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- PDB-7aks: Human ADP-ribosylserine hydrolase ARH3 mutant E41A in complex wit... -

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Basic information

Entry
Database: PDB / ID: 7aks
TitleHuman ADP-ribosylserine hydrolase ARH3 mutant E41A in complex with H2B-S7-mar peptide
Components
  • ADP-ribose glycohydrolase ARH3
  • modified peptide
KeywordsHYDROLASE / ADP-RIBOSYLATION / ADP-RIBOSE / ADPRHL2 / ADP-RIBOSYLHYDROLASE LIKE 2 / SER-ADPR / SERINE-ADPR / ADP-RIBOSYL-L-SERINE
Function / homology
Function and homology information


cellular response to superoxide / peptidyl-serine ADP-deribosylation / ADP-ribosylserine hydrolase activity / O-acetyl-ADP-ribose deacetylase activity / poly(ADP-ribose) glycohydrolase activity / poly(ADP-ribose) glycohydrolase / negative regulation of necroptotic process / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds / site of DNA damage ...cellular response to superoxide / peptidyl-serine ADP-deribosylation / ADP-ribosylserine hydrolase activity / O-acetyl-ADP-ribose deacetylase activity / poly(ADP-ribose) glycohydrolase activity / poly(ADP-ribose) glycohydrolase / negative regulation of necroptotic process / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds / site of DNA damage / POLB-Dependent Long Patch Base Excision Repair / hydrolase activity, hydrolyzing O-glycosyl compounds / base-excision repair, gap-filling / nuclear body / mitochondrial matrix / DNA repair / magnesium ion binding / mitochondrion / nucleoplasm / nucleus / cytoplasm
Similarity search - Function
ADP-ribosylation/Crystallin J1 / ADP-ribosylglycohydrolase / ADP-ribosylation/Crystallin J1 superfamily / :
Similarity search - Domain/homology
ACETATE ION / Chem-AR6 / ADP-ribosylhydrolase ARH3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.86 Å
AuthorsAriza, A.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Wellcome Trust101794 United Kingdom
Wellcome Trust210634 United Kingdom
CitationJournal: Nat Commun / Year: 2021
Title: Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.
Authors: Rack, J.G.M. / Liu, Q. / Zorzini, V. / Voorneveld, J. / Ariza, A. / Honarmand Ebrahimi, K. / Reber, J.M. / Krassnig, S.C. / Ahel, D. / van der Marel, G.A. / Mangerich, A. / McCullagh, J.S.O. ...Authors: Rack, J.G.M. / Liu, Q. / Zorzini, V. / Voorneveld, J. / Ariza, A. / Honarmand Ebrahimi, K. / Reber, J.M. / Krassnig, S.C. / Ahel, D. / van der Marel, G.A. / Mangerich, A. / McCullagh, J.S.O. / Filippov, D.V. / Ahel, I.
History
DepositionOct 2, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 16, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 6, 2021Group: Data collection / Database references
Category: citation / citation_author ...citation / citation_author / database_2 / database_PDB_rev / database_PDB_rev_record / diffrn_source / pdbx_database_proc
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site
Revision 1.2Jan 31, 2024Group: Data collection / Derived calculations ...Data collection / Derived calculations / Refinement description / Source and taxonomy
Category: atom_type / chem_comp_atom ...atom_type / chem_comp_atom / chem_comp_bond / diffrn_source / entity_src_gen / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z ..._atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z / _diffrn_source.pdbx_synchrotron_site / _entity_src_gen.gene_src_common_name / _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
AAA: ADP-ribose glycohydrolase ARH3
BaB: modified peptide
CCC: ADP-ribose glycohydrolase ARH3
DaD: modified peptide
EEE: ADP-ribose glycohydrolase ARH3
FaF: modified peptide
GGG: ADP-ribose glycohydrolase ARH3
HaH: modified peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)160,85968
Polymers155,5708
Non-polymers5,28960
Water13,655758
1
AAA: ADP-ribose glycohydrolase ARH3
BaB: modified peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,04114
Polymers38,8932
Non-polymers1,14812
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3560 Å2
ΔGint-20 kcal/mol
Surface area13970 Å2
MethodPISA
2
CCC: ADP-ribose glycohydrolase ARH3
DaD: modified peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,37020
Polymers38,8932
Non-polymers1,47718
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3650 Å2
ΔGint-23 kcal/mol
Surface area14050 Å2
MethodPISA
3
EEE: ADP-ribose glycohydrolase ARH3
FaF: modified peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,34819
Polymers38,8932
Non-polymers1,45617
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3420 Å2
ΔGint-19 kcal/mol
Surface area14430 Å2
MethodPISA
4
GGG: ADP-ribose glycohydrolase ARH3
HaH: modified peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,10015
Polymers38,8932
Non-polymers1,20713
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4180 Å2
ΔGint-13 kcal/mol
Surface area13840 Å2
MethodPISA
Unit cell
Length a, b, c (Å)123.360, 158.638, 74.920
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11AAA
21CCC
32AAA
42EEE
53AAA
63GGG
74CCC
84EEE
95CCC
105GGG
116EEE
126GGG

NCS domain segments:

Beg auth comp-ID: SER / Beg label comp-ID: SER / End auth comp-ID: GLN / End label comp-ID: GLN / Auth seq-ID: 18 - 361 / Label seq-ID: 4 - 347

Dom-IDComponent-IDEns-IDAuth asym-IDLabel asym-ID
111AAAA
221CCCC
332AAAA
442EEEE
553AAAA
663GGGG
774CCCC
884EEEE
995CCCC
10105GGGG
11116EEEE
12126GGGG

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12

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Components

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Protein / Protein/peptide , 2 types, 8 molecules AAACCCEEEGGGBaBDaDFaFHaH

#1: Protein
ADP-ribose glycohydrolase ARH3 / ADP-ribosylhydrolase 3 / O-acetyl-ADP-ribose deacetylase ARH3 / Poly(ADP-ribose) glycohydrolase ...ADP-ribosylhydrolase 3 / O-acetyl-ADP-ribose deacetylase ARH3 / Poly(ADP-ribose) glycohydrolase ARH3 / [Protein ADP-ribosylarginine] hydrolase-like protein 2 / [Protein ADP-ribosylserine] hydrolase


Mass: 37796.262 Da / Num. of mol.: 4 / Mutation: E41A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ADPRS, ADPRHL2, ARH3 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9NX46, Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides, poly(ADP-ribose) glycohydrolase, Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds
#2: Protein/peptide
modified peptide


Mass: 1096.299 Da / Num. of mol.: 4 / Mutation: E41A / Source method: obtained synthetically
Details: chemically sinthesised peptide with ADP-ribosylated serine
Source: (synth.) Homo sapiens (human)
References: Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides, poly(ADP-ribose) glycohydrolase, Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds

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Non-polymers , 5 types, 818 molecules

#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Mg
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 19 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical...
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 28 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical
ChemComp-AR6 / [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE / Adenosine-5-Diphosphoribose


Mass: 559.316 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C15H23N5O14P2 / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 758 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.51 Å3/Da / Density % sol: 50.91 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop
Details: sodium citrate (pH 6.1), 18% (w/v) PEG4000 and 400 mM ammonium acetate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.96863 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Sep 20, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.96863 Å / Relative weight: 1
ReflectionResolution: 1.86→158.62 Å / Num. obs: 124986 / % possible obs: 99.9 % / Redundancy: 21.4 % / CC1/2: 0.999 / Rmerge(I) obs: 0.167 / Rpim(I) all: 0.036 / Rrim(I) all: 0.171 / Net I/σ(I): 12.9
Reflection shellResolution: 1.86→1.9 Å / Redundancy: 11.5 % / Rmerge(I) obs: 1.824 / Mean I/σ(I) obs: 1.4 / Num. unique obs: 5897 / CC1/2: 0.542 / Rpim(I) all: 0.532 / Rrim(I) all: 1.905 / % possible all: 97.7

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
DIALSdata reduction
Aimlessdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6D36

6d36


Resolution: 1.86→97.572 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.954 / SU B: 7.175 / SU ML: 0.089 / Cross valid method: FREE R-VALUE / ESU R: 0.128 / ESU R Free: 0.115
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.1946 6145 4.917 %
Rwork0.1685 118841 -
all0.17 --
obs-124986 99.205 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 29.039 Å2
Baniso -1Baniso -2Baniso -3
1-1.194 Å20 Å20 Å2
2--0.37 Å2-0 Å2
3----1.564 Å2
Refinement stepCycle: LAST / Resolution: 1.86→97.572 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10274 0 377 758 11409
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.01311119
X-RAY DIFFRACTIONr_bond_other_d0.0010.01710363
X-RAY DIFFRACTIONr_angle_refined_deg1.561.64714971
X-RAY DIFFRACTIONr_angle_other_deg1.4641.58423856
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.63951415
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.59922.154571
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.323151804
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.5711575
X-RAY DIFFRACTIONr_chiral_restr0.0860.21416
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0212684
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022514
X-RAY DIFFRACTIONr_nbd_refined0.2260.22581
X-RAY DIFFRACTIONr_symmetry_nbd_other0.180.29288
X-RAY DIFFRACTIONr_nbtor_refined0.1660.25435
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0860.24603
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.170.2644
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.1020.23
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.2680.227
X-RAY DIFFRACTIONr_nbd_other0.2270.294
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.1090.219
X-RAY DIFFRACTIONr_mcbond_it1.6872.3775526
X-RAY DIFFRACTIONr_mcbond_other1.6832.3765525
X-RAY DIFFRACTIONr_mcangle_it2.6623.5286869
X-RAY DIFFRACTIONr_mcangle_other2.6623.5286870
X-RAY DIFFRACTIONr_scbond_it2.2882.7255593
X-RAY DIFFRACTIONr_scbond_other2.2882.7255594
X-RAY DIFFRACTIONr_scangle_it3.6923.9888068
X-RAY DIFFRACTIONr_scangle_other3.6923.9888069
X-RAY DIFFRACTIONr_lrange_it6.05928.7812810
X-RAY DIFFRACTIONr_lrange_other6.05428.77712810
X-RAY DIFFRACTIONr_ncsr_local_group_10.0930.0510625
X-RAY DIFFRACTIONr_ncsr_local_group_20.0890.0510516
X-RAY DIFFRACTIONr_ncsr_local_group_30.0670.0510831
X-RAY DIFFRACTIONr_ncsr_local_group_40.0740.0510893
X-RAY DIFFRACTIONr_ncsr_local_group_50.0910.0510958
X-RAY DIFFRACTIONr_ncsr_local_group_60.0940.0510819
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AAAX-RAY DIFFRACTIONLocal ncs0.093250.05007
12CCCX-RAY DIFFRACTIONLocal ncs0.093250.05007
23AAAX-RAY DIFFRACTIONLocal ncs0.088550.05007
24EEEX-RAY DIFFRACTIONLocal ncs0.088550.05007
35AAAX-RAY DIFFRACTIONLocal ncs0.067060.05008
36GGGX-RAY DIFFRACTIONLocal ncs0.067060.05008
47CCCX-RAY DIFFRACTIONLocal ncs0.073790.05008
48EEEX-RAY DIFFRACTIONLocal ncs0.073790.05008
59CCCX-RAY DIFFRACTIONLocal ncs0.090650.05007
510GGGX-RAY DIFFRACTIONLocal ncs0.090650.05007
611EEEX-RAY DIFFRACTIONLocal ncs0.094340.05007
612GGGX-RAY DIFFRACTIONLocal ncs0.094340.05007
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.86-1.8970.3354510.3177974X-RAY DIFFRACTION91.1796
1.897-1.9490.2944630.2948328X-RAY DIFFRACTION98.2125
1.949-2.0060.274350.2538308X-RAY DIFFRACTION99.9657
2.006-2.0680.264130.2328068X-RAY DIFFRACTION99.9882
2.068-2.1350.2074210.1947837X-RAY DIFFRACTION99.9395
2.135-2.210.1973940.1767591X-RAY DIFFRACTION99.9249
2.21-2.2940.1993670.167314X-RAY DIFFRACTION99.974
2.294-2.3870.193290.1487103X-RAY DIFFRACTION99.9596
2.387-2.4940.1743320.146816X-RAY DIFFRACTION99.986
2.494-2.6150.1563280.1366490X-RAY DIFFRACTION99.9707
2.615-2.7570.1572900.1386208X-RAY DIFFRACTION99.9846
2.757-2.9240.173010.145844X-RAY DIFFRACTION100
2.924-3.1250.1792990.1475524X-RAY DIFFRACTION99.9828
3.125-3.3760.1642690.1495146X-RAY DIFFRACTION100
3.376-3.6980.1862560.1574754X-RAY DIFFRACTION100
3.698-4.1340.1732170.1454330X-RAY DIFFRACTION100
4.134-4.7720.1812000.1393838X-RAY DIFFRACTION100
4.772-5.8430.21740.1793269X-RAY DIFFRACTION100
5.843-8.2530.2091290.1992584X-RAY DIFFRACTION100
8.253-97.5720.19770.1871515X-RAY DIFFRACTION99.8745
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)
10.7166-0.10950.27790.1746-0.05530.68690.0837-0.0854-0.0137-0.06610.0191-0.02450.047-0.0979-0.10280.06910.0122-0.01030.03290.00210.0282-62.749935.83379.3005
20.3315-0.3696-0.8541.00050.24573.06550.09590.03310.04350.0097-0.0631-0.1327-0.3771-0.0554-0.03280.08810.0284-0.02750.03480.00240.0404-57.606646.054419.4255
30.5557-0.21530.07610.2589-0.0110.1847-0.0090.034-0.01180.05360.0163-0.0313-0.0242-0.0195-0.00720.05360.0141-0.01450.0118-0.00350.0316-60.394848.664542.146
40.051-0.0017-0.1960.04690.23921.91520.03390.0518-0.03650.06090.0731-0.0570.3090.0137-0.1070.10340.0599-0.05930.0934-0.0850.114-61.859436.857332.4713
50.1894-0.10950.04840.5494-0.0340.38430.0355-0.00840.0368-0.04890.0131-0.02020.0537-0.0035-0.04850.04540.0187-0.00160.02030.00530.026-26.72042.1448.1425
60.06090.03920.42740.14080.03423.50990.0383-0.03220.01560.09960.06140.1143-0.041-0.3466-0.09970.07210.03480.08540.06490.03930.1065-37.55044.495818.2071
70.22630.02180.04670.6443-0.17020.51140.0024-0.0310.0084-0.03090.08150.01290.0483-0.0613-0.08390.02370.0014-0.0050.03890.02060.0258-39.64473.272341.2169
80.4992-0.43730.15720.4468-0.00090.3450.0412-0.04270.0686-0.0740.0538-0.1141-0.06220.0414-0.09490.0612-0.01250.02370.0768-0.00320.0654-29.44075.399630.8509
Refinement TLS group
IDRefine-IDRefine TLS-IDSelectionAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1ALLAAA18 - 361
2X-RAY DIFFRACTION1ALLAaA401
3X-RAY DIFFRACTION1ALLAbA402
4X-RAY DIFFRACTION1ALLAcA403
5X-RAY DIFFRACTION1ALLAdA404
6X-RAY DIFFRACTION1ALLAeA405
7X-RAY DIFFRACTION1ALLAfA406
8X-RAY DIFFRACTION1ALLAgA407
9X-RAY DIFFRACTION1ALLAhA408
10X-RAY DIFFRACTION1ALLAiA409
11X-RAY DIFFRACTION1ALLAjA410
12X-RAY DIFFRACTION1ALLAkA411
13X-RAY DIFFRACTION1ALLAlA501 - 641
14X-RAY DIFFRACTION2ALLBBB4 - -10000
15X-RAY DIFFRACTION2ALLBaB5 - 11
16X-RAY DIFFRACTION2ALLBbB101
17X-RAY DIFFRACTION2ALLBcB201 - 208
18X-RAY DIFFRACTION3ALLCCC18 - 361
19X-RAY DIFFRACTION3ALLCaC401
20X-RAY DIFFRACTION3ALLCbC402
21X-RAY DIFFRACTION3ALLCcC403
22X-RAY DIFFRACTION3ALLCdC404
23X-RAY DIFFRACTION3ALLCeC405
24X-RAY DIFFRACTION3ALLCfC406
25X-RAY DIFFRACTION3ALLCgC407
26X-RAY DIFFRACTION3ALLChC408
27X-RAY DIFFRACTION3ALLCiC409
28X-RAY DIFFRACTION3ALLCjC410
29X-RAY DIFFRACTION3ALLCkC411
30X-RAY DIFFRACTION3ALLClC412
31X-RAY DIFFRACTION3ALLCmC413
32X-RAY DIFFRACTION3ALLCnC414
33X-RAY DIFFRACTION3ALLCoC415
34X-RAY DIFFRACTION3ALLCpC416
35X-RAY DIFFRACTION3ALLCqC417
36X-RAY DIFFRACTION3ALLCrC501 - 709
37X-RAY DIFFRACTION4ALLDDD4 - -10000
38X-RAY DIFFRACTION4ALLDaD5 - 11
39X-RAY DIFFRACTION4ALLDbD101
40X-RAY DIFFRACTION4ALLDcD201 - 209
41X-RAY DIFFRACTION5ALLEEE18 - 362
42X-RAY DIFFRACTION5ALLEaE401
43X-RAY DIFFRACTION5ALLEbE402
44X-RAY DIFFRACTION5ALLEcE403
45X-RAY DIFFRACTION5ALLEdE404
46X-RAY DIFFRACTION5ALLEeE405
47X-RAY DIFFRACTION5ALLEfE406
48X-RAY DIFFRACTION5ALLEgE407
49X-RAY DIFFRACTION5ALLEhE408
50X-RAY DIFFRACTION5ALLEiE409
51X-RAY DIFFRACTION5ALLEjE410
52X-RAY DIFFRACTION5ALLEkE411
53X-RAY DIFFRACTION5ALLElE412
54X-RAY DIFFRACTION5ALLEmE413
55X-RAY DIFFRACTION5ALLEnE414
56X-RAY DIFFRACTION5ALLEoE415
57X-RAY DIFFRACTION5ALLEpE416
58X-RAY DIFFRACTION5ALLEqE501 - 697
59X-RAY DIFFRACTION6ALLFFF4 - -10000
60X-RAY DIFFRACTION6ALLFaF5 - 10
61X-RAY DIFFRACTION6ALLFbF101
62X-RAY DIFFRACTION6ALLFcF201 - 207
63X-RAY DIFFRACTION7ALLGGG18 - 361
64X-RAY DIFFRACTION7ALLGaG401
65X-RAY DIFFRACTION7ALLGbG402
66X-RAY DIFFRACTION7ALLGcG403
67X-RAY DIFFRACTION7ALLGdG404
68X-RAY DIFFRACTION7ALLGeG405
69X-RAY DIFFRACTION7ALLGfG406
70X-RAY DIFFRACTION7ALLGgG407
71X-RAY DIFFRACTION7ALLGhG408
72X-RAY DIFFRACTION7ALLGiG409
73X-RAY DIFFRACTION7ALLGjG410
74X-RAY DIFFRACTION7ALLGkG411
75X-RAY DIFFRACTION7ALLGlG412
76X-RAY DIFFRACTION7ALLGmG501 - 679
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78X-RAY DIFFRACTION8ALLHaH5 - 10
79X-RAY DIFFRACTION8ALLHbH101
80X-RAY DIFFRACTION8ALLHcH201 - 208

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