase L
D: Polyubiquitin-B (Fragment)


Theoretical massNumber of molelcules
Total (without water)29,2142
Polymers29,2142
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2280 Å2
ΔGint-11 kcal/mol
Surface area11400 Å2
MethodPISA
Unit cell
Length a, b, c (Å)60.462, 65.651, 133.133
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein RNA-directed RNA polymerase L / Protein L / Large structural protein / Replicase / Transcriptase


Mass: 20574.312 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Crimean-Congo hemorrhagic fever virus / Strain: IbAr10200 / Plasmid: pET11A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q6TQR6, UniProt: Q6TFZ7*PLUS, ubiquitinyl hydrolase 1, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases, Hydrolases; Acting on ester bonds, RNA-directed RNA polymerase
#2: Protein Polyubiquitin-B (Fragment)


Mass: 8639.770 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Plasmid: pTYB2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 CodonPlus / References: UniProt: J3QS39, UniProt: P0CG48*PLUS
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 220 / 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: 2.27 Å3/Da / Density % sol: 45.83 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 22-26% PEG 8000, 0.1 M Na cacodylate, 0.2 M Mg acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 0.978 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Oct 31, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.978 Å / Relative weight: 1
ReflectionResolution: 2.3→66.57 Å / Num. all: 24243 / Num. obs: 23928 / % possible obs: 98.7 % / Rmerge(I) obs: 0.072
Reflection shellResolution: 2.3→2.34 Å / Rmerge(I) obs: 0.322 / % possible all: 100

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Processing

Software
NameVersionClassificationNB
REFMACrefinement
PDB_EXTRACT3.1data extraction
HKL-2000data collection
DENZOdata reduction
SCALEPACKdata scaling
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 2.3→29.48 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.903 / WRfactor Rfree: 0.2624 / WRfactor Rwork: 0.1961 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.8116 / SU B: 16.219 / SU ML: 0.183 / SU R Cruickshank DPI: 0.4011 / SU Rfree: 0.2697 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.401 / ESU R Free: 0.27 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2672 1212 5.1 %RANDOM
Rwork0.2043 ---
obs0.2076 23872 98.42 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 91.87 Å2 / Biso mean: 34.7658 Å2 / Biso min: 12.79 Å2
Baniso -1Baniso -2Baniso -3
1-3.84 Å2-0 Å2-0 Å2
2---2.21 Å20 Å2
3----1.64 Å2
Refinement stepCycle: LAST / Resolution: 2.3→29.48 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3788 0 8 220 4016
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.0224040
X-RAY DIFFRACTIONr_angle_refined_deg1.6421.9585487
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.6685505
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.35724.264197
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.32215722
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.1811528
X-RAY DIFFRACTIONr_chiral_restr0.110.2607
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0213094
X-RAY DIFFRACTIONr_mcbond_it0.7571.52455
X-RAY DIFFRACTIONr_mcangle_it1.3623996
X-RAY DIFFRACTIONr_scbond_it2.69931585
X-RAY DIFFRACTIONr_scangle_it4.0964.51490
LS refinement shellResolution: 2.3→2.36 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.335 85 -
Rwork0.229 1633 -
all-1718 -
obs--97.06 %
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)
16.76985.90351.96822.77546.38915.64680.1703-0.05340.78790.2104-0.34110.8566-0.6434-0.32220.17080.14160.01510.0170.24740.01450.2307-23.41841.38450.3297
20.2074-0.4920.65832.2658-0.72162.7767-0.08280.01010.05390.1393-0.0459-0.1189-0.28840.05960.12870.04770.00590.01720.07870.00360.0969-11.3857-4.31017.3346
30.2212-0.8984-0.27633.87441.17820.3599-0.2143-0.0929-0.01011.07650.14050.12570.32350.05260.07380.36290.02460.04260.3837-0.03980.191-9.8555-11.520622.3155
43.6244-0.12280.14125.3843-1.41170.4813-0.08990.0731-0.304-0.1470.2140.44080.1728-0.1748-0.12410.2431-0.10450.01790.19290.02240.1938-16.2061-25.64568.345
50.113-0.47250.12375.2962-1.55410.4655-0.0213-0.1162-0.1057-0.11360.01060.05810.07660.01730.01070.23420.05450.0340.25260.09350.2221-8.4853-21.586710.2072
610.70423.9227-4.07938.5766-2.9726.7045-0.0475-0.207-0.14360.1641-0.1045-0.03340.04650.1450.1520.0330.0325-0.03450.0554-0.05690.0775-15.9921-6.05864.7627
75.0767-2.47940.21215.1070.70262.8716-0.10830.0090.08390.00390.047-0.0107-0.2060.00970.06130.06910.0002-0.01710.04250.00860.0302-10.9518-3.79078.8478
814.2562-23.2443-8.359740.03947.415222.9567-0.4497-0.033-0.41550.94380.52020.8072-0.2465-1.3062-0.07050.27410.0371-0.03270.3542-0.03760.3733-18.25849.869113.2771
94.96880.5867-0.38466.27562.65775.0920.08610.2579-0.0178-0.27730.1744-0.0257-0.18410.0246-0.26050.1242-0.02010.00010.09180.03280.1122-14.5069-10.3864-17.9751
106.5080.3435-2.64774.77943.6714.1293-0.24360.2457-0.11280.27690.3229-0.11390.33490.1754-0.07920.22120.0562-0.02240.1487-0.06880.2132-12.0023-23.0597-18.4695
112.99830.06710.71770.57871.18775.12110.1261-0.0033-0.3538-0.0133-0.0009-0.22860.30830.1305-0.12520.09060.01480.01820.0810.00880.2038-14.8483-19.7641-11.9412
125.7680.37075.13571.65031.26158.9362-0.28710.44120.3201-0.3601-0.08610.0874-0.29010.08560.37320.1228-0.01450.0220.09090.01670.1074-16.0933-14.4275-10.9594
134.5373-3.81480.722214.964810.612210.82750.67920.1592-0.44520.0637-0.96510.69710.6703-0.84630.28590.4629-0.00680.01240.39330.07790.4167-22.3901-0.3612-19.8159
140.19370.4047-0.44093.5063-0.7873.2356-0.17490.0678-0.0119-0.11670.0749-0.17070.34360.10160.10.1951-0.0503-0.04260.1650.00610.1353-12.63587.976-22.0066
155.34440.9881-4.16766.41295.890310.5515-0.42050.81350.0511-0.38590.4492-0.00130.0461-0.0265-0.02860.2869-0.0070.08640.52440.05160.1478-7.495514.2519-37.0612
1623.9579-7.5537-14.50182.90166.063813.09380.02271.06811.1657-0.2727-0.0545-0.1607-0.7132-0.10620.03180.4532-0.1510.04660.23170.06360.2572-9.783923.5292-37.2957
173.2617-1.04341.50364.0898-3.975711.9048-0.1547-0.34210.4177-0.02990.0180.2337-0.4402-0.80360.13670.19370.0330.02090.21520.00030.2125-17.942729.4521-24.5193
188.1327-3.27-3.02833.9733.70658.54410.1110.27770.2441-0.3839-0.1345-0.4645-0.23880.05530.02350.2283-0.05240.04050.162-0.00920.2427-8.248932.7884-27.2584
192.78050.985-0.51765.0637-0.77824.4936-0.12780.162-0.0324-0.39760.1037-0.1010.3498-0.07650.02410.1579-0.01770.0470.1266-0.03160.1274-13.445113.2896-24.5165
203.6449-0.2771-1.55949.979-0.73431.00410.0775-0.0111-0.3261-0.0128-0.153-0.16540.284-0.16420.07550.5468-0.065-0.01920.29850.09780.1497-9.03565.1504-26.8555
217.296-2.21970.67678.9308-2.34950.6215-0.2361-0.15390.06830.40230.29260.2538-0.0879-0.0819-0.05650.2162-0.02740.00820.07450.01590.1814-16.534816.1395-0.0751
221.0492-2.3242-0.200718.97910.53930.1033-0.044-0.13530.15980.32730.07670.30120.08870.0821-0.03270.16140.0115-0.02120.1371-0.00680.2031-14.084720.80621.8745
234.47290.3464-0.80513.09750.53185.53820.08890.13670.4209-0.04530.0471-0.1406-0.30350.1652-0.1360.1301-0.0043-0.00430.1077-0.01820.1473-13.762424.7608-5.1837
246.9611.2022-6.08572.6798-1.079.8867-0.2762-0.254-0.1890.11670.12140.11720.40390.04490.15490.11130.0044-0.04940.05430.00360.1849-16.043419.4493-7.0752
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 11
2X-RAY DIFFRACTION2A12 - 46
3X-RAY DIFFRACTION3A47 - 62
4X-RAY DIFFRACTION4A63 - 87
5X-RAY DIFFRACTION5A88 - 109
6X-RAY DIFFRACTION6A110 - 137
7X-RAY DIFFRACTION7A138 - 157
8X-RAY DIFFRACTION8A158 - 162
9X-RAY DIFFRACTION9B1 - 17
10X-RAY DIFFRACTION10B18 - 29
11X-RAY DIFFRACTION11B30 - 60
12X-RAY DIFFRACTION12B61 - 75
13X-RAY DIFFRACTION13C2 - 8
14X-RAY DIFFRACTION14C9 - 39
15X-RAY DIFFRACTION15C40 - 57
16X-RAY DIFFRACTION16C58 - 66
17X-RAY DIFFRACTION17C67 - 81
18X-RAY DIFFRACTION18C82 - 95
19X-RAY DIFFRACTION19C96 - 145
20X-RAY DIFFRACTION20C146 - 162
21X-RAY DIFFRACTION21D1 - 8
22X-RAY DIFFRACTION22D9 - 23
23X-RAY DIFFRACTION23D24 - 60
24X-RAY DIFFRACTION24D61 - 75

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