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- PDB-2bev: Reactivity modulation of human branched-chain alpha-ketoacid dehy... -

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Basic information

Entry
Database: PDB / ID: 2bev
TitleReactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch
Components
  • (2-OXOISOVALERATE DEHYDROGENASE ...) x 2
  • PEPTIDE ALA-TYR-ARG
KeywordsOXIDOREDUCTASE / OXIDATIVE DECARBOXYLATION / MAPLE SYRUP URINE DISEASE / THIAMINE DIPHOSPHATE / PHOSPHORYLATION / CONFORMATIONAL SWITCH
Function / homology
Function and homology information


: / 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) / 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity / branched-chain amino acid catabolic process / Branched-chain amino acid catabolism / Glyoxylate metabolism and glycine degradation / carboxy-lyase activity / response to glucocorticoid / response to cAMP / response to nutrient ...: / 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) / 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity / branched-chain amino acid catabolic process / Branched-chain amino acid catabolism / Glyoxylate metabolism and glycine degradation / carboxy-lyase activity / response to glucocorticoid / response to cAMP / response to nutrient / lipid metabolic process / mitochondrial matrix / protein-containing complex binding / nucleolus / mitochondrion / nucleoplasm / metal ion binding
Similarity search - Function
Dehydrogenase, E1 component / Dehydrogenase E1 component / Transketolase, C-terminal domain / Transketolase, C-terminal domain / Rossmann fold - #920 / Transketolase-like, pyrimidine-binding domain / Transketolase, pyrimidine binding domain / Transketolase, pyrimidine binding domain / Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II / Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains ...Dehydrogenase, E1 component / Dehydrogenase E1 component / Transketolase, C-terminal domain / Transketolase, C-terminal domain / Rossmann fold - #920 / Transketolase-like, pyrimidine-binding domain / Transketolase, pyrimidine binding domain / Transketolase, pyrimidine binding domain / Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II / Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains / Thiamin diphosphate-binding fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
: / : / C2-1-HYDROXY-2-METHYL-BUTYL-THIAMIN DIPHOSPHATE / 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial / 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
SYNTHETIC CONSTRUCT (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.8 Å
AuthorsMachius, M. / Wynn, R.M. / Chuang, J.L. / Tomchick, D.R. / Brautigam, C.A. / Chuang, D.T.
Citation
Journal: Structure / Year: 2006
Title: A Versatile Conformational Switch Regulates Reactivity in Human Branched-Chain Alpha-Ketoacid Dehydrogenase.
Authors: Machius, M. / Wynn, R.M. / Chuang, J.L. / Li, J. / Kluger, R. / Yu, D. / Tomchick, D.R. / Brautigam, C.A. / Chuang, D.T.
#1: Journal: J.Biol.Chem. / Year: 2004
Title: Crosstalk between Cofactor Binding and the Phosphorylation Loop Conformation in the Bckd Machine
Authors: Li, J. / Wynn, R.M. / Machius, M. / Chuang, J.L. / Karthikeyan, S. / Tomchick, D.R. / Chuang, D.T.
#2: Journal: J.Biol.Chem. / Year: 2003
Title: Roles of His291-Alpha and His146-Beta in the Reductive Acylation Reaction Catalyzed by Human Branched-Chain Alpha-Ketoacid Dehydrogenase: Refined Phosphorylation Loop Structure in the Active Site
Authors: Wynn, R. / Machius, M. / Chuang, J. / Li, J. / Tomchick, D. / Chuang, D.
#3: Journal: J.Biol.Chem. / Year: 2001
Title: Roles of Active Site and Novel Potassium Ion- Binding Site Residues in Human Mitochondrial Branched-Chain Alpha-Ketoacid Decarboxylase- Dehydrogenase
Authors: Wynn, R.M. / Ho, R. / Chuang, J.L. / Chuang, D.T.
History
DepositionNov 30, 2004Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 16, 2006Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Dec 21, 2016Group: Data collection / Source and taxonomy
Revision 1.3May 15, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval
Revision 1.4Sep 25, 2019Group: Data collection / Experimental preparation / Other / Category: exptl_crystal_grow / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.status_code_sf
Revision 1.5Dec 13, 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_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_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.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.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_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: 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT
B: 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT
C: PEPTIDE ALA-TYR-ARG
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,78111
Polymers83,8833
Non-polymers8998
Water12,484693
1
A: 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT
B: 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT
C: PEPTIDE ALA-TYR-ARG
hetero molecules

A: 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT
B: 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT
C: PEPTIDE ALA-TYR-ARG
hetero molecules


Theoretical massNumber of molelcules
Total (without water)169,56322
Polymers167,7666
Non-polymers1,79716
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation5_555x-y,-y,-z+2/31
Buried area31140 Å2
ΔGint-211.3 kcal/mol
Surface area43000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)144.473, 144.473, 69.480
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121
Components on special symmetry positions
IDModelComponents
11B-2119-

HOH

21B-2122-

HOH

DetailsTHIS PROTEIN IS A ALPHA-BETA TETRAMER, BUT INTHE PRESENT ENTRY, THEY ARE IN COMPLEX WITH A PEPTIDECHAIN C, THEREBY MAKING THE WHOLE ASSEMBLY A HEXAMERCHAIN C IS A FRAGMENT OF CHAIN B. IT IS NOT CLEAR WHETHERTHIS FRAGMENT IS AN ALTERNATIVE CONFORMATION OF THE CORRESPONDINGRESIDUES IN CHAIN B OF THE SAME MOLECULE OR OF A NEIGHBORING,SYMMETRY-RELATED MOLECULE. IT COULD ALSO COME FROM PROTEOLYSIS,BUT THE AUTHORS DO NOT HAVE ANY EVIDENCE FOR THAT.

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Components

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2-OXOISOVALERATE DEHYDROGENASE ... , 2 types, 2 molecules AB

#1: Protein 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT / BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE E1 COMPONENT ALPHA CHAIN / BCKDH E1-ALPHA / BCKDE1A


Mass: 45571.098 Da / Num. of mol.: 1 / Fragment: RESIDUES 46-445
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PTRC-ALPHA-BETAHIS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21
References: UniProt: P12694, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)
#2: Protein 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT / BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE E1 COMPONENT BETA CHAIN / BCKDH E1-BETA


Mass: 37902.270 Da / Num. of mol.: 1 / Fragment: RESIDUES 51-392
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PTRC-ALPHA-BETAHIS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21
References: UniProt: P21953, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)

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Protein/peptide , 1 types, 1 molecules C

#3: Protein/peptide PEPTIDE ALA-TYR-ARG


Mass: 409.461 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others)

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Non-polymers , 6 types, 701 molecules

#4: Chemical ChemComp-THY / C2-1-HYDROXY-2-METHYL-BUTYL-THIAMIN DIPHOSPHATE


Mass: 510.439 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C17H28N4O8P2S
#5: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: K
#6: Chemical ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mn
#7: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#8: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 693 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsCATALYTIC ACTIVITY: 3-METHYL-2-OXOBUTANOATE + [DIHYDROLIPOYLLYSINE-RESIDUE (2-METHYLPROPANOYL) ...CATALYTIC ACTIVITY: 3-METHYL-2-OXOBUTANOATE + [DIHYDROLIPOYLLYSINE-RESIDUE (2-METHYLPROPANOYL)TRANSFERASE] LIPOYLLYSINE = [DIHYDROLIPOYLLYSINE-RESIDUE (2- METHYLPROPANOYL)TRANSFERASE] S-(2- METHYLPROPANOYL)DIHYDROLIPOYLLYSINE + CO(2).
Sequence detailsCHAIN C IS A FRAGMENT OF CHAIN B. IT IS NOT CLEAR WHETHER THIS FRAGMENT IS AN ALTERNATIVE ...CHAIN C IS A FRAGMENT OF CHAIN B. IT IS NOT CLEAR WHETHER THIS FRAGMENT IS AN ALTERNATIVE CONFORMATION OF THE CORRESPONDING RESIDUES IN CHAIN B OF THE SAME MOLECULE OR OF A NEIGHBORING, SYMMETRY-RELATED MOLECULE. IT COULD ALSO COME FROM PROTEOLYSIS,BUT THE AUTHORS DO NOT HAVE ANY EVIDENCE FOR THAT.

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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: 2.5 Å3/Da / Density % sol: 53.4 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 5.5
Details: CRYSTALS WERE GROWN AT 20C VIA THE VAPOR DIFFUSION METHOD BY MIXING EQUAL AMOUNTS OF PROTEIN (20-25 MG/ML IN 50 MM HEPES/NAOH, PH 7.5, 250 MM KCL, 0.5 MM PMSF, 1 MM BENZAMIDINE AND 5% (V/V) ...Details: CRYSTALS WERE GROWN AT 20C VIA THE VAPOR DIFFUSION METHOD BY MIXING EQUAL AMOUNTS OF PROTEIN (20-25 MG/ML IN 50 MM HEPES/NAOH, PH 7.5, 250 MM KCL, 0.5 MM PMSF, 1 MM BENZAMIDINE AND 5% (V/V) GLYCEROL) WITH WELL SOLUTION (1.4- 1.6 M AMMONIUM SULFATE, 0.1 M NA-CITRATE PH 5.8, 20 MM B-MERCAPTOETHANOL). SERIALLY DILUTED CRUSHED CRYSTALS WERE USED FOR MICRO-SEEDING ONE DAY AFTER THE DROPS WERE SET UP. CRYSTALS APPEARED ONE DAY AFTER SEEDING AND GREW TO A MAXIMUM SIZE OF 120 X 800 UM WITHIN 10 DAYS. CRYSTALS WERE STABILIZED FOR 12 HOURS BY TRANSFER TO FRESH WELL SOLUTION. THEY WERE THEN CRYO-PROTECTED BY STEP-WISE TRANSFER INTO CRYO-BUFFER CONTAINING 1.6 M AMMONIUM SULFATE, 50 MM HEPES, PH 7.5, 100 MM NA-CITRATE, PH 5.8, 100 MM KCL, 50 MM DTT AND UP TO 20% (V/V) GLYCEROL. IT WAS FOUND THAT MANGANESE IONS COULD REPLACE THE MAGNESIUM REQUIRED FOR THE BINDING OF THDP TO THE ENZYME.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 1.00691
DetectorType: CUSTOM / Detector: CCD / Date: Jun 25, 2003
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00691 Å / Relative weight: 1
ReflectionResolution: 1.8→32.05 Å / Num. obs: 77268 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 6 % / Biso Wilson estimate: 15.2 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 21.7
Reflection shellResolution: 1.8→1.83 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.67 / Mean I/σ(I) obs: 3 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.2.0003refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: PDB ENTRY 1OLS

1ols


Resolution: 1.8→30 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.954 / SU B: 3.616 / SU ML: 0.059 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.092 / ESU R Free: 0.091 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DISORDERED REGIONS WERE MODELED STEREOCHEMICALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.17 1441 1.9 %RANDOM
Rwork0.138 ---
obs0.139 75773 100 %-
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: 13.26 Å2
Baniso -1Baniso -2Baniso -3
1-0.75 Å20.37 Å20 Å2
2--0.75 Å20 Å2
3----1.12 Å2
Refinement stepCycle: LAST / Resolution: 1.8→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5783 0 49 693 6525
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.0226155
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.6671.948371
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9245764
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.72923.615296
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.85151005
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.1891543
X-RAY DIFFRACTIONr_chiral_restr0.1320.2876
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.024840
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2220.23258
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3130.24352
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1530.2614
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1860.2228
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1740.270
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9261.53751
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.58826076
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.98232444
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.6894.52295
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
LS refinement shellResolution: 1.8→1.85 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.238 84
Rwork0.181 5534
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)
10.99680.4309-0.21440.6052-0.77881.1698-0.0017-0.06930.0147-0.0190.08080.2732-0.0445-0.1744-0.0791-0.04130.00040.03190.00020.0580.067948.4706-5.999632.1317
20.503-0.0559-0.04770.3342-0.19260.59750.0210.09920.0177-0.03570.02160.0563-0.0651-0.0942-0.0426-0.00890.0265-0.01-0.04030.0064-0.018864.926515.51645.1356
31.0344-0.4999-0.02640.8568-0.13080.03420.03420.10720.1494-0.0396-0.0839-0.1163-0.15230.20540.0497-0.0047-0.05070.01180.01230.03060.0059101.303818.52096.8061
40.3303-0.74331.240375.24819.652911.5030.0814-0.05310.3110.7988-0.1702-0.9157-0.25230.0240.08880.00220.01030.00430.00620.01690.0044100.21464.016150.876
50.2585-0.01070.04250.2247-0.1250.53770.023-0.02910.04870.0658-0.0265-0.0147-0.11520.06160.00350.0242-0.0194-0.0016-0.0506-0.0103-0.013884.274212.51534.9295
60.43020.0613-0.04330.5873-0.10190.65240.0108-0.0561-0.01880.0937-0.0553-0.1538-0.05850.24070.0445-0.0566-0.0336-0.03610.03220.0177-0.0142106.65663.808437.5452
73.32646.8228-1.69414.0503-2.480118.53590.12581.6654-0.0389-0.1988-0.273-0.0674-0.3185-1.50450.1472-0.001-0.0009-0.00230.0004-0.0006-0.000179.9926-2.7908-2.3075
812.2055-5.29211.4663.7445-3.70216.6612-0.0112-0.04230.5936-0.326-0.1583-0.1471-0.076-0.08530.16950.05990.0236-0.0185-0.0529-0.01410.02974.18313.21147.6018
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A6 - 30
2X-RAY DIFFRACTION2A31 - 355
3X-RAY DIFFRACTION3A356 - 400
4X-RAY DIFFRACTION4B1002 - 1008
5X-RAY DIFFRACTION5B1014 - 1191
6X-RAY DIFFRACTION6B1192 - 1342
7X-RAY DIFFRACTION7C2299 - 2301
8X-RAY DIFFRACTION8A601

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