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- PDB-3iiq: Crystallographic analysis of bacterial signal peptidase in ternar... -

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Basic information

Entry
Database: PDB / ID: 3iiq
TitleCrystallographic analysis of bacterial signal peptidase in ternary complex with Arylomycin A2 and a beta-sultam inhibitor
Components
  • ARYLOMYCIN A2
  • SIGNAL PEPTIDASE I
KeywordsHYDROLASE/ANTIBIOTIC/INHIBITOR / SER/LYS DYAD / LIPOPEPTIDE / SERINE PROTEASE / BIARYL BRIDGE / MORPHOLINO BETA-SULTAM / ANTIBIOTIC / PEPTIDASE / HYDROLASE-ANTIBIOTIC-INHIBITOR COMPLEX
Function / homology
Function and homology information


signal peptidase I / signal peptide processing / protein processing / peptidase activity / endopeptidase activity / serine-type endopeptidase activity / proteolysis / plasma membrane
Similarity search - Function
Signal Peptidase I; Chain: A, domain 2 / Signal Peptidase I; Chain: A, domain 2 - #10 / Signal peptidase I, all-beta subdomain / Peptidase S26A, signal peptidase I, lysine active site / Signal peptidases I lysine active site. / Peptidase S26A, signal peptidase I / Signal peptidase, peptidase S26 / Peptidase S26A, signal peptidase I, conserved site / Signal peptidases I signature 3. / Peptidase S26A, signal peptidase I, serine active site ...Signal Peptidase I; Chain: A, domain 2 / Signal Peptidase I; Chain: A, domain 2 - #10 / Signal peptidase I, all-beta subdomain / Peptidase S26A, signal peptidase I, lysine active site / Signal peptidases I lysine active site. / Peptidase S26A, signal peptidase I / Signal peptidase, peptidase S26 / Peptidase S26A, signal peptidase I, conserved site / Signal peptidases I signature 3. / Peptidase S26A, signal peptidase I, serine active site / Signal peptidases I serine active site. / Peptidase S26 / Umud Fragment, subunit A / Umud Fragment, subunit A / LexA/Signal peptidase-like superfamily / Beta Complex / Ribbon / Mainly Beta
Similarity search - Domain/homology
ARYLOMYCIN A2 / ACETONITRILE / Chem-JZA / 10-METHYLUNDECANOIC ACID / : / Signal peptidase I
Similarity search - Component
Biological speciesESCHERICHIA COLI (E. coli)
STREPTOMYCES SP. (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsPaetzel, M.
CitationJournal: Biochemistry / Year: 2009
Title: Crystallographic Analysis of Bacterial Signal Peptidase in Ternary Complex with Arylomycin A2 and a Beta-Sultam Inhibitor.
Authors: Luo, C. / Roussel, P. / Dreier, J. / Page, M.G. / Paetzel, M.
History
DepositionAug 3, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 1, 2009Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jul 27, 2011Group: Advisory / Atomic model ...Advisory / Atomic model / Database references / Derived calculations / Non-polymer description / Structure summary
Revision 1.4Dec 12, 2012Group: Other
Revision 2.0Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Polymer sequence / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / entity_poly / pdbx_initial_refinement_model / 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 / _entity_poly.pdbx_seq_one_letter_code_can / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_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: SIGNAL PEPTIDASE I
B: SIGNAL PEPTIDASE I
C: ARYLOMYCIN A2
D: ARYLOMYCIN A2
C: 10-METHYLUNDECANOIC ACID
D: 10-METHYLUNDECANOIC ACID
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,21916
Polymers57,2234
Non-polymers1,99712
Water4,432246
1
B: SIGNAL PEPTIDASE I
D: ARYLOMYCIN A2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,3845
Polymers28,6112
Non-polymers7733
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area950 Å2
ΔGint-4.4 kcal/mol
Surface area11380 Å2
MethodPISA
2
A: SIGNAL PEPTIDASE I
C: ARYLOMYCIN A2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,83511
Polymers28,6112
Non-polymers1,2249
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3000 Å2
ΔGint4.2 kcal/mol
Surface area11150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)70.007, 70.007, 259.894
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

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Protein / Protein/peptide , 2 types, 4 molecules ABCD

#1: Protein SIGNAL PEPTIDASE I / / SPASE I / LEADER PEPTIDASE I


Mass: 27966.658 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 76-323, PERIPLASMIC DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Strain: K-12 / Gene: LEPB / Plasmid: PET / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: P00803, signal peptidase I
#2: Protein/peptide ARYLOMYCIN A2 / /


Type: Lipopeptide / Class: Antibiotic / Mass: 644.674 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Details: ARYLOMYCIN A2 IS A BIARYL-BRIDGED LIPOPEPTIDE. THE SCAFFOLD IS MADE OF TWO PARTS: (1) N-TERM EXOCYCLIC TRIPEPTIDE (2) A TRICYCLIC PEPTIDE, WITH [3,3] BIARYL BOND BETWEEN RESIDUE 4 AND 6 AN ...Details: ARYLOMYCIN A2 IS A BIARYL-BRIDGED LIPOPEPTIDE. THE SCAFFOLD IS MADE OF TWO PARTS: (1) N-TERM EXOCYCLIC TRIPEPTIDE (2) A TRICYCLIC PEPTIDE, WITH [3,3] BIARYL BOND BETWEEN RESIDUE 4 AND 6 AN ISO-C12 FATTY ACID IS LINKED TO RESIDUE 1.
Source: (natural) STREPTOMYCES SP. (bacteria) / References: NOR: NOR01115, ARYLOMYCIN A2

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Non-polymers , 6 types, 258 molecules CD

#3: Chemical ChemComp-JZA / 4-[(1,1-dioxido-1,2-thiazetidin-2-yl)carbonyl]morpholine / beta-sultam


Mass: 220.246 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C7H12N2O4S
#4: Chemical ChemComp-TRT / FRAGMENT OF TRITON X-100 / 1-{2-[2-(2-METHOXYETHOXY)ETHOXY]ETHOXY}-4-(1,1,3,3-TETRAMETHYLBUTYL)BENZENE / Triton X-100


Mass: 352.508 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H36O4 / Comment: detergent*YM
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-CCN / ACETONITRILE / Acetonitrile


Mass: 41.052 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3N
#7: Chemical
ChemComp-M12 / 10-METHYLUNDECANOIC ACID /


Type: Lipopeptide / Class: Antibiotic / Mass: 200.318 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C12H24O2
Details: ARYLOMYCIN A2 IS A BIARYL-BRIDGED LIPOPEPTIDE. THE SCAFFOLD IS MADE OF TWO PARTS: (1) N-TERM EXOCYCLIC TRIPEPTIDE (2) A TRICYCLIC PEPTIDE, WITH [3,3] BIARYL BOND BETWEEN RESIDUE 4 AND 6 AN ...Details: ARYLOMYCIN A2 IS A BIARYL-BRIDGED LIPOPEPTIDE. THE SCAFFOLD IS MADE OF TWO PARTS: (1) N-TERM EXOCYCLIC TRIPEPTIDE (2) A TRICYCLIC PEPTIDE, WITH [3,3] BIARYL BOND BETWEEN RESIDUE 4 AND 6 AN ISO-C12 FATTY ACID IS LINKED TO RESIDUE 1.
References: ARYLOMYCIN A2
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 246 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsARYLOMYCIN A2 IS A CYCLIC LIPOHEXAPEPTIDE, A MEMBER OF THE ARYLOMYCIN FAMILY. ALL MEMBERS HAVE A ...ARYLOMYCIN A2 IS A CYCLIC LIPOHEXAPEPTIDE, A MEMBER OF THE ARYLOMYCIN FAMILY. ALL MEMBERS HAVE A FATTY ACID AT THE N-TERM AND A CORE STRUCTURE OF TRIPEPTIDE MACROCYCLE FORMED BY A C-C BIARYL LINKAGE BETWEEN RESIDUES 4 AND 6. HERE, ARYLOMYCIN A2 IS REPRESENTED BY GROUPING TOGETHER THE SEQUENCE (SEQRES) AND ONE LIGAND (HET) M12.
Nonpolymer detailsLIGAND JZA, MORPHOLINO-BETA-SULTAM, IS A BETA-LACTAMSE TYPE INHIBITOR.

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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: 2.84 Å3/Da / Density % sol: 56.61 %
Crystal growpH: 6.5
Details: 0.2M NH4 FORMATE, 25% PEG 2000, 0.1M NA CACODYLATE PH 6.5, AND 5% TERTIARY-AMYL ALCOHOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 1.1217
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 1, 2007 / Details: MIRRORS
RadiationMonochromator: MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1217 Å / Relative weight: 1
ReflectionResolution: 2→67.4 Å / Num. obs: 40272 / % possible obs: 95.2 % / Observed criterion σ(I): 2 / Redundancy: 7.1 % / Biso Wilson estimate: 14 Å2 / Rmerge(I) obs: 0.068 / Rsym value: 0.069 / Net I/σ(I): 10.4
Reflection shellResolution: 2→2.14 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.43 / Mean I/σ(I) obs: 5.1 / Rsym value: 0.052 / % possible all: 95.1

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Processing

Software
NameVersionClassification
AMoREphasing
REFMAC5.2.0005refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1T7D CHAIN A WITH LIGANDS REMOVED

1t7d


Resolution: 2→67.4 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.931 / SU B: 9.239 / SU ML: 0.145 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.183 / ESU R Free: 0.169 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25 2035 5.1 %RANDOM
Rwork0.207 ---
obs0.21 38237 95.1 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 40.59 Å2
Baniso -1Baniso -2Baniso -3
1-1.17 Å20 Å20 Å2
2--1.17 Å20 Å2
3----2.34 Å2
Refinement stepCycle: LAST / Resolution: 2→67.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3573 0 114 246 3933
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.030.0223770
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.3482.0145115
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg9.3835431
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.36524165
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.88215577
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.2291522
X-RAY DIFFRACTIONr_chiral_restr0.3210.2534
X-RAY DIFFRACTIONr_gen_planes_refined0.0110.022873
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2470.21663
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3250.22426
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1940.2244
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2620.258
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1980.215
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.8241.52255
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.33423542
X-RAY DIFFRACTIONr_scbond_it3.30131762
X-RAY DIFFRACTIONr_scangle_it4.3684.51569
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2→2.09 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.302 113 -
Rwork0.266 1741 -
obs--60.77 %
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)
131.0406-11.79487.646743.0687-5.66594.43930.6596-1.67251.18411.4435-1.6351-4.6309-1.4652-0.46940.97550.0838-0.136-0.23540.0988-0.04750.19737.484421.964-7.4643
21.09610.48280.0073.00680.8291.78140.02660.1207-0.12520.3484-0.0244-0.18450.1058-0.0562-0.0023-0.0199-0.0086-0.01210.2388-0.01330.0158-3.412211.8379-14.8828
321.8851-10.181111.20811.7696-11.075613.846-0.416-0.38221.18450.68250.3913-0.9353-0.7251-0.12920.02470.06150.01490.03370.14930.01820.0157-0.385929.0444-12.9678
41.4260.5352-0.30023.1456-1.95295.28650.10380.23020.12620.37860.0840.1687-0.1424-0.4678-0.18780.03350.01390.01390.22230.01830.0083-9.874522.1636-10.4581
51.12842.5643-0.06338.72371.98511.5686-0.05710.39520.2438-0.09790.17320.3956-0.1625-0.4738-0.1161-0.10930.0573-0.01690.39080.15590.0661-20.129927.7514-24.1147
61.40071.21151.07489.1683-0.54431.0923-0.26580.48970.17120.12820.45680.4585-0.0401-0.3118-0.191-0.0699-0.0010.06250.50840.02920.0424-15.49119.7669-27.4731
72.1901-0.7792-3.117117.43691.48485.6903-0.02790.1228-0.21190.20220.6382-0.45260.83770.1793-0.6103-0.1869-0.1133-0.07730.35-0.150.0758-11.44771.2802-24.7457
82.3891-0.7479-0.05544.9963-0.16153.3899-0.2774-0.1153-0.3495-0.21960.1536-0.29020.47330.17180.1237-0.0863-0.08380.00350.4865-0.0567-0.012-17.0548-0.703-28.0131
94.39632.1315-0.74562.757-0.10180.16560.00290.52320.0085-0.26340.06370.2473-0.0333-0.0881-0.0666-0.0686-0.047-0.02830.44880.0237-0.0181-14.086217.563-27.5193
1028.4464-1.457-2.803612.8139-4.049144.8897-0.31180.0785-1.56370.3377-0.7880.14290.7579-1.23991.0998-0.10490.05860.15260.50580.01670.322-28.724619.3224-15.6738
115.70934.8882.971727.5398-6.29624.8930.3315-0.31880.34750.39850.27381.7815-0.593-0.9548-0.6053-0.01530.19090.21170.36160.11880.118-26.824330.7231-12.1948
1248.31542.370122.321242.984927.659421.527-0.96470.64532.33780.13450.21582.3335-1.5175-1.87920.74880.00890.0990.10290.66550.37160.2458-26.569228.6704-18.2243
131.3780.2393-0.7381.46820.38570.71520.03610.25680.20340.32750.06620.2242-0.1492-0.2541-0.1023-0.01790.04960.03310.30930.0685-0.0041-16.655323.7842-14.8124
142.9014-2.6197-1.99116.16782.22144.09140.06160.2497-0.08420.2198-0.0036-0.13260.0268-0.0795-0.0580.0357-0.0364-0.0580.27180.0210.0778-1.405217.2662-12.645
15135.6967-42.4202-40.177640.63559.997712.1357-1.4872-3.7451-0.40290.72731.8581-1.64511.2374-0.0847-0.37090.3839-0.34670.11480.3291-0.13790.2451-5.3397-1.1229-11.8291
164.295-1.4959-1.52736.2051-1.26274.1240.0230.5144-0.303-0.0109-0.2066-0.25910.12520.10930.1836-0.0745-0.0098-0.00740.3129-0.03520.06662.99329.4707-21.7008
173.9601-0.0094-1.45282.55990.94024.354-0.0741-0.09380.1639-0.29850.0032-0.20030.06470.25710.07090.02160.01-0.02530.1980.0180.047515.252435.9121-48.8929
1814.087117.1875-6.726225.2374-0.974615.4679-0.75840.108-0.5933-1.44010.6841-0.96172.01320.39830.0743-0.03650.2528-0.05610.21710.05030.017120.653420.8459-51.1883
192.0989-0.4507-0.67432.5916-1.36386.9447-0.078-0.0834-0.0456-0.13040.05480.140.344-0.15250.02320.0842-0.00840.01780.17380.0240.012810.062826.4056-53.8963
208.3269-3.8757-5.88242.54794.29457.4125-0.2212-0.3479-0.4972-0.0992-0.01430.12080.6643-0.31270.23540.0591-0.05270.05030.17230.1055-0.01331.427416.9824-41.7493
2145.7228-28.326-31.686344.508117.148425.19910.04220.0601-2.4986-1.1833-1.17921.11591.8554-0.86341.1370.32880.0670.03810.41470.27090.06846.36829.333-42.0772
224.4116-4.93222.60468.39451.1427.24390.7253-0.2355-1.05760.687-1.43850.04043.3708-1.79840.71320.557-0.11490.29960.1904-0.0130.04296.98337.9548-39.7575
232.1887-2.3979-0.35696.9636-0.84271.96880.14030.07180.2198-0.30.00530.0747-0.1563-0.1562-0.1455-0.0660.0005-0.02040.3608-0.0250.0461-0.017839.3835-38.2956
247.3974-6.97660.76899.5408-1.53941.2729-0.3891-0.570.51250.62620.332-0.3268-0.2475-0.35560.0571-0.03460.0581-0.03180.4464-0.06990.029-0.852540.7269-31.852
254.8775-0.98131.04114.7724-1.79612.7199-0.0461-0.3129-0.0693-0.09550.001-0.38470.32390.33650.04510.00820.0586-0.00550.38980.0253-0.05757.704625.6625-35.8282
262.8502-3.1422-3.067113.6319.94869.40010.22220.2073-0.4942-0.5014-0.48220.40580.5103-1.36750.260.0743-0.0918-0.03790.25430.0065-0.0178-6.530819.8563-48.9172
2740.9657-19.9292-12.792510.32576.015638.24680.0870.1876-2.4193-0.3763-0.21471.39991.042-1.70430.12770.2084-0.1351-0.05350.21440.12830.1448-3.84913.5797-47.4077
281.5435-1.4029-0.48372.70112.02473.1772-0.1566-0.1699-0.2614-0.1490.13830.10730.5338-0.03120.01830.0898-0.03670.03360.18210.0714-0.00485.701520.8634-48.2507
292.38030.63550.47210.6990.51222.5658-0.0459-0.0851-0.0187-0.06040.0419-0.08610.27050.05970.00410.14230.00860.00020.22630.04490.047611.11926.4627-51.7443
3047.1171-16.909216.377114.3838-9.12528.358-0.3959-0.27590.2357-0.51550.32760.9841-1.2567-2.28990.0682-0.09990.076-0.09720.1201-0.02350.02179.802246.2807-47.1978
3110.4247-4.74545.046835.0323-15.716916.348-0.30160.38381.1737-1.26620.80832.5315-2.1038-1.4189-0.50670.14750.1742-0.20560.155-0.0290.087713.487149.2604-45.0337
3219.95663.39274.00797.84658.44779.10170.4069-1.1662-0.86460.4063-0.0721-0.20620.6501-0.4539-0.3348-0.0285-0.0088-0.05110.35720.07870.102319.369636.6726-39.9678
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A79 - 82
2X-RAY DIFFRACTION2A83 - 103
3X-RAY DIFFRACTION3A104 - 126
4X-RAY DIFFRACTION4A127 - 150
5X-RAY DIFFRACTION5A151 - 168
6X-RAY DIFFRACTION6A169 - 197
7X-RAY DIFFRACTION7A206 - 213
8X-RAY DIFFRACTION8A214 - 224
9X-RAY DIFFRACTION9A225 - 245
10X-RAY DIFFRACTION10A246 - 250
11X-RAY DIFFRACTION11A251 - 256
12X-RAY DIFFRACTION12A257 - 261
13X-RAY DIFFRACTION13A262 - 286
14X-RAY DIFFRACTION14A287 - 305
15X-RAY DIFFRACTION15A306 - 312
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