PDB-2c2b: Crystallographic structure of Arabidopsis thaliana Threonine synt...

ID or keywords:

Entry

Database: PDB / ID: 2c2b

Title

Crystallographic structure of Arabidopsis thaliana Threonine synthase complexed with pyridoxal phosphate and S-adenosylmethionine

Components

THREONINE SYNTHASE 1, CHLOROPLASTIC

Keywords

LYASE / THREONINE SYNTHESIS /

ALLOSTERY /

SYNTHASE

Function / homology

Function and homology information

threonine synthase /

threonine synthase activity / threonine biosynthetic process /

chloroplast stroma /

chloroplast /

pyridoxal phosphate binding /

plasma membrane
Similarity search - Function

Biological species

ARABIDOPSIS THALIANA (thale cress)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.6 Å

Authors

Mas-Droux, C. / Biou, V. / Dumas, R.

Citation

Journal: J.Biol.Chem. / Year: 2006
Title: Allosteric Threonine Synthase: Reorganization of the Pyridoxal Phosphate Site Upon Asymmetric Activation Through S-Adenosylmethionine Binding to a Novel Site.
Authors: Mas-Droux, C. / Biou, V. / Dumas, R.

History

Deposition	Sep 27, 2005	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Nov 28, 2005	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Refinement description / Version format compliance
Revision 1.2	Nov 11, 2015	Group: Atomic model / Derived calculations ...Atomic model / Derived calculations / Non-polymer description / Other / Refinement description / Structure summary
Revision 1.3	Dec 13, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_conn / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_conn.pdbx_leaving_atom_flag / _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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/c2/2c2b ftp://data.pdbj.org/pub/pdb/validation_reports/c2/2c2b	HTTPS FTP

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Related structure data

Related structure data	2c2gC 1e5xS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	6bpm-1 6bpm-2 2y8n-3 4lng-d 5hia-d 6dgi-d 1nba-d 4r1z-d 6bpo-1 1itw-2 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

Related structure data

2c2gC

1e5xS

S: Starting model for refinement

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#228 - Dec 2018 Directed Evolution of Enzymes similarity (3) #139 - Jul 2011 DNA Methyltransferase similarity (1)

Deposited unit

A: THREONINE SYNTHASE 1, CHLOROPLASTIC

B: THREONINE SYNTHASE 1, CHLOROPLASTIC

C: THREONINE SYNTHASE 1, CHLOROPLASTIC

D: THREONINE SYNTHASE 1, CHLOROPLASTIC

E: THREONINE SYNTHASE 1, CHLOROPLASTIC

F: THREONINE SYNTHASE 1, CHLOROPLASTIC

hetero molecules

327 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: THREONINE SYNTHASE 1, CHLOROPLASTIC

B: THREONINE SYNTHASE 1, CHLOROPLASTIC

hetero molecules

defined by author&software
109 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: THREONINE SYNTHASE 1, CHLOROPLASTIC

D: THREONINE SYNTHASE 1, CHLOROPLASTIC

hetero molecules

defined by author&software
109 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

E: THREONINE SYNTHASE 1, CHLOROPLASTIC

F: THREONINE SYNTHASE 1, CHLOROPLASTIC

hetero molecules

defined by author&software
109 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	191.920, 110.846, 152.779
Angle α, β, γ (deg.)	90.00, 89.98, 90.00
Int Tables number	5
Space group name H-M	C121

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	C
3	1	F
1	2	B
2	2	D
3	2	E
1	3	A
2	3	C
3	3	F

NCS domain segments:

Component-ID: 1

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	SER	SER	ALA	ALA	5	A	A	40 - 470	40 - 470
2	1	SER	SER	ALA	ALA	5	C	C	40 - 470	40 - 470
3	1	SER	SER	ALA	ALA	5	F	F	40 - 470	40 - 470
1	2	SER	SER	ALA	ALA	5	B	B	40 - 470	40 - 470
2	2	SER	SER	ALA	ALA	5	D	D	40 - 470	40 - 470
3	2	SER	SER	ALA	ALA	5	E	E	40 - 470	40 - 470
1	3	TRS	TRS	TRS	TRS	4	A	I	800
2	3	TRS	TRS	TRS	TRS	4	C	P	800
3	3	TRS	TRS	TRS	TRS	4	F	Z	800

NCS ensembles :

ID
1
2
3

NCS oper:

ID	Code	Matrix	Vector
1	given	(-0.49938, 0.86639, 0.00017), (-0.86639, -0.49938, -0.00063), (-0.00047, -0.00046, 1)	32.06766, 55.19161, -50.8735
2	given	(0.50075, 0.86559, 0.00023), (0.86559, -0.50075, 0.00035), (0.00042, 2.0E-5, -1)	32.0809, -55.6683, 101.83951
3	given	(-0.4998, 0.86614, 6.0E-5), (-0.86614, -0.4998, 0.00068), (0.00062, 0.00029, 1)	32.11317, 55.10795, -50.94014
4	given	(0.5005, 0.86574, -0.00043), (0.86574, -0.5005, -0.00037), (-0.00054, -0.00019, -1)	32.15505, -55.63955, 101.86627

Details

THE BIOLOGICAL UNIT OF ARABIDOPSIS THALIANA THREONINESYNTHASE (HOMODIMER) IN COMPLEX WITH SAM IS FORMED BY TWOASYMETRIC MONOMERS. IN ONE MONOMER THE ACTIVE SITECORRESPONDS TO AN INACTIVE FORM WHEREAS IN THE OTHERMONOMER, THE ACTIVE SITE CORRESPONDS TO AN ACTIVE FORM WITHA STANDARD PLP ORIENTATION FOR A TYPE II FAMILY PLPENZYMES.

#1: Protein	THREONINE SYNTHASE 1, CHLOROPLASTIC / / THREONINE SYNTHASE / TS / PROTEIN METHIONINE OVER-ACCUMULATOR 2 Mass: 53385.590 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ARABIDOPSIS THALIANA (thale cress) / Plasmid: PET23D / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q9S7B5, threonine synthase
#2: Chemical	ChemComp-SAM / S-ADENOSYLMETHIONINE / S-Adenosyl methionine Mass: 398.437 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C₁₅H₂₂N₆O₅S
#3: Chemical	ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER / Tris Mass: 122.143 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₄H₁₂NO₃ / Comment: pH buffer*YM
#4: Chemical	ChemComp-PLP / PYRIDOXAL-5'-PHOSPHATE / VITAMIN B6 Phosphate / Pyridoxal phosphate Mass: 247.142 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₈H₁₀NO₆P
#5: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 313 / Source method: isolated from a natural source / Formula: H₂O
Sequence details	THIS SEQUENCE CORRESPONDS TO THE MATURE SEQUENCE WITHOUT THE TRANSIT PEPTIDE

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 5.3 Å³/Da / Density % sol: 76.4 %
Crystal grow	pH: 6.5 Details: 10 MM CACL2, 15% (W/V) PEG 2000 MONOMETHYL ETHER, 1 MM PLP, 5MM SAM, 100 MM BISTRIS PH 6.5 BUFFER

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934
Detector	Type: ADSC CCD / Detector: CCD / Date: Nov 30, 2004 / Details: MIRRORS
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.934 Å / Relative weight: 1
Reflection	Resolution: 2.6→30 Å / Num. obs: 93317 / % possible obs: 99.8 % / Redundancy: 3.7 % / R_merge(I) obs: 0.08 / Net I/σ(I): 11.7
Reflection shell	Resolution: 2.6→2.74 Å / Redundancy: 3.7 % / R_merge(I) obs: 0.44 / Mean I/σ(I) obs: 2.8 / % possible all: 99.9

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0005	refinement
MOSFLM		data reduction
SCALA		data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1E5X

1e5x

Resolution: 2.6→29.89 Å / Cor.coef. F_o:F_c: 0.945 / Cor.coef. F_o:F_c free: 0.922 / SU B: 25.549 / SU ML: 0.272 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.812 / ESU R Free: 0.311 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-35 AND 480-486 ARE DISORDERED IN MONOMERS A, C AND F RESIDUS 1-34, 344-362 AND 482-486 ARE DISORDERED IN MONOMERS B, D AND E.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.248	4904	5 %	RANDOM
R_work	0.206	-	-	-
obs	0.208	93254	100 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 60.9 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.72 Å²	0 Å²	-0.26 Å²
2-	-	-0.12 Å²	0 Å²
3-	-	-	-0.6 Å²

Refinement step

Cycle: LAST / Resolution: 2.6→29.89 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	20207	0	438	313	20958

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.006	0.022	21143
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	0.961	1.976	28733
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	4.405	5	2608
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.564	24.224	883
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.487	15	3403
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	16.294	15	102
X-RAY DIFFRACTION	r_chiral_restr	0.06	0.2	3160
X-RAY DIFFRACTION	r_gen_planes_refined	0.002	0.02	15932
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.174	0.2	10204
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.297	0.2	14637
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.112	0.2	719
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.135	0.2	118
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.175	0.2	15
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	0.733	2	13378
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	1.296	3	21002
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	1.832	4	9015
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	2.797	6	7731
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	1724	medium positional	0.09	0.5
1	2	C	1724	medium positional	0.07	0.5
1	3	F	1724	medium positional	0.07	0.5
2	1	B	1648	medium positional	0.07	0.5
2	2	D	1648	medium positional	0.08	0.5
2	3	E	1648	medium positional	0.07	0.5
3	1	A	8	medium positional	0.48	0.5
3	2	C	8	medium positional	0.44	0.5
3	3	F	8	medium positional	0.56	0.5
1	1	A	1612	loose positional	0.31	5
1	2	C	1612	loose positional	0.3	5
1	3	F	1612	loose positional	0.35	5
2	1	B	1550	loose positional	0.26	5
2	2	D	1550	loose positional	0.24	5
2	3	E	1550	loose positional	0.24	5
1	1	A	1724	medium thermal	0.14	2
1	2	C	1724	medium thermal	0.15	2
1	3	F	1724	medium thermal	0.15	2
2	1	B	1648	medium thermal	0.14	2
2	2	D	1648	medium thermal	0.14	2
2	3	E	1648	medium thermal	0.14	2
3	1	A	8	medium thermal	0.06	2
3	2	C	8	medium thermal	0.09	2
3	3	F	8	medium thermal	0.13	2
1	1	A	1612	loose thermal	0.81	10
1	2	C	1612	loose thermal	0.9	10
1	3	F	1612	loose thermal	0.85	10
2	1	B	1550	loose thermal	0.86	10
2	2	D	1550	loose thermal	0.85	10
2	3	E	1550	loose thermal	0.85	10

LS refinement shell

Resolution: 2.6→2.67 Å / Total num. of bins used: 20 /

	R_factor	Num. reflection
R_free	0.347	356
R_work	0.3	6882

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°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)
1	1.5691	-0.3075	1.4481	1.8604	2.0692	6.1114	-0.1701	0.2278	0.0097	-0.0707	0.1346	-0.2239	-0.7974	1.2009	0.0355	-0.1289	-0.3368	0.0084	-0.0915	0.1066	-0.1676	52.01	49.878	82.433
2	1.9355	-0.0497	0.3199	1.5264	2.0888	6.27	-0.0499	0.4295	-0.1168	-0.4585	-0.0567	0.0959	-0.4778	0.3679	0.1066	-0.0368	-0.0756	0.0233	-0.1514	0.0095	-0.2281	38.571	35.266	45.596
3	2.8366	2.0762	2.196	2.3593	2.0991	5.6918	-0.1682	-0.6911	0.5739	-0.0744	-0.5493	0.5123	-0.5774	-1.3442	0.7175	-0.1649	0.0298	-0.0448	0.0199	-0.1641	-0.0929	28.124	46.765	90.31
4	2.2247	-0.4801	0.4856	2.3168	0.0539	2.5474	-0.2383	0.3573	0.0969	-0.6514	-0.2929	0.6054	-1.0777	-1.2705	0.5312	0.4107	0.3495	-0.3143	0.2987	-0.1734	-0.0047	18.057	49.321	48.745
5	2.0289	0.4469	0.7367	1.4071	0.7649	5.5008	-0.5104	0.0956	0.4993	-0.5033	-0.0947	0.1775	-2.3818	0.1758	0.6051	0.876	-0.0537	-0.2804	-0.3096	0.0491	-0.0343	37.529	64.192	69.139
6	1.7713	-0.1979	-0.6092	1.6018	0.7793	5.9373	-0.0971	0.2052	-0.1681	-0.0826	-0.1719	0.1678	0.8328	-0.9462	0.269	-0.1448	-0.1621	0.0304	-0.1897	-0.0744	-0.1789	27.943	27.174	65.983
7	1.9235	-0.4212	0.6065	1.4251	-1.9967	5.891	0.0154	-0.0319	-0.1638	-0.3725	-0.0936	0.0348	1.5297	-0.043	0.0782	0.1091	0.1864	0.1047	-0.3437	-0.04	-0.1575	49.456	-14.771	31.492
8	1.5028	0.1014	1.3534	1.5951	-1.4425	6.5631	-0.041	0.4178	0.1157	-0.5531	-0.0666	0.0663	0.6325	0.2831	0.1076	-0.1058	0.1109	0.0113	-0.0872	-0.0119	-0.2199	43.386	4.129	-5.315
9	0.9782	-0.702	0.812	4.4411	-2.3782	4.7569	-0.1149	0.0403	0.1604	0.6805	-0.5796	-0.7257	-0.8637	1.132	0.6945	-0.1007	-0.0679	-0.0994	-0.0318	0.1407	-0.0965	58.596	7.434	39.4
10	2.7657	-0.1784	0.1268	1.1818	-0.4235	2.3325	-0.167	0.6053	0.5005	-0.4412	-0.4155	-0.3497	-0.6017	1.4656	0.5826	-0.0072	-0.1231	0.0278	0.6644	0.373	0.0068	65.817	14.878	-2.162
11	1.0062	-0.1111	0.4117	2.2123	-1.3647	5.9693	-0.0221	0.2134	-0.0267	-0.4559	-0.6422	-0.4535	1.3964	2.1579	0.6644	-0.061	0.6104	0.2491	0.6242	0.2194	-0.0566	68.926	-9.468	18.202
12	1.9662	0.1426	1.0872	1.5361	-0.0771	5.987	-0.2194	0.1614	0.2206	-0.0808	-0.0613	0.0729	-1.2668	-0.2305	0.2807	-0.0903	0.1349	-0.0589	-0.2416	0.0322	-0.1718	41.711	17.365	15.055
13	1.6863	-0.6737	-2.6144	1.7806	-0.7365	6.1514	0.0959	-0.345	0.1014	0.075	-0.1978	-0.1152	-0.832	1.4103	0.1019	-0.4297	-0.1635	-0.0289	0.1785	0.0471	-0.1677	101.328	-35.627	19.444
14	1.4878	0.0384	-2.156	1.8587	0.5896	6.8401	0.0022	-0.5369	-0.0206	0.3859	-0.0923	0.1268	-0.1117	0.5795	0.0901	-0.2604	0.0338	0.0122	0.0308	-0.0063	-0.211	81.979	-39.927	56.241
15	3.8828	1.2246	-2.3324	1.2078	-0.601	5.4521	-0.7037	0.3187	-0.6825	-0.3122	0.0803	-0.252	1.443	-0.1961	0.6234	-0.0669	-0.05	0.2116	-0.1156	-0.0363	-0.0979	86.687	-54.767	11.569
16	2.0874	-0.6542	-0.496	2.5648	0.2473	2.5732	-0.3752	-0.5544	-0.5495	0.5277	-0.155	0.2865	1.6929	0.225	0.5302	0.5782	0.2316	0.3257	0.1159	0.193	-0.0286	83.853	-64.723	53.088
17	1.8126	0.2625	-1.1764	1.2735	-0.3093	5.7775	-0.3761	-0.5952	-0.3721	-0.0132	-0.2496	-0.3064	1.0908	2.2142	0.6257	-0.1163	0.5416	0.1457	0.6617	0.259	-0.0442	106.493	-55.282	32.74
18	1.2271	0.0962	-0.505	1.8692	0.6898	5.8018	-0.1133	-0.0438	-0.0307	0.236	-0.1446	0.2405	0.4569	-1.2679	0.2579	-0.3585	-0.0209	0.0966	0.034	-0.0559	-0.1582	69.655	-45.093	35.863

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	36 - 132
2	X-RAY DIFFRACTION	2	B	36 - 132
3	X-RAY DIFFRACTION	3	A	163 - 271
4	X-RAY DIFFRACTION	3	B	450 - 481
5	X-RAY DIFFRACTION	4	B	163 - 271
6	X-RAY DIFFRACTION	4	A	450 - 480
7	X-RAY DIFFRACTION	5	A	133 - 162
8	X-RAY DIFFRACTION	5	A	272 - 343
9	X-RAY DIFFRACTION	5	A	363 - 449
10	X-RAY DIFFRACTION	6	B	133 - 162
11	X-RAY DIFFRACTION	6	B	272 - 343
12	X-RAY DIFFRACTION	6	B	363 - 449
13	X-RAY DIFFRACTION	7	C	37 - 132
14	X-RAY DIFFRACTION	8	D	36 - 132
15	X-RAY DIFFRACTION	9	C	163 - 271
16	X-RAY DIFFRACTION	9	D	450 - 481
17	X-RAY DIFFRACTION	10	D	163 - 271
18	X-RAY DIFFRACTION	10	C	450 - 480
19	X-RAY DIFFRACTION	11	C	133 - 162
20	X-RAY DIFFRACTION	11	C	272 - 346
21	X-RAY DIFFRACTION	11	C	363 - 449
22	X-RAY DIFFRACTION	12	D	133 - 162
23	X-RAY DIFFRACTION	12	D	272 - 343
24	X-RAY DIFFRACTION	12	D	363 - 449
25	X-RAY DIFFRACTION	13	F	36 - 132
26	X-RAY DIFFRACTION	14	E	36 - 132
27	X-RAY DIFFRACTION	15	F	163 - 271
28	X-RAY DIFFRACTION	15	E	450 - 480
29	X-RAY DIFFRACTION	16	E	163 - 271
30	X-RAY DIFFRACTION	16	F	450 - 480
31	X-RAY DIFFRACTION	17	F	133 - 162
32	X-RAY DIFFRACTION	17	F	272 - 346
33	X-RAY DIFFRACTION	17	F	363 - 449
34	X-RAY DIFFRACTION	18	E	133 - 162
35	X-RAY DIFFRACTION	18	E	272 - 343
36	X-RAY DIFFRACTION	18	E	363 - 449

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