PDB-3jz4: Crystal structure of E. coli NADP dependent enzyme

ID or keywords:

Entry

Database: PDB / ID: 3jz4

Title

Crystal structure of E. coli NADP dependent enzyme

Components

Succinate-semialdehyde dehydrogenase [NADP+]

Keywords

OXIDOREDUCTASE /

Tetramer /

NADP binding /

NADP

Function / homology

Function and homology information

glutarate-semialdehyde dehydrogenase (NADP+) activity /

succinate-semialdehyde dehydrogenase (NADP+) /

succinate-semialdehyde dehydrogenase (NADP+) activity / succinate-semialdehyde dehydrogenase [NAD(P)+] activity / succinate-semialdehyde dehydrogenase (NAD+) activity / gamma-aminobutyric acid catabolic process /

Oxidoreductases; Acting on the aldehyde or oxo group of donors; With NAD+ or NADP+ as acceptor /

: /

NADP binding / protein homotetramerization
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.3 Å

Authors

Langendorf, C.G. / Key, T.L.G. / Fenalti, G. / Kan, W.T. / Buckle, A.M. / Caradoc-Davies, T. / Tuck, K.L. / Law, R.H.P. / Whisstock, J.C.

Citation

Journal: Plos One / Year: 2010
Title: The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions.
Authors: Langendorf, C.G. / Key, T.L. / Fenalti, G. / Kan, W.T. / Buckle, A.M. / Caradoc-Davies, T. / Tuck, K.L. / Law, R.H. / Whisstock, J.C.

History

Deposition	Sep 22, 2009	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 16, 2010	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.2	Feb 21, 2024	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 / 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 / _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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Download

PDBx/mmCIF format	3jz4.cif.gz	369.1 KB	Display	PDBx/mmCIF format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/jz/3jz4 ftp://data.pdbj.org/pub/pdb/validation_reports/jz/3jz4	HTTPS FTP

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Related structure data

Similar structure data	3ek1-1 4v6h-6 2w8p-2 5kf0-d 3k2w-1 3ek1-2 4qyj-1 2w8o-2 4pxl-1 5mz5-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	#127 - Jul 2010 Crystallins similarity (7) #89 - May 2007 Aconitase and Iron Regulatory Protein 1 similarity (7)

Deposited unit

A: Succinate-semialdehyde dehydrogenase [NADP+]

B: Succinate-semialdehyde dehydrogenase [NADP+]

C: Succinate-semialdehyde dehydrogenase [NADP+]

D: Succinate-semialdehyde dehydrogenase [NADP+]

hetero molecules

210 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)	151.885, 151.885, 165.772
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	90
Space group name H-M	P42₁2

Noncrystallographic symmetry (NCS)

NCS domain:

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

NCS domain segments:

Ens-ID: 1

Dom-ID	Component-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	LEU	LEU	ARG	ARG	1	A	A	2 - 9	2 - 9
2	1	LEU	LEU	ARG	ARG	1	B	B	2 - 9	2 - 9
3	1	LEU	LEU	ARG	ARG	1	C	C	2 - 9	2 - 9
4	1	LEU	LEU	ARG	ARG	1	D	D	2 - 9	2 - 9
1	2	GLN	GLN	VAL	VAL	1	A	A	10 - 208	10 - 208
2	2	GLN	GLN	VAL	VAL	1	B	B	10 - 208	10 - 208
3	2	GLN	GLN	VAL	VAL	1	C	C	10 - 208	10 - 208
4	2	GLN	GLN	VAL	VAL	1	D	D	10 - 208	10 - 208
1	3	THR	THR	ALA	ALA	6	A	A	209 - 214	209 - 214
2	3	THR	THR	ALA	ALA	6	B	B	209 - 214	209 - 214
3	3	THR	THR	ALA	ALA	6	C	C	209 - 214	209 - 214
4	3	THR	THR	ALA	ALA	6	D	D	209 - 214	209 - 214
1	4	VAL	VAL	MET	MET	1	A	A	215 - 312	215 - 312
2	4	VAL	VAL	MET	MET	1	B	B	215 - 312	215 - 312
3	4	VAL	VAL	MET	MET	1	C	C	215 - 312	215 - 312
4	4	VAL	VAL	MET	MET	1	D	D	215 - 312	215 - 312
1	5	SER	SER	HIS	HIS	6	A	A	313 - 316	313 - 316
2	5	SER	SER	HIS	HIS	6	B	B	313 - 316	313 - 316
3	5	SER	SER	HIS	HIS	6	C	C	313 - 316	313 - 316
4	5	SER	SER	HIS	HIS	6	D	D	313 - 316	313 - 316
1	6	ILE	ILE	PRO	PRO	1	A	A	317 - 329	317 - 329
2	6	ILE	ILE	PRO	PRO	1	B	B	317 - 329	317 - 329
3	6	ILE	ILE	PRO	PRO	1	C	C	317 - 329	317 - 329
4	6	ILE	ILE	PRO	PRO	1	D	D	317 - 329	317 - 329
1	7	LEU	LEU	ALA	ALA	4	A	A	330 - 359	330 - 359
2	7	LEU	LEU	ALA	ALA	4	B	B	330 - 359	330 - 359
3	7	LEU	LEU	ALA	ALA	4	C	C	330 - 359	330 - 359
4	7	LEU	LEU	ALA	ALA	4	D	D	330 - 359	330 - 359
1	8	HIS	HIS	ASN	ASN	3	A	A	360 - 365	360 - 365
2	8	HIS	HIS	ASN	ASN	3	B	B	360 - 365	360 - 365
3	8	HIS	HIS	ASN	ASN	3	C	C	360 - 365	360 - 365
4	8	HIS	HIS	ASN	ASN	3	D	D	360 - 365	360 - 365
1	9	PHE	PHE	ALA	ALA	4	A	A	366 - 400	366 - 400
2	9	PHE	PHE	ALA	ALA	4	B	B	366 - 400	366 - 400
3	9	PHE	PHE	ALA	ALA	4	C	C	366 - 400	366 - 400
4	9	PHE	PHE	ALA	ALA	4	D	D	366 - 400	366 - 400
1	10	ASP	ASP	GLU	GLU	1	A	A	401 - 462	401 - 462
2	10	ASP	ASP	GLU	GLU	1	B	B	401 - 462	401 - 462
3	10	ASP	ASP	GLU	GLU	1	C	C	401 - 462	401 - 462
4	10	ASP	ASP	GLU	GLU	1	D	D	401 - 462	401 - 462
1	11	GLY	GLY	TYR	TYR	6	A	A	463 - 466	463 - 466
2	11	GLY	GLY	TYR	TYR	6	B	B	463 - 466	463 - 466
3	11	GLY	GLY	TYR	TYR	6	C	C	463 - 466	463 - 466
4	11	GLY	GLY	TYR	TYR	6	D	D	463 - 466	463 - 466
1	12	GLY	GLY	LEU	LEU	1	A	A	467 - 481	467 - 481
2	12	GLY	GLY	LEU	LEU	1	B	B	467 - 481	467 - 481
3	12	GLY	GLY	LEU	LEU	1	C	C	467 - 481	467 - 481
4	12	GLY	GLY	LEU	LEU	1	D	D	467 - 481	467 - 481

Details

Four monomers related by non-crystallographic 222 symetry

#1: Protein	Succinate-semialdehyde dehydrogenase [NADP+] / SSDH / NADP dependent enzyme Mass: 51677.719 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: MC1061 / Gene: b2661, gabD, JW2636, NA / Plasmid: pRSETc / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: P25526, succinate-semialdehyde dehydrogenase [NAD(P)+]
#2: Chemical	ChemComp-NAP / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE / Nicotinamide adenine dinucleotide phosphate Mass: 743.405 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₂₁H₂₈N₇O₁₇P₃
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 331 / Source method: isolated from a natural source / Formula: H₂O
Sequence details	THE AUTHORS SAID THEY BELIEVE THE MISMATCH OBSERVED REPRESENTS A NATURALLY OCCURRING VARIANT OF THE ...THE AUTHORS SAID THEY BELIEVE THE MISMATCH OBSERVED REPRESENTS A NATURALLY OCCURRING VARIANT OF THE E. COLI SSADH GENE. AUTHORS SEQUENCED MANY SSADH CDNA SEQUENCES FROM GENOMIC DNA ISOLATED FROM THE E. COLI VARIANT MC1061 AND FOUND THIS MISMATCH OCCURRED IN ALL SEQUENCES. THE MISMATCH ARISES FROM A SINGLE NUCLEOTIDE CHANGE FROM GTG TO ATG RESULTING IN A CHANGE IN THE PROTEIN SEQUENCE VAL TO MET.

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.31 Å³/Da / Density % sol: 46.81 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.2 M ammonium tartrate, 30 % PEG 3350, 10 mM 2-mercaptoethanol, 0.1 M tris, pH 7.5, temperature 298K, VAPOR DIFFUSION, HANGING DROP

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.95364 Å
Detector	Type: ADSC QUANTUM 210r / Detector: CCD / Date: Mar 15, 2008 / Details: NA
Radiation	Monochromator: NA / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.95364 Å / Relative weight: 1
Reflection	Resolution: 2.3→37.56 Å / Num. obs: 74567 / R_merge(I) obs: 0.188
Reflection shell	Highest resolution: 2.3 Å / R_merge(I) obs: 0.188 / Mean I/σ(I) obs: 3.2

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
MOSFLM		data reduction
SCALA		data scaling
PHASER		phasing
REFMAC		refinement
PDB_EXTRACT	3.005	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.3→37.56 Å / Cor.coef. F_o:F_c: 0.949 / Cor.coef. F_o:F_c free: 0.916 / WR_factor R_free: 0.169 / WR_factor R_work: 0.135 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.878 / SU B: 13.053 / SU ML: 0.158 / SU R Cruickshank DPI: 0.518 / SU R_free: 0.243 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.518 / ESU R Free: 0.243 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.213	3717	5 %	RANDOM
R_work	0.168	-	-	-
obs	0.17	74545	86.33 %	-

Solvent computation

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

Displacement parameters

B_iso max: 69.15 Å² / B_iso mean: 19.734 Å² / B_iso min: 2 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.14 Å²	0 Å²	0 Å²
2-	-	-0.14 Å²	0 Å²
3-	-	-	0.28 Å²

Refinement step

Cycle: LAST / Resolution: 2.3→37.56 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	14380	0	192	331	14903

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.01	0.022	15060
X-RAY DIFFRACTION	r_angle_refined_deg	1.297	1.979	20475
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.056	5	1977
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	34.037	24.664	639
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.89	15	2456
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	14.936	15	87
X-RAY DIFFRACTION	r_chiral_restr	0.094	0.2	2294
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.02	11437
X-RAY DIFFRACTION	r_nbd_refined	0.198	0.2	7251
X-RAY DIFFRACTION	r_nbtor_refined	0.3	0.2	10370
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.136	0.2	800
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.264	0.2	71
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.136	0.2	13
X-RAY DIFFRACTION	r_mcbond_it	1.456	4	9851
X-RAY DIFFRACTION	r_mcangle_it	2.191	6	15300
X-RAY DIFFRACTION	r_scbond_it	1.845	4	5862
X-RAY DIFFRACTION	r_scangle_it	2.775	6	5150

Refine LS restraints NCS

Dom-ID: 1 / Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
A	2939	TIGHT POSITIONAL	0.06	0.05
B	2939	TIGHT POSITIONAL	0.06	0.05
C	2939	TIGHT POSITIONAL	0.04	0.05
D	2939	TIGHT POSITIONAL	0.04	0.05
A	467	MEDIUM POSITIONAL	0.6	0.5
B	467	MEDIUM POSITIONAL	0.66	0.5
C	467	MEDIUM POSITIONAL	0.39	0.5
D	467	MEDIUM POSITIONAL	0.36	0.5
A	107	LOOSE POSITIONAL	0.39	5
B	107	LOOSE POSITIONAL	0.62	5
C	107	LOOSE POSITIONAL	0.29	5
D	107	LOOSE POSITIONAL	0.58	5
A	2939	TIGHT THERMAL	0.11	0.5
B	2939	TIGHT THERMAL	0.1	0.5
C	2939	TIGHT THERMAL	0.09	0.5
D	2939	TIGHT THERMAL	0.09	0.5
A	467	MEDIUM THERMAL	0.74	2
B	467	MEDIUM THERMAL	0.68	2
C	467	MEDIUM THERMAL	0.66	2
D	467	MEDIUM THERMAL	0.61	2
A	107	LOOSE THERMAL	5.27	10
B	107	LOOSE THERMAL	2.6	10
C	107	LOOSE THERMAL	2.91	10
D	107	LOOSE THERMAL	2.24	10

LS refinement shell

Highest resolution: 2.3 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.214	246	-
R_work	0.17	4599	-
all	-	4845	-
obs	-	74567	77.17 %

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	1.0855	-0.5949	0.1826	1.3283	-0.7105	1.3322	0.0628	0.1446	0.0794	-0.1138	-0.0783	-0.1429	-0.0358	0.1623	0.0155	0.0244	-0.0024	0.047	0.1192	0.0066	0.0769	-6.663	42.5695	9.8909
2	0.3491	-0.0223	-0.1254	0.2799	0.0717	0.2499	0.0194	-0.0011	0.0186	-0.0213	-0.0026	-0.017	0.0173	0.0115	-0.0168	0.0567	0.0094	0.0009	0.0788	-0.0108	0.0674	-18.8533	38.6646	22.3396
3	3.8948	-0.1409	-1.1066	0.9834	-0.2592	1.9213	0.1395	0.3585	0.1655	-0.1257	-0.0385	0.0371	-0.0567	-0.1456	-0.101	0.0436	0.0277	-0.0047	0.0345	0.0388	0.0473	-37.7593	60.4983	11.5624
4	1.385	-1.0486	0.2867	1.656	-0.2946	0.5432	-0.0647	0.0367	0.0805	0.0762	0.0346	0.0265	-0.0008	-0.0565	0.0301	0.055	-0.0216	0.0197	0.0723	0.0019	0.0563	-38.7237	42.0862	26.0531
5	1.2593	-0.288	0.1905	1.952	-0.0676	1.1484	0.0452	0.0049	-0.1307	-0.242	-0.0234	0.3557	0.0952	-0.0684	-0.0219	0.1118	-0.0205	-0.0327	0.0552	-0.003	0.0561	-55.6011	9.5843	15.0519
6	0.3851	0.0613	0.1253	0.2942	0.0599	0.294	0.0035	-0.0197	-0.0405	-0.0304	-0.0045	-0.0265	0.0407	-0.0177	0.001	0.1031	-0.0027	-0.0018	0.0648	0.0141	0.0595	-43.6447	18.4856	25.6486
7	1.7426	0.6777	0.3455	0.9777	0.5461	0.3645	0.0206	0.1816	-0.3015	-0.0791	0.0983	-0.1739	0.0564	0.1003	-0.1189	0.139	0.0299	0.0112	0.0351	-0.0087	0.1316	-24.153	-5.2586	23.1118
8	1.495	-1.21	0.1019	1.8839	0.0071	0.4586	-0.0251	-0.0132	-0.084	0.0456	0.0935	-0.1219	0.0931	0.0352	-0.0684	0.082	-0.0151	-0.0139	0.0663	0.0074	0.0832	-23.898	16.9305	30.7837
9	0.5277	-0.2171	-0.7849	0.8875	0.015	1.6996	-0.0883	0.0027	-0.0405	0.2803	0.0218	0.1942	0.2185	-0.1143	0.0665	0.2186	-0.0398	0.0525	0.0972	0.007	0.0754	-54.0411	18.5587	64.7875
10	0.2626	0.0432	0.0138	0.478	0.0398	0.1848	-0.0389	-0.0813	0.0118	0.1896	0.0147	0.0262	0.0946	-0.0063	0.0242	0.2058	0.0187	-0.0004	0.1494	0.015	0.0459	-41.0866	26.8112	61.6239
11	0.4743	0.6774	-0.8859	3.4833	-1.4053	1.6625	0.0674	0.078	0.0221	0.4945	0.0712	0.3743	-0.1676	-0.1545	-0.1386	0.1366	0.0264	0.0598	0.1429	0.0299	0.1327	-63.1539	49.5899	62.3528
12	1.073	-0.752	0.2869	1.4131	-0.1384	0.7445	-0.0153	-0.13	0.0026	0.0903	0.0145	0.1286	-0.1009	-0.094	0.0008	0.0947	-0.0126	0.0078	0.1032	0.002	0.0571	-42.7138	44.0675	52.1067
13	4.2339	-1.1665	0.5369	1.1823	0.4448	1.6091	-0.146	-0.173	0.4234	0.1435	0.2569	-0.3337	-0.2213	0.2995	-0.1109	0.1123	-0.0055	-0.0665	0.2113	-0.1372	0.1907	-9.6225	56.4406	67.4512
14	0.3196	-0.0387	0.025	0.4378	0.3872	0.6704	-0.0376	-0.1562	0.0324	0.0826	0.1231	-0.1069	0.0141	0.1095	-0.0855	0.1088	0.0254	-0.0304	0.1772	-0.0501	0.0842	-19.0509	44.2967	57.0826
15	2.1814	0.4329	0.4292	4.2596	0.6555	1.1932	-0.0313	-0.6982	0.0178	0.4626	0.1466	-0.07	0.2537	0.1558	-0.1153	0.1914	0.1433	-0.0835	0.3615	-0.0355	0.0261	-0.8135	21.8185	68.04
16	1.3702	-0.683	0.0354	1.284	0.0059	0.8372	-0.0525	-0.2283	-0.0634	0.2161	0.0911	-0.1288	0.1851	0.155	-0.0385	0.149	0.0222	-0.0269	0.1278	-0.0014	0.0701	-20.7966	23.6108	56.2609

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 60
2	X-RAY DIFFRACTION	2	A	61 - 264
3	X-RAY DIFFRACTION	3	A	265 - 394
4	X-RAY DIFFRACTION	4	A	395 - 481
5	X-RAY DIFFRACTION	5	B	1 - 58
6	X-RAY DIFFRACTION	6	B	59 - 264
7	X-RAY DIFFRACTION	7	B	265 - 394
8	X-RAY DIFFRACTION	8	B	395 - 481
9	X-RAY DIFFRACTION	9	C	1 - 113
10	X-RAY DIFFRACTION	10	C	114 - 264
11	X-RAY DIFFRACTION	11	C	265 - 394
12	X-RAY DIFFRACTION	12	C	395 - 481
13	X-RAY DIFFRACTION	13	D	1 - 58
14	X-RAY DIFFRACTION	14	D	59 - 264
15	X-RAY DIFFRACTION	15	D	265 - 394
16	X-RAY DIFFRACTION	16	D	395 - 481

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