PDB-7qtf: Crystal Structure of the Fe(II)/alpha-ketoglutarate dependent dio...

ID or keywords:

Entry

Database: PDB / ID: 7qtf

Title

Crystal Structure of the Fe(II)/alpha-ketoglutarate dependent dioxygenase PlaO1 in complex with sodium succinate

Components

PlaO1

Keywords

BIOSYNTHETIC PROTEIN / Dioxygenase / non-heme iron / Fe(II) / alpha-ketoglutarate / 2-oxoglutarate / terpene synthesis / Phenalinolactone

Function / homology

Function and homology information

taurine dioxygenase activity / sulfur compound metabolic process / metal ion binding / cytoplasm
Similarity search - Function

Biological species

Streptomyces sp. Tu6071 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.55 Å

Authors

Lukat, P. / Daum, M. / Bechthold, A. / Einsle, O.

Funding support

1items

Citation

Journal: Thesis / Year: 2011
Title: Structural investigations on the Fe(II)/alpha-ketoglutarate dependent dioxygense PlaO1 from Streptomyces sp. Tu6071
Authors: Lukat, P.

History

Deposition	Jan 14, 2022	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jan 18, 2023	Provider: repository / Type: Initial release
Revision 1.1	Aug 16, 2023	Group: Data collection / Database references Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / citation_author Item: _citation.journal_abbrev / _citation.journal_id_CSD / _citation.year
Revision 1.2	Jan 31, 2024	Group: Refinement description / Category: pdbx_initial_refinement_model

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	7qtf.cif.gz	682.1 KB	Display	PDBx/mmCIF format
PDB format	pdb7qtf.ent.gz	574.6 KB	Display	PDB format
PDBx/mmJSON format	7qtf.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	7qtf_validation.pdf.gz	1.8 MB	Display	wwPDB validaton report
Full document	7qtf_full_validation.pdf.gz	1.8 MB	Display
Data in XML	7qtf_validation.xml.gz	52.6 KB	Display
Data in CIF	7qtf_validation.cif.gz	78 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qt/7qtf ftp://data.pdbj.org/pub/pdb/validation_reports/qt/7qtf	HTTPS FTP

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Related structure data

Related structure data	7qtdC 7qteC 7qtgC 1gqwS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	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

Deposited unit

A: PlaO1

B: PlaO1

C: PlaO1

D: PlaO1

hetero molecules

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

1

Idetical with deposited unit
defined by author&software
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	63.894, 108.172, 115.033
Angle α, β, γ (deg.)	90.000, 93.870, 90.000
Int Tables number	4
Space group name H-M	P12₁1
Symmetry operation	#1: x,y,z #2: -x,y+1/2,-z

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Protein , 1 types, 4 molecules ABCD

#1: Protein	PlaO1 Mass: 33847.844 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: PlaO1 expressed with C-terminal TEV protease cleavage site and Strep-tag II after digestion with TEV protease Source: (gene. exp.) Streptomyces sp. Tu6071 (bacteria) / Gene: plaO1, STTU_1451 / Plasmid: pETTSC / Details (production host): modified pET21a(+) / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Star / References: UniProt: Q2I752

#1: Protein

PlaO1

Mass: 33847.844 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: PlaO1 expressed with C-terminal TEV protease cleavage site and Strep-tag II after digestion with TEV protease
Source: (gene. exp.)

Streptomyces sp. Tu6071 (bacteria) / Gene: plaO1, STTU_1451 / Plasmid: pETTSC / Details (production host): modified pET21a(+) / Production host:

Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Star / References: UniProt: Q2I752

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Non-polymers , 5 types, 1078 molecules

#2: Chemical	ChemComp-MLI / MALONATE ION Mass: 102.046 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₃H₂O₄
#3: Chemical	ChemComp-SIN / SUCCINIC ACID Mass: 118.088 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₄H₆O₄ / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical	ChemComp-ACT / ACETATE ION Mass: 59.044 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂H₃O₂
#5: Chemical	ChemComp-NA / SODIUM ION Mass: 22.990 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Na
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1067 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	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: 2.93 Å³/Da / Density % sol: 58.01 %
Crystal grow	Temperature: 310 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 36 % Tacsimate pH 7.0 soak: 15 min 375 mM Na succinate, 250 mM NaHCO3 Cryo: 100 % Tacsimate pH 7.0

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

SLS

/ Beamline: X06SA / Wavelength: 1 Å

Detector

Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Sep 17, 2010

Radiation

Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1 Å / Relative weight: 1

Reflection

Resolution: 1.55→78.72 Å / Num. obs: 226503 / % possible obs: 99.8 % / Redundancy: 3.8 % / B_iso Wilson estimate: 17.57 Å² / CC_1/2: 1 / R_merge(I) obs: 0.039 / R_pim(I) all: 0.024 / R_rim(I) all: 0.046 / Net I/σ(I): 19.4 / Num. measured all: 857403 / Scaling rejects: 8

Reflection shell

Diffraction-ID: 1 / Redundancy: 3.7 %

Resolution (Å)	R_merge(I) obs	Num. measured all	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Net I/σ(I) obs	% possible all
1.55-1.63	0.548	123600	33039	0.844	0.329	0.641	2.4	99.9
4.89-78.72	0.014	27291	7290	1	0.008	0.016	61.1	99.3

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
PHENIX	1.20-4459	refinement
autoPROC	1.0.5	data reduction
Aimless	0.7.4	data scaling
MOLREP		phasing
PDB_EXTRACT	3.27	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1gqw

1gqw

Resolution: 1.55→48.46 Å / SU ML: 0.15 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 17.14 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1729	11058	4.88 %
R_work	0.1505	215340	-
obs	0.1516	226398	99.76 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL

Displacement parameters

B_iso max: 116.29 Å² / B_iso mean: 27.7524 Å² / B_iso min: 10.65 Å²

Refinement step

Cycle: final / Resolution: 1.55→48.46 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8943	0	77	1067	10087
B_iso mean	-	-	35.89	33.59	-
Num. residues	-	-	-	-	1117

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 30

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.55-1.56	0.2489	374	0.2449	7161	7535	100
1.56-1.58	0.2552	398	0.2372	7078	7476	100
1.58-1.6	0.2483	353	0.2246	7208	7561	100
1.6-1.62	0.2456	364	0.2163	7159	7523	100
1.62-1.64	0.2278	401	0.2031	7191	7592	100
1.64-1.67	0.2151	393	0.1892	7094	7487	100
1.67-1.69	0.1987	360	0.1771	7182	7542	100
1.69-1.72	0.209	383	0.1741	7127	7510	100
1.72-1.74	0.1925	372	0.1716	7143	7515	100
1.74-1.77	0.2152	346	0.1666	7261	7607	100
1.77-1.8	0.1954	361	0.1703	7123	7484	100
1.8-1.83	0.1958	398	0.1633	7165	7563	100
1.83-1.87	0.1867	339	0.1652	7172	7511	100
1.87-1.91	0.2018	347	0.1626	7203	7550	100
1.91-1.95	0.1575	372	0.1428	7179	7551	100
1.95-1.99	0.1741	341	0.1414	7232	7573	100
1.99-2.04	0.1724	347	0.1405	7135	7482	100
2.04-2.1	0.1758	373	0.1371	7176	7549	100
2.1-2.16	0.143	370	0.1326	7154	7524	100
2.16-2.23	0.1482	359	0.1299	7170	7529	100
2.23-2.31	0.1646	375	0.1361	7202	7577	100
2.31-2.4	0.158	379	0.1375	7155	7534	100
2.4-2.51	0.1657	359	0.1385	7223	7582	100
2.51-2.64	0.1791	386	0.1476	7150	7536	100
2.64-2.81	0.1727	372	0.1524	7165	7537	100
2.81-3.03	0.1865	361	0.1597	7209	7570	100
3.03-3.33	0.1704	365	0.1479	7184	7549	100
3.33-3.81	0.1491	352	0.1335	7232	7584	100
3.81-4.8	0.134	391	0.1184	7233	7624	100
4.8-48.46	0.1931	367	0.1756	7274	7641	99

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	2.9578	0.2177	1.354	2.4009	0.1256	6.1908	-0.1055	0.3777	-0.0241	-0.361	-0.0754	-0.156	-0.0612	0.1841	0.2335	0.2347	0.0089	0.0151	0.2081	-0.004	0.1658	-0.1687	-11.1663	-6.4042
2	2.3352	-0.0606	1.071	1.5203	0.77	2.1807	0.0487	0.2206	0.086	-0.3636	-0.1673	0.0966	-0.0173	0.037	0.0895	0.2466	0.0343	-0.0218	0.1769	-0.0175	0.165	-9.9477	-18.2854	-10.1482
3	1.9083	-0.3205	0.8996	2.2134	0.2716	1.6914	0.0012	0.0332	0.0928	-0.2068	-0.176	0.5126	-0.096	-0.3115	0.1274	0.208	0.031	-0.0541	0.2264	-0.0642	0.2479	-19.0045	-11.6338	-6.203
4	1.1719	-0.4802	0.6725	0.2066	-0.1491	1.3151	0.0653	-0.0337	0.254	-0.0287	-0.2172	0.348	-0.1203	-0.2869	0.0587	0.1713	0.0446	-0.0392	0.2031	-0.0617	0.3082	-21.1748	-6.5933	4.7071
5	0.7566	0.2013	-0.01	0.7146	0.3272	0.8318	-0.0254	0.0359	0.0414	0.0063	-0.0313	0.0903	-0.0174	0.0081	0.0548	0.1292	-0.0037	0.0001	0.1276	-0.0168	0.1304	-5.1635	-11.3737	9.6875
6	4.5718	-3.8593	1.5036	6.6943	-2.2054	2.3031	-0.166	-0.0885	0.0541	0.1737	0.1418	0.788	-0.2391	-0.6587	0.0113	0.1581	0.0237	-0.0001	0.297	-0.0435	0.2645	-21.0564	-12.3188	20.4051
7	0.6514	-0.0931	-0.1207	0.8367	0.2188	1.4492	-0.0132	0.0121	-0.0095	-0.0077	-0.0756	0.1055	0.0321	-0.0834	0.084	0.1406	-0.0157	-0.0047	0.1465	-0.0043	0.1389	-7.9938	-13.5644	19.9868
8	0.9709	0.9401	0.109	1.2949	0.5012	0.907	-0.0433	0.0735	0.2632	-0.2024	-0.0564	0.2946	-0.1015	-0.098	0.0716	0.1631	0.0204	-0.04	0.1404	-0.005	0.1897	-10.0467	-3.6001	1.3937
9	0.8507	0.2716	0.1584	1.1995	-0.0923	2.2199	0.103	0.0065	0.0422	0.1206	-0.0115	0.3948	0.1788	-0.425	0.0013	0.2877	-0.0805	0.0814	0.2551	-0.0091	0.2783	-15.3508	-22.0588	26.2959
10	1.548	0.376	-0.1616	3.4956	-1.6149	3.455	-0.261	-0.0407	-0.1233	0.1524	0.1953	0.1501	0.1831	-0.4009	0.0133	0.2901	0.0034	0.0196	0.3096	-0.0445	0.3358	-14.0168	0.9635	30.8647
11	2.1948	0.6167	-0.5145	1.7393	-0.3603	1.5544	-0.0709	0.2518	0.0651	-0.539	0.0463	-0.1123	0.0505	0.0374	-0.0004	0.2592	0.0089	0.0192	0.1681	0.0151	0.1278	7.6604	14.7772	-8.2194
12	2.2884	-0.1207	-0.4513	2.1056	0.0755	1.1432	0.015	0.0899	-0.0023	-0.232	0.0182	-0.5197	0.031	0.2791	-0.0426	0.2159	0.023	0.0622	0.2404	0.0118	0.2757	21.5807	9.8199	-4.4163
13	1.7341	-0.3289	-0.8755	0.0937	0.2773	0.8658	0.0438	-0.03	-0.4103	0.0963	-0.0917	-0.395	0.2022	0.2822	0.0982	0.1916	0.0548	0.025	0.247	0.0024	0.3849	21.7224	1.4106	5.4358
14	0.5729	0.1825	-0.1025	0.7207	0.3497	1.2308	0.0017	-0.0103	-0.0334	-0.0238	0.006	-0.1232	0.0034	0.1371	-0.0148	0.1205	-0.0022	0.0028	0.1464	0.0165	0.1479	10.8589	13.1165	14.9718
15	1.2826	-0.5489	0.9379	0.9311	-0.3358	4.8773	0.0339	-0.0452	-0.0609	0.0387	-0.0602	-0.0424	0.1654	0.0626	0.006	0.1136	-0.0118	0.004	0.1228	0	0.1208	3.392	8.5996	24.3976
16	1.0634	1.0352	0.0042	1.5466	-0.0328	0.9963	0.0066	0.0683	-0.2847	-0.148	-0.0045	-0.3563	0.1466	0.1155	-0.0054	0.1632	0.0278	0.0152	0.1509	-0.0017	0.2041	11.7909	2.3884	2.9356
17	1.3059	0.3341	-0.3423	1.5462	0.2108	1.9808	0.1231	-0.1497	-0.0451	0.1957	0.0244	-0.2582	-0.1497	0.284	-0.1221	0.2295	-0.0474	-0.0448	0.2021	-0.0057	0.2164	13.0716	21.7283	27.4701
18	1.3531	-0.1599	0.0428	3.1915	1.2749	2.4232	-0.1298	-0.0845	-0.0545	0.1536	0.1325	-0.026	-0.1501	0.3234	0.0128	0.3094	-0.0112	0.0195	0.3397	0.0617	0.3149	11.7446	-1.3713	32.5038
19	1.7514	-0.272	0.5126	1.4094	-0.3642	1.566	-0.0817	-0.2845	-0.06	0.5553	0.0144	-0.0921	-0.1578	-0.005	0.0382	0.2784	-0.011	-0.0067	0.1809	0.0233	0.1323	3.0536	-14.7377	66.8357
20	2.1258	0.1259	0.556	2.3725	0.1401	1.5618	0.0209	-0.1438	0.0924	0.2355	-0.0664	-0.5632	-0.1059	0.3058	0.0502	0.2185	-0.047	-0.0726	0.2311	0.0521	0.2413	16.8065	-9.8988	64.4457
21	0.601	-0.1836	0.0991	0.7518	-0.1042	1.2694	-0.0151	-0.0434	0.109	0.0813	-0.057	-0.2309	-0.0765	0.1711	0.0486	0.1406	-0.013	-0.0169	0.1603	0.0321	0.1853	10.2824	-8.128	50.5247
22	2.5855	1.7773	0.1302	3.6743	0.494	1.489	-0.0708	0.0285	0.1341	-0.1121	0.004	-0.6148	-0.1594	0.6241	-0.0098	0.143	-0.035	-0.0004	0.303	0.0493	0.267	19.5355	-11.2766	37.4706
23	0.8887	-0.0112	-0.445	1.2922	-0.2311	2.3414	-0.0102	-0.0278	-0.0384	0.0113	-0.086	-0.0294	0.0609	0.1521	0.0933	0.1289	0.0227	-0.0037	0.1501	0.0174	0.1357	7.7958	-16.4765	40.9807
24	1.2905	0.0031	-1.2306	1.2568	0.006	4.3447	0.0444	0.0414	0.0337	-0.0799	-0.0723	-0.079	-0.144	0.0972	0.0201	0.1466	0.0101	-0.011	0.1405	0.0036	0.1337	2.5131	-8.4112	33.8174
25	1.1731	-1.0363	-0.041	1.601	-0.5853	1.105	-0.0258	-0.0671	0.2349	0.2045	-0.0496	-0.3443	-0.137	0.1466	0.056	0.179	-0.0276	-0.0293	0.1555	0.0132	0.1893	8.1713	-2.6325	55.8687
26	0.9211	-0.4064	0.2597	0.8301	-0.0955	2.8366	0.131	0.0648	0.0491	-0.1781	-0.0337	-0.3256	0.1768	0.3685	-0.0069	0.3108	0.0742	0.0786	0.2297	0.0124	0.2575	12.89	-21.6987	32.0435
27	1.6853	0.4755	0.4754	5.636	2.7934	4.0479	-0.2714	0.0973	-0.0589	-0.2991	0.2761	-0.1625	0.1145	0.5689	-0.0015	0.3174	-0.0031	-0.0035	0.333	0.0587	0.3118	12.4119	0.9903	26.1833
28	4.0417	-0.4149	-3.1642	2.4674	1.2408	7.8035	-0.2226	-0.4844	-0.0487	0.4639	-0.0116	-0.1252	0.1923	0.1426	0.255	0.2484	0.0046	-0.0208	0.2176	0.0044	0.1493	-4.9461	11.0114	63.5877
29	3.2739	0.389	-1.5036	1.2725	0.6817	2.2924	0.0782	-0.3269	-0.061	0.4656	-0.2045	0.158	0.157	0.0751	0.0899	0.2944	-0.0368	0.0433	0.1864	-0.0251	0.1586	-14.872	18.389	66.0752
30	2.5166	-0.0748	-0.7201	2.2809	-0.2085	1.732	0.0698	-0.1331	-0.0671	0.1807	-0.0381	0.4403	0.0125	-0.2446	-0.0414	0.2387	-0.0283	0.058	0.2151	-0.0234	0.23	-23.5335	11.4489	61.2087
31	1.484	0.4109	-0.7999	0.1077	-0.2213	1.5227	0.013	0.0438	-0.2883	0.027	-0.0877	0.2866	0.1783	-0.2531	0.0452	0.2003	-0.0421	0.0332	0.2262	-0.023	0.3108	-24.0367	5.9661	49.725
32	0.9168	-0.0833	-0.2166	1.1034	-0.3492	1.2092	-0.0115	-0.0613	-0.0685	0.0728	-0.0141	0.0807	0.0187	0.0022	0.025	0.1251	-0.001	0.0034	0.1203	-0.0139	0.1145	-7.6821	11.3342	46.9275
33	3.9468	2.8628	-1.2892	4.7998	-1.6933	2.0304	-0.1411	0.2202	-0.0714	-0.2029	0.1655	0.6151	0.2479	-0.4749	-0.0673	0.1496	-0.0266	0.0006	0.2576	-0.0274	0.2415	-22.0554	12.1229	34.4882
34	0.8716	0.0558	0.1267	1.182	-0.153	1.46	0.0113	-0.0035	0.0152	0.0811	-0.0218	0.0909	0.0292	-0.074	0.0084	0.1117	0.0192	0.0111	0.1304	-0.0069	0.1256	-11.6148	16.616	38.7429
35	1.3463	0.4175	0.8405	0.8627	0.4142	3.6839	0.002	-0.0393	-0.0416	-0.0293	-0.0929	0.1001	0.155	-0.1355	0.0758	0.1449	0.0075	0.0093	0.1501	0.0078	0.1471	-5.493	8.4504	33.0554
36	1.1743	-1.1952	-0.0174	1.3252	0.1247	1.0373	-0.0239	-0.1007	-0.3166	0.1678	-0.0095	0.3107	0.1546	-0.0789	0.0121	0.1909	-0.0268	0.0355	0.1492	0.0065	0.1973	-13.8103	3.3729	54.7159
37	1.2416	-0.3745	-0.1314	1.9907	-0.275	2.3531	0.1271	0.0377	-0.0252	-0.1615	-0.0651	0.2884	-0.2189	-0.4333	-0.0348	0.2099	0.0465	-0.0479	0.2434	-0.0008	0.2585	-15.5817	22.0104	29.3011
38	1.4876	-0.0176	0.0449	2.9689	-1.2151	2.7544	-0.14	0.0545	0.0298	-0.2064	0.0757	0.0261	-0.1233	-0.3209	0.049	0.2841	0.0082	0.0137	0.2958	-0.0451	0.3189	-13.9903	-1.5325	25.0542

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 9 through 23 )	A	9 - 23
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 24 through 45 )	A	24 - 45
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 46 through 78 )	A	46 - 78
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 79 through 112 )	A	79 - 112
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 113 through 150 )	A	113 - 150
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 151 through 169 )	A	151 - 169
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 170 through 212 )	A	170 - 212
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 213 through 254 )	A	213 - 254
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 255 through 274 )	A	255 - 274
10	X-RAY DIFFRACTION	10	chain 'A' and (resid 275 through 288 )	A	275 - 288
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 3 through 45 )	B	3 - 45
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 46 through 80 )	B	46 - 80
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 81 through 102 )	B	81 - 102
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 103 through 196 )	B	103 - 196
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 197 through 212 )	B	197 - 212
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 213 through 254 )	B	213 - 254
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 255 through 274 )	B	255 - 274
18	X-RAY DIFFRACTION	18	chain 'B' and (resid 275 through 288 )	B	275 - 288
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 4 through 45 )	C	4 - 45
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 46 through 79 )	C	46 - 79
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 80 through 150 )	C	80 - 150
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 151 through 169 )	C	151 - 169
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 170 through 196 )	C	170 - 196
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 197 through 212 )	C	197 - 212
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 213 through 254 )	C	213 - 254
26	X-RAY DIFFRACTION	26	chain 'C' and (resid 255 through 274 )	C	255 - 274
27	X-RAY DIFFRACTION	27	chain 'C' and (resid 275 through 288 )	C	275 - 288
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 9 through 23 )	D	9 - 23
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 24 through 45 )	D	24 - 45
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 46 through 78 )	D	46 - 78
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 79 through 112 )	D	79 - 112
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 113 through 150 )	D	113 - 150
33	X-RAY DIFFRACTION	33	chain 'D' and (resid 151 through 169 )	D	151 - 169
34	X-RAY DIFFRACTION	34	chain 'D' and (resid 170 through 196 )	D	170 - 196
35	X-RAY DIFFRACTION	35	chain 'D' and (resid 197 through 212 )	D	197 - 212
36	X-RAY DIFFRACTION	36	chain 'D' and (resid 213 through 254 )	D	213 - 254
37	X-RAY DIFFRACTION	37	chain 'D' and (resid 255 through 274 )	D	255 - 274
38	X-RAY DIFFRACTION	38	chain 'D' and (resid 275 through 288 )	D	275 - 288

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