PDB-6mjn: Crystal structure of an organic hydroperoxide resistance protein ...

ID or keywords:

Entry

Database: PDB / ID: 6mjn

Title

Crystal structure of an organic hydroperoxide resistance protein OsmC, predicted redox protein, regulator of sulfide bond formation from Legionella pneumophila

Components

Organic hydroperoxide resistance protein

Keywords

OXIDOREDUCTASE / NIAID / structural genomics / disulfide / active site cysteine / redox / Seattle Structural Genomics Center for Infectious Disease / SSGCID

Function / homology

Function and homology information

response to oxidative stress
Similarity search - Function

Biological species

Legionella pneumophila (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.75 Å

Authors

Seattle Structural Genomics Center for Infectious Disease / Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Citation

Journal: To Be Published
Title: Crystal structure of an organic hydroperoxide resistance protein OsmC, predicted redox protein, regulator of sulfide bond formation from Legionella pneumophila
Authors: Edwards, T.E. / Delker, S.L. / Horanyi, P.S. / Lorimer, D.D. / Seattle Structural Genomics Center for Infectious Disease

History

Deposition	Sep 21, 2018	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Oct 3, 2018	Provider: repository / Type: Initial release
Revision 1.1	Oct 11, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	6mjn.cif.gz	224.3 KB	Display	PDBx/mmCIF format
PDB format	pdb6mjn.ent.gz	179.4 KB	Display	PDB format
PDBx/mmJSON format	6mjn.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	6mjn_validation.pdf.gz	455 KB	Display	wwPDB validaton report
Full document	6mjn_full_validation.pdf.gz	459.3 KB	Display
Data in XML	6mjn_validation.xml.gz	22.9 KB	Display
Data in CIF	6mjn_validation.cif.gz	32.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/mj/6mjn ftp://data.pdbj.org/pub/pdb/validation_reports/mj/6mjn	HTTPS FTP

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Related structure data

Related structure data	3eerS S: Starting model for refinement
Similar structure data	3jtc-1 2dda-3 2hdc-d 2ddb-3 2ddb-4 2ddb-1 4ese-d 3mz8-1 2epf-3 3zqc-3 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	TargetTrack: LepnA.00074.a

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Organic hydroperoxide resistance protein

B: Organic hydroperoxide resistance protein

C: Organic hydroperoxide resistance protein

D: Organic hydroperoxide resistance protein

hetero molecules

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

1

A: Organic hydroperoxide resistance protein

B: Organic hydroperoxide resistance protein

hetero molecules

defined by author&software
31.6 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Organic hydroperoxide resistance protein

D: Organic hydroperoxide resistance protein

hetero molecules

defined by author&software
31.5 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	76.550, 51.400, 82.340
Angle α, β, γ (deg.)	90.000, 110.090, 90.000
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Organic hydroperoxide resistance protein Mass: 15752.879 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Legionella pneumophila (bacteria) / Gene: C3927_09130 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A2S6F4M7, UniProt: Q5ZU37*PLUS
#2: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 201 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.41 Å³/Da / Density % sol: 49.06 %
Crystal grow	Temperature: 287 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: LepnA.00074.a.B1.PS38428 at 20.78 mg/mL against MCSG1 screen condition C4: 0.17 M ammonium acetate, 0.085 M sodium acetate pH 4.6, 25.5% PEG 4000, 15% ethylene glycol, crystal tracking ID ...Details: LepnA.00074.a.B1.PS38428 at 20.78 mg/mL against MCSG1 screen condition C4: 0.17 M ammonium acetate, 0.085 M sodium acetate pH 4.6, 25.5% PEG 4000, 15% ethylene glycol, crystal tracking ID 300656c4, unique puck ID zem2-15

Crystal

Density Matthews: 2.41 Å³/Da / Density % sol: 49.06 %

Crystal grow

Temperature: 287 K / Method: vapor diffusion, sitting drop / pH: 4.6
Details: LepnA.00074.a.B1.PS38428 at 20.78 mg/mL against MCSG1 screen condition C4: 0.17 M ammonium acetate, 0.085 M sodium acetate pH 4.6, 25.5% PEG 4000, 15% ethylene glycol, crystal tracking ID ...

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

ALS

/ Beamline: 5.0.2 / Wavelength: 0.99999 Å

Detector

Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Sep 2, 2018

Radiation

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

Radiation wavelength

Wavelength: 0.99999 Å / Relative weight: 1

Reflection

Resolution: 1.75→42.806 Å / Num. obs: 59868 / % possible obs: 98.1 % / Redundancy: 3.3 % / B_iso Wilson estimate: 43.206 Å² / CC_1/2: 0.999 / R_merge(I) obs: 0.034 / R_rim(I) all: 0.04 / Χ²: 1.069 / Net I/σ(I): 15.56

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Mean I/σ(I) obs	Num. unique obs	CC_1/2	R_rim(I) all	% possible all
1.75-1.8	3.449	0.435	2.54	4472	0.924	0.517	99.7
1.8-1.84	3.416	0.322	3.36	4359	0.949	0.384	99.9
1.84-1.9	3.368	0.239	4.5	4248	0.972	0.285	99.9
1.9-1.96	3.237	0.159	6.33	4103	0.986	0.191	99.7
1.96-2.02	3.274	0.122	8.04	4027	0.99	0.147	99.8
2.02-2.09	3.486	0.096	10.39	3830	0.993	0.114	99.7
2.09-2.17	3.42	0.08	12.47	3747	0.995	0.096	99.4
2.17-2.26	3.343	0.066	14.79	3565	0.995	0.079	99
2.26-2.36	3.159	0.056	16.64	3418	0.996	0.067	98.8
2.36-2.47	3.227	0.05	18.91	3255	0.997	0.06	98.5
2.47-2.61	3.381	0.044	21.85	3063	0.997	0.053	97.2
2.61-2.77	3.296	0.04	23.94	2871	0.997	0.048	96.4
2.77-2.96	3.143	0.037	25.7	2708	0.997	0.045	96
2.96-3.2	3.031	0.036	26.93	2518	0.997	0.043	95.8
3.2-3.5	3.315	0.032	30.24	2269	0.998	0.038	94.1
3.5-3.91	3.28	0.031	30.9	2035	0.998	0.036	92.8
3.91-4.52	3.028	0.03	30.02	1852	0.998	0.036	96
4.52-5.53	3.24	0.028	31.32	1590	0.998	0.033	95.5
5.53-7.83	3.227	0.026	31.28	1227	0.999	0.031	94.8
7.83-42.806	3.114	0.024	30.96	711	0.998	0.029	95.6

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
XDS		data reduction
XSCALE		data scaling
MOLREP		phasing
PHENIX		refinement
PDB_EXTRACT	3.24	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 3EER

3eer

Resolution: 1.75→42.806 Å / SU ML: 0.21 / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 24.78

	R_factor	Num. reflection	% reflection
R_free	0.2093	3432	6.06 %
R_work	0.1812	-	-
obs	0.183	56617	92.85 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å

Displacement parameters

B_iso max: 148.83 Å² / B_iso mean: 53.5157 Å² / B_iso min: 20.4 Å²

Refinement step

Cycle: final / Resolution: 1.75→42.806 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	3900	0	3	203	4106
B_iso mean	-	-	64.68	51.6	-
Num. residues	-	-	-	-	554

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 25

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.75-1.774	0.3591	115	0.3445	1850	1965	80
1.774-1.7993	0.3709	104	0.3206	1832	1936	82
1.7993-1.8262	0.3464	121	0.2914	1936	2057	84
1.8262-1.8547	0.3251	114	0.281	1917	2031	85
1.8547-1.8851	0.3036	122	0.2677	1955	2077	85
1.8851-1.9176	0.2841	124	0.2435	2002	2126	88
1.9176-1.9525	0.2865	154	0.2447	2051	2205	91
1.9525-1.99	0.2579	142	0.2291	2109	2251	92
1.99-2.0307	0.2398	130	0.2173	2175	2305	95
2.0307-2.0748	0.2059	149	0.2244	2162	2311	96
2.0748-2.1231	0.2702	126	0.2074	2233	2359	97
2.1231-2.1762	0.2365	143	0.2044	2204	2347	97
2.1762-2.235	0.2282	129	0.1954	2246	2375	97
2.235-2.3008	0.2149	125	0.1907	2229	2354	97
2.3008-2.375	0.2193	134	0.1922	2225	2359	97
2.375-2.4599	0.2481	166	0.1968	2230	2396	97
2.4599-2.5584	0.2086	150	0.1966	2213	2363	97
2.5584-2.6748	0.222	159	0.1896	2158	2317	96
2.6748-2.8158	0.2286	148	0.1857	2189	2337	96
2.8158-2.9922	0.249	167	0.1938	2197	2364	96
2.9922-3.2231	0.2092	150	0.1838	2199	2349	96
3.2231-3.5473	0.1864	139	0.1653	2151	2290	94
3.5473-4.0603	0.1716	139	0.1517	2175	2314	94
4.0603-5.1142	0.1526	142	0.1418	2262	2404	96
5.1142-42.8191	0.2098	140	0.1738	2285	2425	95

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	5.4625	0.2081	0.8446	4.0592	0.771	7.0398	0.0104	0.0376	0.2377	-0.1733	-0.0223	0.6566	-0.0165	-0.7402	0.0428	0.2327	-0.0011	-0.02	0.2825	-0.049	0.3885	-4.6312	1.1129	28.3912
2	7.2036	0.8208	-1.03	3.7813	-0.2343	6.2559	-0.2629	1.1751	0.0534	-0.7435	0.0881	0.3266	-0.3349	-0.0703	0.0328	0.4161	0.0387	-0.1033	0.4329	0.1208	0.3647	3.713	9.7854	16.1301
3	4.837	0.8138	3.7478	1.1403	0.7736	6.7746	0.2979	-0.5062	0.3228	0.1251	-0.0941	0.1161	0.149	-0.4695	-0.0081	0.2951	-0.0118	0.0336	0.2214	-0.0323	0.3071	12.0871	5.7999	37.3641
4	4.4329	-0.5149	-0.4419	4.1507	0.5545	8.2689	0.1797	0.038	0.0376	0.001	-0.188	-0.0795	0.1497	-0.2099	0.027	0.2165	-0.0383	0.0091	0.1851	0.0053	0.3272	17.6695	6.3881	32.3027
5	5.2364	0.6056	3.595	3.5072	2.7291	7.7389	-0.1538	0.1992	0.4149	-0.369	-0.2315	0.2614	-0.5762	-0.0766	0.5677	0.2356	-0.0339	0.0434	0.1776	0.0153	0.298	20.3718	8.2096	33.3843
6	5.0375	1.4151	1.5056	0.4736	-0.225	5.5559	0.2971	-0.0078	-0.4681	0.3655	0.0218	-0.3795	0.4864	0.1706	-0.2634	0.321	0.0639	-0.0097	0.2299	-0.0298	0.3343	24.2256	4.4952	43.1144
7	6.2337	4.3232	2.5149	2.8946	2.4064	3.6101	0.2327	0.0953	-0.2082	0.2512	-0.0384	-0.3176	0.2125	0.1618	-0.1902	0.2872	0.04	-0.0235	0.1353	-0.0172	0.2898	18.8831	0.8323	34.3469
8	5.797	-2.171	-1.4284	2.563	1.1751	8.0987	0.144	0.2101	0.5287	-0.1959	-0.0733	-0.1225	-0.235	0.118	-0.211	0.2753	-0.0401	-0.0195	0.2023	0.0507	0.3447	14.0589	10.1902	27.258
9	5.1125	0.8589	-1.0476	4.5874	-5.5761	8.0573	0.1966	0.1535	0.9789	-0.3156	0.1827	0.5466	-0.9878	-0.2464	-0.3826	0.4	0.0369	-0.0255	0.1986	0.0117	0.4665	7.1649	15.6385	28.0906
10	7.2797	2.0346	-0.4686	7.5203	-3.6581	8.1281	0.2554	-0.9674	0.7393	0.8329	-0.2389	0.7609	-0.4991	-0.6374	-0.1658	0.3249	0.0449	0.106	0.3655	-0.0911	0.4161	-0.801	7.9223	40.2851
11	3.4512	0.5709	0.3306	6.8283	5.5039	3.9591	-0.0646	0.5568	0.2214	-0.4715	0.1869	0.0603	-0.3811	-0.1601	-0.1224	0.2547	-0.0454	-0.0059	0.3203	0.0327	0.2722	2.5535	-3.0656	20.794
12	1.9134	0.954	-4.0467	3.6258	-1.2034	8.7981	-0.0573	3.8659	-1.3052	-1.7524	-0.0297	0.6892	-0.1496	-0.6982	0.6185	0.5764	-0.1576	-0.0373	0.8578	-0.2488	0.47	-4.1452	-10.3103	6.6221
13	6.8369	1.8189	2.7638	4.3296	2.6372	7.3471	-0.1386	-0.2243	-0.2623	0.2284	0.1533	-0.0104	0.1227	0.1984	0.0383	0.2661	-0.016	0.0258	0.2143	0.0144	0.3108	2.5644	-6.8221	33.7792
14	7.4597	2.3854	4.4971	3.9099	3.7737	4.1855	-0.1412	-0.6516	0.2822	-0.2214	-0.3761	0.3518	-0.1801	-1.363	0.4846	0.2077	-0.0211	-0.0217	0.2288	0.0038	0.267	-2.3686	-9.9163	24.5181
15	5.8856	4.1032	5.7531	9.2723	6.1922	6.3942	0.0442	0.4078	-1.2014	-0.1106	0.4596	-0.8594	0.3546	0.7572	-0.5245	0.3461	0.0325	-0.0213	0.3537	-0.003	0.3125	0.577	-15.9335	15.905
16	4.5369	-4.9119	3.2538	5.8689	-2.3789	8.4492	0.059	0.2158	-0.5041	-0.4053	0.4163	0.0359	0.6529	-0.1483	-0.4968	0.2746	-0.039	-0.0087	0.2788	-0.0116	0.3131	10.9143	-8.7969	25.3749
17	4.6809	5.9595	4.3985	7.8872	6.1006	4.8483	-0.3213	0.439	-0.1773	-0.2003	0.1697	0.0955	-0.1917	-0.2867	0.2494	0.4074	-0.0652	-0.0201	0.4308	-0.009	0.3945	-4.6646	-13.912	21.9922
18	6.4937	1.6504	4.4771	4.2306	1.7171	3.235	-0.422	0.7128	-1.3881	0.9197	0.5948	-0.3656	0.9902	0.3421	0.3044	0.5944	-0.0436	0.3066	0.8621	-0.3895	0.2515	24.6493	-6.7427	-22.2333
19	4.8919	3.7495	1.01	5.7714	4.3873	4.7296	0.5408	-1.0309	-1.0999	1.2012	-0.9227	-1.2686	-0.9208	-0.1031	-0.4009	1.2554	0.2886	0.0583	0.5554	0.2743	0.7561	26.9511	-13.4516	-1.7851
20	2.0848	-0.2801	-0.5047	2.9653	2.433	2.0318	-0.0937	-0.0463	-1.1367	0.5184	0.797	-1.3528	0.9285	1.0302	1.2551	1.1425	0.8228	0.2006	0.6449	-0.1769	0.8027	32.6559	-12.1641	-10.7831
21	5.0355	-1.6487	-0.2023	7.9115	1.4973	2.0503	0.3155	-0.5649	-0.8887	0.7305	-0.6594	0.5734	0.818	0.5997	-0.284	1.0235	0.8628	-0.0471	1.0031	0.1741	0.5636	30.1374	-6.0439	3.7195
22	4.5641	-0.9538	1.1572	9.3541	-2.4491	3.0335	-0.3238	-0.409	0.0823	-0.5119	0.2223	-0.5896	0.725	1.0077	0.2352	0.2786	0.0819	0.0122	0.5666	-0.0594	0.2959	29.5722	5.7029	-10.9595
23	9.2455	1.9219	-3.7522	3.649	-1.2604	5.6088	-0.5886	-0.7244	-0.0552	-0.2905	0.2909	-0.1767	0.6326	0.7735	0.3799	0.369	0.0329	-0.0011	0.4521	-0.1064	0.2336	25.5331	9.3184	-5.5979
24	8.1104	3.2061	-2.9904	6.0086	-2.7584	6.8169	0.2784	-1.0292	0.9471	0.3391	-0.3199	-0.2421	-1.0642	1.3282	-0.0593	0.3355	-0.0732	-0.0339	0.5605	-0.1492	0.4179	29.0047	16.0468	-8.8392
25	2.2266	-0.4834	-0.5513	3.0519	3.214	3.3243	0.0624	0.3727	1.1001	-0.6619	0.4684	-0.2727	-1.0946	0.038	-0.4733	0.5839	-0.0549	0.0102	0.4484	-0.0341	0.6405	25.2589	19.8988	-16.5697
26	3.6169	4.3573	-3.0465	7.7312	-0.0893	9.0065	-0.3075	-0.2621	0.8945	-0.264	0.4656	0.1449	-0.2319	0.0588	-0.1433	0.2943	0.0216	-0.0282	0.3383	0.0485	0.2928	17.9257	7.1894	-11.636
27	2.2535	2.1901	-2.3324	2.1435	-2.051	7.6897	0.308	-0.6627	1.3634	-0.3179	0.2873	-0.0184	-1.4866	1.5222	-0.1233	0.5211	-0.1493	0.116	0.6506	-0.1591	0.6045	27.3216	19.0344	-8.1976
28	7.5422	-2.4183	-3.6842	3.6239	0.3373	8.8186	-0.2279	-1.067	0.1421	0.0918	0.4005	-0.1982	0.5202	1.246	-0.1408	0.3756	0.0509	-0.0786	0.6802	-0.1439	0.3766	29.9846	6.9633	-2.9867
29	7.6944	2.6396	0.5914	4.6724	1.8923	3.473	-0.1603	-0.1168	-1.0781	0.2696	0.4057	-0.5317	0.9087	1.0992	0.0097	0.5801	0.2668	0.0101	0.622	0.0171	0.4701	29.2799	-4.2008	-9.1705
30	8.6174	2.4856	-2.4229	2.0565	0.0616	6.1895	-0.2248	-0.2283	-0.998	0.3116	0.0132	0.1448	1.1905	-0.2992	0.0082	0.8725	-0.0588	0.1633	0.3286	0.0383	0.5641	15.8381	-11.535	-10.0463
31	9.5525	1.1309	-1.787	8.3238	-2.0742	2.1472	-0.1793	-0.7738	-0.6473	0.5929	0.1461	0.5977	0.9508	-0.1957	0.1671	0.4445	0.0762	0.0788	0.3978	0.0694	0.3355	13.1221	-1.4794	-7.3401
32	0.791	-1.854	1.6933	4.2669	-3.8814	3.4813	0.6286	-0.1328	-1.0512	0.1166	-0.2577	-0.8375	0.6528	-0.4378	-0.5771	1.1844	-0.1762	0.3608	0.4764	-0.0173	1.2457	13.1547	-16.33	-10.6745

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 2 through 26 )	A	2 - 26
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 27 through 44 )	A	27 - 44
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 45 through 67 )	A	45 - 67
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 68 through 90 )	A	68 - 90
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 91 through 105 )	A	91 - 105
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 106 through 119 )	A	106 - 119
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 120 through 139 )	A	120 - 139
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 0 through 16 )	B	0 - 16
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 17 through 26 )	B	17 - 26
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 27 through 44 )	B	27 - 44
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 45 through 67 )	B	45 - 67
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 68 through 73 )	B	68 - 73
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 74 through 90 )	B	74 - 90
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 91 through 105 )	B	91 - 105
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 106 through 118 )	B	106 - 118
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 119 through 131 )	B	119 - 131
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 132 through 139 )	B	132 - 139
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 2 through 8 )	C	2 - 8
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 9 through 16 )	C	9 - 16
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 17 through 26 )	C	17 - 26
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 27 through 36 )	C	27 - 36
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 37 through 68 )	C	37 - 68
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 69 through 91 )	C	69 - 91
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 92 through 105 )	C	92 - 105
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 106 through 119 )	C	106 - 119
26	X-RAY DIFFRACTION	26	chain 'C' and (resid 120 through 131 )	C	120 - 131
27	X-RAY DIFFRACTION	27	chain 'C' and (resid 132 through 138 )	C	132 - 138
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 0 through 17 )	D	0 - 17
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 18 through 67 )	D	18 - 67
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 68 through 117 )	D	68 - 117
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 118 through 131 )	D	118 - 131
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 132 through 138 )	D	132 - 138

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