PDB-1xxx: Crystal structure of Dihydrodipicolinate Synthase (DapA, Rv2753c)...

ID or keywords:

Entry

Database: PDB / ID: 1xxx

Title

Crystal structure of Dihydrodipicolinate Synthase (DapA, Rv2753c) from Mycobacterium tuberculosis

Components

Dihydrodipicolinate synthase

Keywords

LYASE / dihydrodipicolinate synthase / DapA / Rv2753c / Mycobacterium tuberculosis / lysine biosynthesis / Structural Genomics / PSI / Protein Structure Initiative / TB Structural Genomics Consortium / TBSGC

Function / homology

Function and homology information

4-hydroxy-tetrahydrodipicolinate synthase / 4-hydroxy-tetrahydrodipicolinate synthase activity / diaminopimelate biosynthetic process / lysine biosynthetic process via diaminopimelate / plasma membrane / cytosol
Similarity search - Function

Biological species

Mycobacterium tuberculosis (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.28 Å

Authors

Kefala, G. / Panjikar, S. / Janowski, R. / Weiss, M.S. / TB Structural Genomics Consortium (TBSGC)

Citation

Journal: Biochem.J. / Year: 2008
Title: Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis.
Authors: Kefala, G. / Evans, G.L. / Griffin, M.D. / Devenish, S.R. / Pearce, F.G. / Perugini, M.A. / Gerrard, J.A. / Weiss, M.S. / Dobson, R.C.

History

Deposition	Nov 9, 2004	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Feb 14, 2006	Provider: repository / Type: Initial release
Revision 1.1	Apr 30, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.3	Aug 23, 2023	Group: 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_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_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_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_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4	Oct 30, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Remark 999

SEQUENCE Author states that residue number one is indeed a VAL based on TB genome data base. THE ...

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

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Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/xx/1xxx ftp://data.pdbj.org/pub/pdb/validation_reports/xx/1xxx	HTTPS FTP

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Related structure data

Related structure data	1o5kS S: Starting model for refinement
Similar structure data	5j5d-1 5ktl-1 5ud6-d 5f1u-d 6xgs-d 3a5f-1 2yxg-d 7loy-1 3si9-d 4i7v-d 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
Other databases	TargetDB: Rv2753c

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#92 - Aug 2007 Anabolic Steroids similarity (1) #127 - Jul 2010 Crystallins similarity (1) #174 - Jun 2014 GFP-like Proteins similarity (1) #89 - May 2007 Aconitase and Iron Regulatory Protein 1 similarity (1)

Deposited unit

A: Dihydrodipicolinate synthase

B: Dihydrodipicolinate synthase

C: Dihydrodipicolinate synthase

D: Dihydrodipicolinate synthase

E: Dihydrodipicolinate synthase

F: Dihydrodipicolinate synthase

G: Dihydrodipicolinate synthase

H: Dihydrodipicolinate synthase

hetero molecules

251 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Dihydrodipicolinate synthase

B: Dihydrodipicolinate synthase

C: Dihydrodipicolinate synthase

D: Dihydrodipicolinate synthase

hetero molecules

defined by author&software
125 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: Dihydrodipicolinate synthase

F: Dihydrodipicolinate synthase

G: Dihydrodipicolinate synthase

H: Dihydrodipicolinate synthase

hetero molecules

defined by author&software
125 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	94.790, 87.370, 139.850
Angle α, β, γ (deg.)	90.00, 107.78, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Ens-ID: 1 / Refine code: 1

Dom-ID	Component-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	ASP	ASP	SER	SER	A	A	7 - 24	10 - 27
2	1	ASP	ASP	SER	SER	B	B	7 - 24	10 - 27
3	1	ASP	ASP	SER	SER	C	C	7 - 24	10 - 27
4	1	ASP	ASP	SER	SER	D	D	7 - 24	10 - 27
5	1	ASP	ASP	SER	SER	E	E	7 - 24	10 - 27
6	1	ASP	ASP	SER	SER	F	F	7 - 24	10 - 27
7	1	ASP	ASP	SER	SER	G	G	7 - 24	10 - 27
8	1	ASP	ASP	SER	SER	H	H	7 - 24	10 - 27
9	2	SER	SER	ALA	ALA	A	A	28 - 34	31 - 37
10	2	SER	SER	ALA	ALA	B	B	28 - 34	31 - 37
11	2	SER	SER	ALA	ALA	C	C	28 - 34	31 - 37
12	2	SER	SER	ALA	ALA	D	D	28 - 34	31 - 37
13	2	SER	SER	ALA	ALA	E	E	28 - 34	31 - 37
14	2	SER	SER	ALA	ALA	F	F	28 - 34	31 - 37
15	2	SER	SER	ALA	ALA	G	G	28 - 34	31 - 37
16	2	SER	SER	ALA	ALA	H	H	28 - 34	31 - 37
17	3	ALA	ALA	ILE	ILE	A	A	38 - 67	41 - 70
18	3	ALA	ALA	ILE	ILE	B	B	38 - 67	41 - 70
19	3	ALA	ALA	ILE	ILE	C	C	38 - 67	41 - 70
20	3	ALA	ALA	ILE	ILE	D	D	38 - 67	41 - 70
21	3	ALA	ALA	ILE	ILE	E	E	38 - 67	41 - 70
22	3	ALA	ALA	ILE	ILE	F	F	38 - 67	41 - 70
23	3	ALA	ALA	ILE	ILE	G	G	38 - 67	41 - 70
24	3	ALA	ALA	ILE	ILE	H	H	38 - 67	41 - 70
25	4	CYS	CYS	LEU	LEU	A	A	102 - 125	105 - 128
26	4	CYS	CYS	LEU	LEU	B	B	102 - 125	105 - 128
27	4	CYS	CYS	LEU	LEU	C	C	102 - 125	105 - 128
28	4	CYS	CYS	LEU	LEU	D	D	102 - 125	105 - 128
29	4	CYS	CYS	LEU	LEU	E	E	102 - 125	105 - 128
30	4	CYS	CYS	LEU	LEU	F	F	102 - 125	105 - 128
31	4	CYS	CYS	LEU	LEU	G	G	102 - 125	105 - 128
32	4	CYS	CYS	LEU	LEU	H	H	102 - 125	105 - 128
33	5	ALA	ALA	PHE	PHE	A	A	127 - 129	130 - 132
34	5	ALA	ALA	PHE	PHE	B	B	127 - 129	130 - 132
35	5	ALA	ALA	PHE	PHE	C	C	127 - 129	130 - 132
36	5	ALA	ALA	PHE	PHE	D	D	127 - 129	130 - 132
37	5	ALA	ALA	PHE	PHE	E	E	127 - 129	130 - 132
38	5	ALA	ALA	PHE	PHE	F	F	127 - 129	130 - 132
39	5	ALA	ALA	PHE	PHE	G	G	127 - 129	130 - 132
40	5	ALA	ALA	PHE	PHE	H	H	127 - 129	130 - 132
41	6	ALA	ALA	THR	THR	A	A	131 - 136	134 - 139
42	6	ALA	ALA	THR	THR	B	B	131 - 136	134 - 139
43	6	ALA	ALA	THR	THR	C	C	131 - 136	134 - 139
44	6	ALA	ALA	THR	THR	D	D	131 - 136	134 - 139
45	6	ALA	ALA	THR	THR	E	E	131 - 136	134 - 139
46	6	ALA	ALA	THR	THR	F	F	131 - 136	134 - 139
47	6	ALA	ALA	THR	THR	G	G	131 - 136	134 - 139
48	6	ALA	ALA	THR	THR	H	H	131 - 136	134 - 139
49	7	LEU	LEU	ALA	ALA	A	A	138 - 162	141 - 165
50	7	LEU	LEU	ALA	ALA	B	B	138 - 162	141 - 165
51	7	LEU	LEU	ALA	ALA	C	C	138 - 162	141 - 165
52	7	LEU	LEU	ALA	ALA	D	D	138 - 162	141 - 165
53	7	LEU	LEU	ALA	ALA	E	E	138 - 162	141 - 165
54	7	LEU	LEU	ALA	ALA	F	F	138 - 162	141 - 165
55	7	LEU	LEU	ALA	ALA	G	G	138 - 162	141 - 165
56	7	LEU	LEU	ALA	ALA	H	H	138 - 162	141 - 165
57	8	HIS	HIS	ASP	ASP	A	A	164 - 176	167 - 179
58	8	HIS	HIS	ASP	ASP	B	B	164 - 176	167 - 179
59	8	HIS	HIS	ASP	ASP	C	C	164 - 176	167 - 179
60	8	HIS	HIS	ASP	ASP	D	D	164 - 176	167 - 179
61	8	HIS	HIS	ASP	ASP	E	E	164 - 176	167 - 179
62	8	HIS	HIS	ASP	ASP	F	F	164 - 176	167 - 179
63	8	HIS	HIS	ASP	ASP	G	G	164 - 176	167 - 179
64	8	HIS	HIS	ASP	ASP	H	H	164 - 176	167 - 179
65	9	HIS	HIS	GLY	GLY	A	A	178 - 194	181 - 197
66	9	HIS	HIS	GLY	GLY	B	B	178 - 194	181 - 197
67	9	HIS	HIS	GLY	GLY	C	C	178 - 194	181 - 197
68	9	HIS	HIS	GLY	GLY	D	D	178 - 194	181 - 197
69	9	HIS	HIS	GLY	GLY	E	E	178 - 194	181 - 197
70	9	HIS	HIS	GLY	GLY	F	F	178 - 194	181 - 197
71	9	HIS	HIS	GLY	GLY	G	G	178 - 194	181 - 197
72	9	HIS	HIS	GLY	GLY	H	H	178 - 194	181 - 197
73	10	ASP	ASP	LEU	LEU	A	A	196 - 222	199 - 225
74	10	ASP	ASP	LEU	LEU	B	B	196 - 222	199 - 225
75	10	ASP	ASP	LEU	LEU	C	C	196 - 222	199 - 225
76	10	ASP	ASP	LEU	LEU	D	D	196 - 222	199 - 225
77	10	ASP	ASP	LEU	LEU	E	E	196 - 222	199 - 225
78	10	ASP	ASP	LEU	LEU	F	F	196 - 222	199 - 225
79	10	ASP	ASP	LEU	LEU	G	G	196 - 222	199 - 225
80	10	ASP	ASP	LEU	LEU	H	H	196 - 222	199 - 225
81	11	ASN	ASN	THR	THR	A	A	241 - 282	244 - 285
82	11	ASN	ASN	THR	THR	B	B	241 - 282	244 - 285
83	11	ASN	ASN	THR	THR	C	C	241 - 282	244 - 285
84	11	ASN	ASN	THR	THR	D	D	241 - 282	244 - 285
85	11	ASN	ASN	THR	THR	E	E	241 - 282	244 - 285
86	11	ASN	ASN	THR	THR	F	F	241 - 282	244 - 285
87	11	ASN	ASN	THR	THR	G	G	241 - 282	244 - 285
88	11	ASN	ASN	THR	THR	H	H	241 - 282	244 - 285

Details

DapA occurs as a tetramer. The asymmetric unit contains two tetramers ABCD and EFGH.

#1: Protein	Dihydrodipicolinate synthase / DHDPS Mass: 31115.477 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Gene: dapA / Plasmid: pETM-11 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RP References: UniProt: P63945, UniProt: P9WP25*PLUS, dihydrodipicolinate synthase
#2: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#3: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Cl
#4: Chemical	ChemComp-DTT / 2,3-DIHYDROXY-1,4-DITHIOBUTANE / 1,4-DITHIOTHREITOL Mass: 154.251 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₄H₁₀O₂S₂
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1587 / Source method: isolated from a natural source / Formula: H₂O
Has protein modification	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.08 Å³/Da / Density % sol: 40.32 %
Crystal grow	Temperature: 292 K / pH: 8.5 Details: 100 mM Tris-HCl, 28 % PEG 4000, 170 mM MgCl2, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K, pH 8.50

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 0.981
Detector	Type: MARRESEARCH / Detector: CCD / Date: May 7, 2004
Radiation	Monochromator: DOUBLE CRYSTAL (SI111, SI220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.981 Å / Relative weight: 1
Reflection	Resolution: 2.28→99 Å / Num. obs: 99893 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / R_merge(I) obs: 0.085 / Net I/σ(I): 27.98
Reflection shell	Resolution: 2.28→2.32 Å / R_merge(I) obs: 0.192 / Mean I/σ(I) obs: 12.53 / % possible all: 95

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0005	refinement
DENZO		data reduction
SCALEPACK		data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1O5K

1o5k

Resolution: 2.28→30 Å / Cor.coef. F_o:F_c: 0.962 / Cor.coef. F_o:F_c free: 0.927 / SU B: 10.125 / SU ML: 0.139 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.311 / ESU R Free: 0.217 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: TLS REFINEMENT

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.215	1987	2 %	RANDOM
R_work	0.148	-	-	-
obs	0.149	97308	100 %	-
all	-	99362	-	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK

Displacement parameters

B_iso mean: 29.5 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.71 Å²	0 Å²	-1.07 Å²
2-	-	1.44 Å²	0 Å²
3-	-	-	-1.38 Å²

Refinement step

Cycle: LAST / Resolution: 2.28→30 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	17072	0	80	1587	18739

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.018	0.022	17408
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.628	1.984	23708
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.496	5	2356
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	36.971	23.462	624
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	13.805	15	2664
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	17.901	15	128
X-RAY DIFFRACTION	r_chiral_restr	0.096	0.2	2872
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.02	13032
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.219	0.2	10615
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.31	0.2	12512
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.151	0.2	1851
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	0.216	0.2	75
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.202	0.2	48
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_mcbond_it	0.943	1.5	11970
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	1.53	2.5	18604
X-RAY DIFFRACTION	r_scbond_it	4.049	5	5971
X-RAY DIFFRACTION	r_scangle_it	5.89	10	5104
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Ens-ID: 1 / Number: 1517 / Refine-ID: X-RAY DIFFRACTION

Dom-ID	Auth asym-ID	Type	Rms dev position (Å)	Weight position
1	A	tight positional	0.07	0.05
2	B	tight positional	0.06	0.05
3	C	tight positional	0.07	0.05
4	D	tight positional	0.07	0.05
5	E	tight positional	0.06	0.05
6	F	tight positional	0.05	0.05
7	G	tight positional	0.07	0.05
8	H	tight positional	0.06	0.05
1	A	tight thermal	0.97	1.5
2	B	tight thermal	0.93	1.5
3	C	tight thermal	0.94	1.5
4	D	tight thermal	0.9	1.5
5	E	tight thermal	0.83	1.5
6	F	tight thermal	0.77	1.5
7	G	tight thermal	0.93	1.5
8	H	tight thermal	0.89	1.5

LS refinement shell

Resolution: 2.28→2.34 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.235	145	-
R_work	0.165	7137	-
obs	-	-	100 %

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	1.1294	-0.0668	-0.0542	0.8794	0.1549	1.3174	-0.0697	-0.0775	0.0956	0.0956	0.06	0.042	-0.139	-0.1202	0.0097	-0.1625	0.0247	0.0006	-0.1343	0.0027	-0.084	2.7092	44.6836	68.3558
3	1.6981	0.1254	-0.0262	0.5586	0.0042	0.683	-0.0432	-0.0255	-0.157	-0.0395	0.0453	0.0333	0.1192	-0.0432	-0.002	-0.1593	0.0123	0.0208	-0.1342	0.0218	-0.0653	4.0745	-3.2335	79.412
5	1.2817	-0.1696	-0.2281	0.8806	-0.0484	2.0971	-0.0175	-0.0117	-0.0586	-0.0511	-0.0464	0.0463	-0.1572	-0.4121	0.064	0.1257	0.1118	-0.0597	-0.0072	-0.0369	-0.1157	-25.1786	-23.0114	-14.8957
7	1.2956	0.1885	0.2673	1.4131	-0.0935	1.0322	-0.0741	-0.0338	0.0951	-0.0319	-0.0428	-0.0227	-0.1527	-0.08	0.1169	-0.1158	0.0082	-0.0096	-0.1321	-0.0118	-0.1215	-8.7285	-17.2919	31.0321

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	X-RAY DIFFRACTION	1	A	A	5 - 300	8 - 303
2	X-RAY DIFFRACTION	3	C	C	5 - 300	8 - 303
3	X-RAY DIFFRACTION	5	E	E	6 - 300	9 - 303
4	X-RAY DIFFRACTION	7	G	G	6 - 300	9 - 303

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