PDB-2odr: Methanococcus Maripaludis Phosphoseryl-tRNA synthetase

ID or keywords:

Entry

Database: PDB / ID: 2odr

Title

Methanococcus Maripaludis Phosphoseryl-tRNA synthetase

Components

(phosphoseryl-tRNA synthetase

O-phospho-L-serine—tRNA ligase) x 4

Keywords

LIGASE / phosphoserine tRNA synthetase class II

Function / homology

Function and homology information

O-phospho-L-serine-tRNA ligase / phosphoserine-tRNA(Cys) ligase activity / tRNA aminoacylation /

tRNA binding /

translation /

Biological species

Methanococcus maripaludis (archaea)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MIR / Resolution: 3.228 Å

Authors

Steitz, T.A. / Kamtekar, S.

Citation

Journal: Proc.Natl.Acad.Sci.Usa / Year: 2007
Title: Toward understanding phosphoseryl-tRNACys formation: the crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase.
Authors: Kamtekar, S. / Hohn, M.J. / Park, H.S. / Schnitzbauer, M. / Sauerwald, A. / Soll, D. / Steitz, T.A.

History

Deposition	Dec 26, 2006	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Feb 13, 2007	Provider: repository / Type: Initial release
Revision 1.1	May 1, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Source and taxonomy / Version format compliance
Revision 1.3	Oct 18, 2017	Group: Refinement description / Category: software Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.4	Dec 27, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id

Remark 999

SEQUENCE THE INSERTED AND C-TERMINAL DOMAINS OF THE SYNTHETASE ARE PARTIALLY DISORDERED. MANY OF ...

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2odr.cif.gz	341.2 KB	Display	PDBx/mmCIF format
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Others	Other downloads

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Validation report

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

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Related structure data

Similar structure data	5fwp-d 10131 5fwl-d 3341 5fwm-d 21850 6z8k-d 7bvc-d Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#16 - Apr 2001 Aminoacyl-tRNA Synthetases similarity (4)

Deposited unit

A: phosphoseryl-tRNA synthetase

B: phosphoseryl-tRNA synthetase

C: phosphoseryl-tRNA synthetase

D: phosphoseryl-tRNA synthetase

294 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	119.172, 133.943, 208.382
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
3	1	C
4	1	D
1	2	A
2	2	C
3	2	D
1	3	A
2	3	B
1	4	C
2	4	D
1	5	A
2	5	B
3	5	C
4	5	D

NCS domain segments:

Component-ID: 1 / Refine code: 1

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	PRO	PRO	PHE	PHE	A	A	40 - 343	59 - 362
2	1	PRO	PRO	PHE	PHE	B	B	40 - 343	59 - 362
3	1	PRO	PRO	PHE	PHE	C	C	40 - 343	59 - 362
4	1	PRO	PRO	PHE	PHE	D	D	40 - 343	59 - 362
1	2	ARG	ARG	LYS	LYS	A	A	4 - 29	23 - 48
2	2	ARG	ARG	LYS	LYS	C	C	4 - 29	23 - 48
3	2	ARG	ARG	LYS	LYS	D	D	4 - 29	23 - 48
1	3	GLU	GLU	UNK	UNK	A	A	345 - 1537	364 - 607
2	3	GLU	GLU	UNK	UNK	B	B	345 - 1537	364 - 604
1	4	GLU	GLU	UNK	UNK	C	C	345 - 1537	364 - 646
2	4	GLU	GLU	UNK	UNK	D	D	345 - 1537	364 - 647
1	5	UNK	UNK	UNK	UNK	A	A	2214 - 2276	615 - 665
2	5	UNK	UNK	UNK	UNK	B	B	2215 - 2275	612 - 648
3	5	UNK	UNK	UNK	UNK	C	C	2210 - 2275	647 - 701
4	5	UNK	UNK	UNK	UNK	D	D	2216 - 2276	648 - 685

NCS ensembles :

ID
1
2
3
4
5

#1: Protein	phosphoseryl-tRNA synthetase / O-phospho-L-serine—tRNA ligase Mass: 72592.969 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanococcus maripaludis (archaea) / Strain: S2 / Gene: MMP0688 / Plasmid: pet15b / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21 codon plus (DE3) RIL References: UniProt: Q6LZE1, Ligases; Forming carbon-oxygen bonds; Ligases forming aminoacyl-tRNA and related compounds
#2: Protein	phosphoseryl-tRNA synthetase / O-phospho-L-serine—tRNA ligase Mass: 71146.234 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanococcus maripaludis (archaea) / Strain: S2 / Gene: MMP0688 / Plasmid: pet15b / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21 codon plus (DE3) RIL References: UniProt: Q6LZE1, Ligases; Forming carbon-oxygen bonds; Ligases forming aminoacyl-tRNA and related compounds
#3: Protein	phosphoseryl-tRNA synthetase / O-phospho-L-serine—tRNA ligase Mass: 75656.641 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanococcus maripaludis (archaea) / Strain: S2 / Gene: MMP0688 / Plasmid: pet15b / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21 codon plus (DE3) RIL References: UniProt: Q6LZE1, Ligases; Forming carbon-oxygen bonds; Ligases forming aminoacyl-tRNA and related compounds
#4: Protein	phosphoseryl-tRNA synthetase / O-phospho-L-serine—tRNA ligase Mass: 74339.023 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanococcus maripaludis (archaea) / Strain: S2 / Gene: MMP0688 / Plasmid: pet15b / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21 codon plus (DE3) RIL References: UniProt: Q6LZE1, Ligases; Forming carbon-oxygen bonds; Ligases forming aminoacyl-tRNA and related compounds

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.9 Å³/Da / Density % sol: 57.54 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: Well:4-6% PEG 35,000, 5 mM DTT, 100 mM Sodium MES (pH 6.5), 5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

Diffraction

ID	Mean temperature (K)	Crystal-ID
1	100	1
2	100	1
3	100	1
1,2,3		1

Diffraction source

Source	Site	Beamline	ID	Wavelength (Å)
SYNCHROTRON	ALS	8.2.2	1	1.0039
SYNCHROTRON	ALS	8.2.2	2	1.214
SYNCHROTRON	ALS	8.2.2	3	1.0716

Detector

Type	ID	Detector
ADSC QUANTUM 210	1	CCD
ADSC QUANTUM 315	2	CCD
ADSC QUANTUM 210	3	CCD

Radiation

ID	Monochromator	Protocol	Monochromatic (M) / Laue (L)	Scattering type	Wavelength-ID
1	Si 111 CHANNEL	SINGLE WAVELENGTH	M	x-ray	1
2	Si 111 CHANNEL	MAD	M	x-ray	1
3	Si 111 CHANNEL	SINGLE WAVELENGTH	M	x-ray	1

Radiation wavelength

ID	Wavelength (Å)	Relative weight
1	1.0039	1
2	1.214	1
3	1.0716	1

Reflection

D res low: 50 Å

Redundancy (%)	ID	Av σ(I) over netI	Number	R_merge(I) obs	Χ²	D res high (Å)	Num. obs	% possible obs
3.8	1	7.5	157698	0.087	1.05	4.4	41750	100
3.2	2	7.9	120120	0.08	1.01	4.5	37108	95.1

Diffraction reflection shell

Highest resolution (Å)	Lowest resolution (Å)	% possible obs (%)	ID	R_merge(I) obs	Chi squared	Redundancy
9.46	50	99.8	1	0.041	1.051	3.7
7.52	9.46	100	1	0.052	1.031	3.8
6.57	7.52	100	1	0.102	0.975	3.8
5.97	6.57	100	1	0.179	1.029	3.8
5.54	5.97	100	1	0.268	1.053	3.8
5.22	5.54	100	1	0.33	1.053	3.8
4.96	5.22	100	1	0.409	1.069	3.8
4.74	4.96	100	1	0.46	1.076	3.8
4.56	4.74	100	1	0.557	1.075	3.7
4.4	4.56	100	1	0.849	1.092	3.7
9.67	50	99.9	2	0.033	0.937	3.8
7.69	9.67	100	2	0.047	0.935	3.8
6.72	7.69	100	2	0.127	1.029	3.8
6.11	6.72	100	2	0.232	1.06	3.8
5.67	6.11	100	2	0.382	1.059	3.8
5.33	5.67	99.8	2	0.478	1.017	3.5
5.07	5.33	98	2	0.514	1.018	2.9
4.85	5.07	93.7	2	0.552	1.057	2.4
4.66	4.85	85.4	2	0.603	1.052	2.1
4.5	4.66	74	2	0.838	0.992	1.9

Reflection

Resolution: 3.2→50 Å / Num. all: 53862 / Num. obs: 53215 / % possible obs: 98.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.7 % / R_merge(I) obs: 0.053 / Χ²: 1.035 / Net I/σ(I): 11

Reflection shell

Resolution: 3.2→3.31 Å / Redundancy: 3.5 % / R_merge(I) obs: 0.907 / Mean I/σ(I) obs: 1.1 / Num. unique all: 4992 / Χ²: 1.036 / % possible all: 94.4

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Phasing

Phasing

Method:

MIR

Phasing MIR

Resolution: 4.5→50 Å / FOM: 0.52 / Reflection: 19624

Phasing MIR der

ID	Der set-ID
1	1
2	1
3	1
4	1

Phasing MIR der site

B_iso : 60 Å

ID	Der-ID	Atom type symbol	Fract x	Fract y	Fract z	Occupancy
1	1	W	0.0972	0.1353	0.2467	1.0772
1	2	W	0.809	0.9417	0.1306	0.9662
1	3	W	0.0302	0.2071	0.1139	0.7101
1	4	W	0.2584	0.5468	0.2516	0.6198
2	1	Sm	0.3381	0.6271	0.2408	0.8075
2	2	Sm	0.824	0.5541	0.2338	0.7172
2	3	Sm	0.8634	0.8474	0.1238	0.7872
2	4	Sm	0.977	0.2958	0.0999	0.7684

Phasing MIR shell

Resolution (Å)	FOM	Reflection
15.87-50	0.61	973
10.13-15.87	0.63	1683
7.95-10.13	0.63	2133
6.76-7.95	0.63	2464
5.98-6.76	0.58	2744
5.41-5.98	0.5	2971
4.99-5.41	0.42	3230
4.64-4.99	0.34	3426

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
SOLVE	2.06	phasing
REFMAC		refinement
PDB_EXTRACT	2	data extraction
ADSC	QUANTUM	data collection
HKL-2000		data reduction

Refinement

Method to determine structure:

MIR / Resolution: 3.228→50 Å / Cor.coef. F_o:F_c: 0.901 / Cor.coef. F_o:F_c free: 0.893 / SU B: 55.877 / SU ML: 0.461 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.524 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.306	2697	5.1 %	RANDOM
R_work	0.292	-	-	-
obs	0.292	53170	97.86 %	-

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: 115.697 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-1.52 Å²	0 Å²	0 Å²
2-	-	-1.63 Å²	0 Å²
3-	-	-	3.15 Å²

Refinement step

Cycle: LAST / Resolution: 3.228→50 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13538	0	0	0	13538

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.008	0.022	13726
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	8914
X-RAY DIFFRACTION	r_angle_refined_deg	1.04	1.951	18541
X-RAY DIFFRACTION	r_angle_other_deg	0.842	3	21778
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.023	5	1795
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	34.031	24.423	520
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	18.539	15	2118
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	10.616	15	57
X-RAY DIFFRACTION	r_chiral_restr	0.062	0.2	2158
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.02	15371
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	2699
X-RAY DIFFRACTION	r_nbd_refined	0.224	0.2	3396
X-RAY DIFFRACTION	r_nbd_other	0.184	0.2	9440
X-RAY DIFFRACTION	r_nbtor_refined	0.182	0.2	6675
X-RAY DIFFRACTION	r_nbtor_other	0.086	0.2	7699
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.149	0.2	281
X-RAY DIFFRACTION	r_xyhbond_nbd_other	0.033	0.2	5
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.588	0.2	9
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.521	0.2	15
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.083	0.2	2
X-RAY DIFFRACTION	r_mcbond_it	0.378	1.5	11705
X-RAY DIFFRACTION	r_mcbond_other	0.146	1.5	3722
X-RAY DIFFRACTION	r_mcangle_it	0.498	2	14346
X-RAY DIFFRACTION	r_scbond_it	0.732	3	5418
X-RAY DIFFRACTION	r_scangle_it	0.976	4.5	4195

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	3237	TIGHT POSITIONAL	0.02	0.05
1	2	B	3237	TIGHT POSITIONAL	0.02	0.05
1	3	C	3237	TIGHT POSITIONAL	0.02	0.05
1	4	D	3237	TIGHT POSITIONAL	0.02	0.05
1	1	A	3237	TIGHT THERMAL	0.04	0.5
1	2	B	3237	TIGHT THERMAL	0.04	0.5
1	3	C	3237	TIGHT THERMAL	0.04	0.5
1	4	D	3237	TIGHT THERMAL	0.04	0.5
2	1	A	370	TIGHT POSITIONAL	0.01	0.05
2	2	C	370	TIGHT POSITIONAL	0.01	0.05
2	3	D	370	TIGHT POSITIONAL	0.01	0.05
2	1	A	370	TIGHT THERMAL	0.02	0.5
2	2	C	370	TIGHT THERMAL	0.02	0.5
2	3	D	370	TIGHT THERMAL	0.02	0.5
3	1	A	1808	TIGHT POSITIONAL	0.02	0.05
3	1	A	1808	TIGHT THERMAL	0.02	0.5
4	1	C	1249	TIGHT POSITIONAL	0.02	0.05
4	1	C	1249	TIGHT THERMAL	0.03	0.5
5	1	A	238	TIGHT POSITIONAL	0.01	0.05
5	2	B	238	TIGHT POSITIONAL	0.01	0.05
5	3	C	238	TIGHT POSITIONAL	0.01	0.05
5	4	D	238	TIGHT POSITIONAL	0.01	0.05
5	1	A	238	TIGHT THERMAL	0.02	0.5
5	2	B	238	TIGHT THERMAL	0.02	0.5
5	3	C	238	TIGHT THERMAL	0.02	0.5
5	4	D	238	TIGHT THERMAL	0.01	0.5

LS refinement shell

Resolution: 3.228→3.312 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.375	178	-
R_work	0.373	3037	-
obs	-	3215	80.74 %

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	1.4762	0.6864	0.2644	2.443	0.3109	3.9554	0.2023	0.174	-0.062	0.6187	0.0146	-0.5403	0.222	0.7124	-0.2169	-0.5346	0.1664	-0.0652	-0.6608	-0.0713	-0.1172	69.5189	16.4487	47.2078
2	2.3966	0.4654	-0.2015	1.7785	0.5836	4.6419	-0.0694	0.7192	0.4001	-0.03	0.2152	-0.0258	-0.4995	0.2752	-0.1458	-0.5056	0.0286	0.0064	-0.7098	0.128	-0.1208	62.0502	26.7577	28.9038
3	1.7195	0.4705	0.7599	1.9978	0.5577	4.3365	0.161	-0.1548	0.0364	0.5997	-0.058	0.867	-0.0606	-0.998	-0.103	-0.5126	0.1399	0.1277	-0.4142	0.1175	0.1366	30.6039	7.0733	47.2555
4	2.1337	0.2959	-0.2323	1.6666	0.4604	5.2188	0.0729	0.5357	-0.5487	0.1515	0.1135	0.4529	0.8621	-0.3275	-0.1864	-0.3962	0.0178	-0.1313	-0.6819	0.0665	0.0154	38.7769	-5.868	31.5113
5	4.4108	-3.6404	1.8898	11.0452	-2.9818	6.5553	-0.4701	0.3925	-0.3151	0.1993	0.2086	0.6731	0.8446	-1.6227	0.2615	0.3024	-0.1378	-0.364	0.48	-0.0683	0.3793	27.3216	-12.5183	7.0484
6	8.525	-3.9841	-2.9238	2.859	-2.037	12.6197	0.0061	0.7836	0.2784	-0.8273	0.59	-0.7543	-0.689	0.9744	-0.5962	-0.0384	-0.2654	0.2092	0.3457	0.1049	0.2099	73.9769	29.283	4.3168
7	12.2256	-0.8233	-1.7385	2.112	2.3182	12.0433	0.1014	-1.4073	0.4784	1.5862	-0.0908	-0.7872	-0.0442	0.3211	-0.0106	0.272	-0.0905	-0.278	-0.2818	-0.201	-0.0188	77.9067	27.6533	71.1288
8	4.6563	0.4686	1.5353	2.9504	1.9018	4.2857	-0.1411	0.4324	-0.2892	-0.0355	0.4504	-0.3352	-0.3652	0.3628	-0.3093	-0.1895	0.0311	-0.06	-0.0543	-0.1206	-0.0098	61.1015	-12.4868	1.5342
9	3.1758	1.4118	-3.4471	3.1965	-1.8324	5.461	0.3989	-0.2817	0.3544	0.1037	-0.0835	0.0949	-0.1629	0.4993	-0.3153	-0.1135	0.0596	0.145	-0.2131	-0.0976	0.0816	33.6942	32.1264	74.9978
10	5.0235	0.2188	-0.3344	1.1521	-1.6829	2.4583	-0.0164	1.0945	0.6948	-1.1643	0.1799	-0.003	-0.5656	0.6044	-0.1635	0.287	-0.1435	-0.1664	0.6214	0.3261	0.2564	43.945	27.9817	-9.6182
11	1.291	1.3813	0.0562	1.6246	-0.1175	3.9193	-0.0335	-1.1038	-0.1183	0.7596	0.0729	-0.056	0.114	0.5011	-0.0394	0.6266	-0.0486	-0.2407	0.2132	-0.0365	0.0829	64.8288	1.3339	87.6441
12	0.1283	1.3412	-0.8504	14.0238	-8.8915	5.6375	0.5183	0.4607	-0.393	-1.2462	-0.1831	0.1234	-0.6606	-0.0979	-0.3352	0.3534	-0.0403	0.3153	0.4707	-0.1051	0.24	79.0132	52.1396	15.5701
13	22.9361	6.093	5.2762	5.1641	5.8638	26.6165	-0.6687	-0.8547	0.2249	0.2897	-0.389	0.4921	-0.5094	-0.3737	1.0577	0.2919	0.2108	-0.2162	0.3728	-0.1084	0.6575	99.7401	22.3808	56.707
14	0.5349	-0.9104	-2.1907	7.4219	2.77	9.1281	0.7582	0.9705	-0.4101	-1.1698	-0.3322	-0.0699	0.9145	-0.2385	-0.4261	0.1875	-0.1593	-0.3647	0.5011	-0.0259	0.5201	22.6117	-33.3105	23.026
15	19.6625	6.8656	-8.8042	6.7201	-5.7567	30.3159	0.1228	-0.1989	0.0204	1.0339	-0.7612	0.1857	-0.2852	0.4801	0.6384	0.2853	0.1076	0.126	0.4884	0.0598	0.7621	0.8247	0.6296	58.6197

Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Selection: ALL

ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	A	A	30 - 343	49 - 362
2	2	B	B	31 - 343	50 - 362
3	3	C	C	30 - 343	49 - 362
4	4	D	D	30 - 343	49 - 362
5	5	A	A	4 - 26	23 - 45
6	6	C	C	4 - 26	23 - 45
7	7	D	D	4 - 26	23 - 45
8	8	A	A	345 - 1997	364 - 614
9	9	B	B	345 - 1997	364 - 611
10	10	C	C	1364 - 1537	557 - 646
11	11	D	D	1364 - 1537	557 - 647
12	12	A	A	2214 - 2276	615 - 665
13	13	B	B	2215 - 2275	612 - 648
14	14	C	C	2210 - 2275	647 - 701
15	15	D	D	2216 - 2276	648 - 685

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