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

ID or keywords:

Entry

Database: PDB / ID: 7qtd

Title

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

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: 1.75 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	7qtd.cif.gz	693.4 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	7qtd_validation.pdf.gz	2.5 MB	Display	wwPDB validaton report
Full document	7qtd_full_validation.pdf.gz	2.5 MB	Display
Data in XML	7qtd_validation.xml.gz	52.6 KB	Display
Data in CIF	7qtd_validation.cif.gz	77.7 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qt/7qtd ftp://data.pdbj.org/pub/pdb/validation_reports/qt/7qtd	HTTPS FTP

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Related structure data

Related structure data	7qteC 7qtfC 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
Related items in Molecule of the Month	#240 - Dec 2019 Hypoxia-Inducible Factors similarity (2) #111 - Mar 2009 Hydrogenase similarity (1) #244 - Apr 2020 Photosynthetic Supercomplexes similarity (1) #129 - Sep 2010 Isocitrate Dehydrogenase similarity (1) #147 - Mar 2012 Rhodopsin similarity (1) #61 - Jan 2005 Phenylalanine Hydroxylase similarity (1)

Deposited unit

A: PlaO1

B: PlaO1

C: PlaO1

D: PlaO1

hetero molecules

137 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)	64.124, 108.215, 116.408
Angle α, β, γ (deg.)	90.000, 94.750, 90.000
Int Tables number	4
Space group name H-M	P12₁1

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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 cleavage site 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) / 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 cleavage site 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) / References: UniProt: Q2I752

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Non-polymers , 6 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-FE2 / FE (II) ION Mass: 55.845 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical	ChemComp-AKG / 2-OXOGLUTARIC ACID Mass: 146.098 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₅H₆O₅
#5: Chemical	ChemComp-ACT / ACETATE ION Mass: 59.044 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₂H₃O₂
#6: Chemical	ChemComp-NA / SODIUM ION Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1060 / 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: 2.97 Å³/Da / Density % sol: 58.63 %
Crystal grow	Temperature: 310 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 34% 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: X06DA / Wavelength: 1 Å

Detector

Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Dec 10, 2009

Radiation

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

Radiation wavelength

Wavelength: 1 Å / Relative weight: 1

Reflection

Resolution: 1.75→108.21 Å / Num. obs: 160147 / % possible obs: 99.9 % / Redundancy: 3.8 % / B_iso Wilson estimate: 18.79 Å² / CC_1/2: 0.998 / R_merge(I) obs: 0.067 / R_pim(I) all: 0.04 / R_rim(I) all: 0.078 / Net I/σ(I): 13.5 / Num. measured all: 606869 / Scaling rejects: 2

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	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
1.75-1.84	3.8	0.557	87796	23289	0.797	0.335	0.651	2.4	100
5.52-108.21	3.7	0.027	19228	5188	0.999	0.017	0.032	36.9	99.7

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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	0.5.17	data scaling
MOLREP		phasing
PDB_EXTRACT	3.27	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1GQW

1gqw

Resolution: 1.75→63.9 Å / SU ML: 0.15 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 16.33 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1646	7714	4.82 %
R_work	0.1406	152340	-
obs	0.1417	160054	99.88 %

Solvent computation

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

Displacement parameters

B_iso max: 119.27 Å² / B_iso mean: 29.4928 Å² / B_iso min: 9.77 Å²

Refinement step

Cycle: final / Resolution: 1.75→63.9 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9004	0	122	1060	10186
B_iso mean	-	-	42.58	34.87	-
Num. residues	-	-	-	-	1121

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 (%)
1.75-1.77	0.2483	253	0.239	5097	5350	100
1.77-1.79	0.269	218	0.23	5059	5277	100
1.79-1.81	0.2239	243	0.2168	5062	5305	100
1.81-1.83	0.2276	310	0.2035	5049	5359	100
1.83-1.86	0.2338	259	0.1882	4994	5253	100
1.86-1.88	0.2409	241	0.1885	5136	5377	100
1.88-1.91	0.2019	236	0.1772	5077	5313	100
1.91-1.94	0.2035	268	0.17	5078	5346	100
1.94-1.97	0.2064	264	0.1661	5033	5297	100
1.97-2	0.1957	214	0.1653	5134	5348	100
2-2.03	0.1996	263	0.1628	4989	5252	100
2.03-2.07	0.1743	252	0.1414	5128	5380	100
2.07-2.11	0.1677	256	0.1365	5031	5287	100
2.11-2.15	0.1536	247	0.1249	5104	5351	100
2.15-2.2	0.1662	271	0.1222	5051	5322	100
2.2-2.25	0.1456	259	0.1259	5084	5343	100
2.25-2.31	0.1712	269	0.1291	5070	5339	100
2.31-2.37	0.1688	264	0.1308	5086	5350	100
2.37-2.44	0.1486	256	0.1269	5027	5283	100
2.44-2.52	0.1816	255	0.128	5106	5361	100
2.52-2.61	0.187	266	0.1368	5054	5320	100
2.61-2.71	0.1593	283	0.141	5057	5340	100
2.71-2.84	0.1731	251	0.1396	5108	5359	100
2.84-2.99	0.1557	253	0.1337	5088	5341	100
2.99-3.17	0.163	246	0.136	5103	5349	100
3.17-3.42	0.1463	270	0.1276	5089	5359	100
3.42-3.76	0.1285	236	0.123	5116	5352	100
3.76-4.31	0.1212	297	0.1083	5078	5375	100
4.31-5.42	0.1213	246	0.113	5101	5347	100
5.42-63.9	0.196	268	0.1795	5151	5419	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	2.956	0.3109	2.6582	2.664	2.2235	6.9748	-0.2046	0.3384	-0.0707	-0.4386	0.0935	-0.1734	-0.3097	0.2698	0.0366	0.2209	-0.0101	0.0381	0.1924	-0.0192	0.1604	0.1666	-11.2162	-5.9701
2	1.629	-0.142	0.403	2.5464	0.3208	2.0785	-0.0025	0.1635	0.0415	-0.2714	-0.1208	0.3039	-0.122	-0.2112	0.0851	0.2111	0.037	-0.0435	0.1893	-0.0403	0.1621	-14.9455	-14.3332	-7.7747
3	0.9414	-0.1069	0.3506	0.6122	-0.0344	1.4391	0.0072	0.0023	0.0597	-0.011	-0.063	0.1963	-0.091	-0.2301	0.0587	0.1399	0.0171	-0.0161	0.1604	-0.0439	0.1957	-14.9165	-9.0612	9.6538
4	0.7611	-0.3922	-0.1799	0.6334	0.2333	1.6297	0.0343	0.0596	-0.0524	-0.0538	-0.1133	0.0843	0.1004	-0.203	0.0636	0.1435	-0.0347	-0.006	0.1406	-0.0201	0.1626	-10.3534	-17.0326	17.3503
5	1.4488	-0.9449	-1.2435	0.8064	0.7978	3.9297	0.0146	0.0617	0.0015	0.0424	-0.0559	0.0161	-0.0444	-0.0751	0.0072	0.1371	-0.0207	-0.0061	0.1296	-0.0007	0.1448	-5.4043	-8.6619	24.4812
6	1.1052	1.1857	0.235	1.4175	0.6223	0.7176	-0.038	0.0972	0.2936	-0.2021	-0.0647	0.2879	-0.1618	-0.0525	0.0731	0.1832	0.0311	-0.0405	0.1607	-0.0119	0.2152	-10.2957	-3.7749	1.7617
7	0.7466	0.4979	0.4172	0.8862	0.0148	2.5634	0.1479	-0.032	-0.0334	0.217	-0.0147	0.4246	0.1087	-0.5307	-0.012	0.3026	-0.074	0.0882	0.2457	0.0071	0.3354	-15.6759	-21.8147	26.4546
8	1.7602	-0.923	0.8326	5.93	-2.4269	3.5736	-0.2679	0.1593	-0.0774	0.3263	0.1877	0.0514	0.0472	-0.4136	0.0287	0.1937	-0.0022	0.0064	0.2812	-0.0542	0.2552	-15.2323	1.2174	31.1825
9	2.5376	0.776	-0.537	1.8431	-0.6064	2.2199	-0.0692	0.3648	0.1726	-0.5725	0.032	-0.0951	-0.0105	-0.0586	0.0354	0.313	0.0257	0.0207	0.2045	0.0259	0.1724	8.1425	14.8556	-8.0437
10	2.4622	-0.1707	-0.2986	2.0703	0.2362	1.0355	0.0638	0.296	-0.0048	-0.2547	0.0116	-0.4964	0.0686	0.405	-0.0715	0.2379	0.0323	0.0761	0.3015	0.0019	0.288	21.5171	10.0246	-3.5532
11	2.8544	-0.5361	-1.6972	0.0959	0.3297	1.3365	-0.0166	0.0393	-0.4858	0.018	-0.0668	-0.3571	0.1596	0.2923	0.0775	0.1938	0.042	0.0271	0.2828	-0.0167	0.3925	22.7376	1.814	5.4386
12	0.8624	0.2338	-0.0156	0.9049	0.3978	1.4824	0.0261	0.0185	-0.0446	-0.0294	-0.0062	-0.1667	-0.0126	0.1612	-0.0262	0.1104	-0.0006	-0.0029	0.1269	0.0216	0.1408	10.6383	13.0368	15.3568
13	1.3245	-0.752	0.9869	0.7529	-0.7011	5.0646	0.0234	-0.028	-0.1078	0.0589	0.0012	-0.0013	-0.0231	0.0965	-0.0735	0.1262	-0.0095	-0.001	0.1266	0.0026	0.1358	2.9723	8.7515	24.6646
14	2.3817	0.7411	-0.3366	1.8985	-0.5531	0.6151	0.0075	0.1296	-0.279	-0.2747	-0.0756	-0.2203	0.0969	0.0328	0.0495	0.1758	0.0214	0.0202	0.1536	-0.0111	0.1582	7.224	4.0637	1.1822
15	1.6176	0.7449	-0.1631	0.6546	-0.2923	1.1167	0.0122	0.0954	-0.3469	-0.054	0.0446	-0.4245	0.1292	0.1497	-0.1164	0.1202	0.0186	0.0005	0.1543	0.0103	0.2427	14.8822	8.2606	8.819
16	0.6965	-0.5503	-0.2931	2.5899	-0.4135	0.8477	-0.0931	-0.1815	-0.0649	0.6246	-0.0144	-0.1597	-0.0143	0.2599	0.0383	0.2182	-0.0193	-0.0602	0.2643	0.0318	0.1964	11.9511	6.0968	34.9973
17	2.0215	-0.3237	-0.3074	2.5888	-2.4716	3.5839	-0.1621	-0.3447	-0.23	0.5393	0.061	0.3248	0.3167	-0.2097	0.052	0.3479	-0.0132	0.0705	0.2566	0.0154	0.1933	-3.9455	-13.7689	64.3691
18	2.0865	0.094	-0.0983	2.1516	0.3016	1.9292	0.0419	-0.3777	-0.0145	0.4126	-0.0655	-0.3807	-0.0587	0.329	-0.0028	0.2877	-0.0319	-0.0718	0.2669	0.0365	0.1848	11.0912	-11.8931	66.8885
19	0.6856	-0.13	-0.0846	0.7401	0.1276	1.3719	0.0107	-0.0704	0.0764	0.0683	-0.0366	-0.1664	-0.0181	0.1985	0.0054	0.1384	-0.0053	-0.0157	0.1528	0.0252	0.1666	10.4245	-10.1821	46.9398
20	1.8216	0.7113	-1.9201	0.5572	-0.3065	4.8307	-0.0141	-0.0192	0.0441	-0.0384	-0.0193	-0.0108	0.0379	0.0952	-0.0288	0.1433	0.0068	-0.0062	0.1214	0.0012	0.1338	2.2003	-8.6185	34.1089
21	1.3976	-1.2371	-0.1074	1.7208	-0.624	0.9141	-0.0066	-0.1125	0.2812	0.2183	-0.0416	-0.3357	-0.161	0.0487	0.0343	0.2034	-0.0272	-0.0312	0.1649	0.0041	0.1883	5.3146	-2.236	55.4719
22	0.4506	0.3646	0.4711	1.6805	-0.0889	1.2043	-0.0281	0.055	0.0558	-0.2779	-0.0548	-0.1793	0.1488	0.2228	0.0788	0.1274	0.0448	0.0466	0.2263	0.0226	0.2388	12.9889	-10.1101	34.8261
23	4.2743	-0.1493	-2.5102	2.4022	0.8462	6.3689	-0.1672	-0.5927	0.1563	0.5357	0.1025	-0.1701	0.0415	0.3167	0.0146	0.2758	0.0261	-0.027	0.2316	-0.0238	0.1335	-6.2557	11.614	64.449
24	3.2551	-0.3212	-1.2477	1.5893	1.0877	2.6988	0.067	-0.269	-0.0973	0.3764	-0.2324	0.1774	0.1006	-0.074	0.0528	0.2774	-0.0342	0.0372	0.1977	-0.0423	0.1644	-16.0816	18.6956	66.2456
25	2.7349	0.0274	-0.7213	2.3392	0.2655	1.8117	0.0083	-0.1099	-0.1223	0.0736	-0.1172	0.4377	0.2008	-0.3683	0.0933	0.2304	-0.0526	0.0606	0.2465	-0.0509	0.2356	-24.7114	11.6091	61.1526
26	1.8623	0.239	-0.8999	0.0199	-0.1397	1.5251	0.0216	0.02	-0.2677	0.018	-0.1008	0.2287	0.1405	-0.2466	0.0362	0.1885	-0.0392	0.0259	0.2219	-0.0431	0.276	-24.514	7.1038	49.2479
27	2.0238	-0.7312	-1.0029	0.3858	0.5543	0.7887	-0.1831	-0.4675	-0.7052	0.229	0.1637	0.7066	0.1927	0.0186	0.0593	0.2509	-0.0416	0.0675	0.2651	0.0585	0.3569	-18.1659	-0.1264	59.3718
28	0.7309	-0.2622	-0.054	1.0299	-0.4098	1.9083	0.0329	0.0112	0.0335	0.0071	-0.0376	0.1534	-0.0503	-0.1434	0.0209	0.1186	0.0132	0.0079	0.1287	-0.0222	0.1402	-11.8885	15.8834	38.6036
29	1.3593	0.3599	1.0791	1.0145	0.3385	5.7545	0.0709	-0.0151	-0.1166	-0.0419	-0.0251	0.0402	0.0498	-0.0319	-0.0077	0.1272	0.0107	0.0067	0.1293	0.0002	0.1472	-6.1723	8.9682	32.9164
30	1.3257	-1.3348	-0.2357	1.2921	0.1171	1.071	-0.0567	-0.0855	-0.3819	0.1895	-0.0061	0.387	0.2062	-0.1001	0.0161	0.1921	-0.0395	0.0392	0.1672	-0.0131	0.2357	-14.9684	4.2668	54.557
31	1.1283	-0.568	-0.5743	1.4859	-0.1575	1.5601	0.173	0.1658	0.0592	-0.2631	-0.0318	0.2634	-0.1073	-0.4336	0.0523	0.2327	0.0499	-0.0586	0.2337	0.0098	0.2445	-15.9588	21.6207	29.1195
32	1.8933	1.7763	-1.638	6.1337	-2.648	3.3912	-0.2139	0.1127	-0.0929	-0.19	0.1526	-0.0063	-0.1373	-0.4258	0.003	0.1996	-0.0085	0.0028	0.2577	-0.0472	0.2191	-14.7808	-1.3671	24.7029

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 77 )	A	24 - 77
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 78 through 169 )	A	78 - 169
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 170 through 196 )	A	170 - 196
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 197 through 212 )	A	197 - 212
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 213 through 254 )	A	213 - 254
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 255 through 274 )	A	255 - 274
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 275 through 288 )	A	275 - 288
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 3 through 45 )	B	3 - 45
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 46 through 78 )	B	46 - 78
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 79 through 102 )	B	79 - 102
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 103 through 196 )	B	103 - 196
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 197 through 212 )	B	197 - 212
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 213 through 231 )	B	213 - 231
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 232 through 265 )	B	232 - 265
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 266 through 288 )	B	266 - 288
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 3 through 19 )	C	3 - 19
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 20 through 79 )	C	20 - 79
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 80 through 196 )	C	80 - 196
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 197 through 212 )	C	197 - 212
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 213 through 247 )	C	213 - 247
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 248 through 288 )	C	248 - 288
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 8 through 23 )	D	8 - 23
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 24 through 45 )	D	24 - 45
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 46 through 79 )	D	46 - 79
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 80 through 112 )	D	80 - 112
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 113 through 127 )	D	113 - 127
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 128 through 196 )	D	128 - 196
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 197 through 212 )	D	197 - 212
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 213 through 254 )	D	213 - 254
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 255 through 274 )	D	255 - 274
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 275 through 288 )	D	275 - 288

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