PDB-5cw2: Crystal structure of Epoxide Hydrolase A from Mycobacterium therm...

ID or keywords:

Entry

Database: PDB / ID: 5cw2

Title

Crystal structure of Epoxide Hydrolase A from Mycobacterium thermoresistibile

Components

Putative epoxide hydrolase EPHA

Keywords

HYDROLASE /

Epoxide hydrolase / 1 / 3-diphenylurea Mycobacterium alpha/beta

Function / homology

Function and homology information

hydrolase activity
Similarity search - Function

Biological species

Mycobacterium thermoresistibile ATCC 19527 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2 Å

Authors

Schulz, E.C. / Wilmanns, M.

Citation

Journal: To Be Published
Title: The crystal structure of mycobacterial Epoxide Hydrolase A
Authors: Schulz, E.C. / Wilmanns, M. / Henderson, S. / Southall, S.

History

Deposition	Jul 27, 2015	Deposition site: RCSB / Processing site: PDBE
Revision 1.0	Aug 17, 2016	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5cw2.cif.gz	669.2 KB	Display	PDBx/mmCIF format
PDB format	pdb5cw2.ent.gz	585.7 KB	Display	PDB format
PDBx/mmJSON format	5cw2.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/cw/5cw2 ftp://data.pdbj.org/pub/pdb/validation_reports/cw/5cw2	HTTPS FTP

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Related structure data

Similar structure data	3r43-d 1lbs-1 1wma-d 4bym-1 6dno-d 2pdj-d 4mp0-2 3n5u-2 4v0u-2 3r6i-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) 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

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#165 - Sep 2013 Designed Protein Cages similarity (3) #220 - Apr 2018 Dehalogenases similarity (3) #216 - Dec 2017 Biodegradable Plastic similarity (1)

Deposited unit

C: Putative epoxide hydrolase EPHA

A: Putative epoxide hydrolase EPHA

B: Putative epoxide hydrolase EPHA

D: Putative epoxide hydrolase EPHA

hetero molecules

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

1

C: Putative epoxide hydrolase EPHA

hetero molecules

defined by author&software
35.8 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

A: Putative epoxide hydrolase EPHA

hetero molecules

defined by author&software
35.8 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

B: Putative epoxide hydrolase EPHA

hetero molecules

defined by author&software
35.8 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: Putative epoxide hydrolase EPHA

hetero molecules

defined by author&software
35.8 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	61.800, 105.010, 108.950
Angle α, β, γ (deg.)	90.00, 90.11, 90.00
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Putative epoxide hydrolase EPHA Mass: 35578.023 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium thermoresistibile ATCC 19527 (bacteria) Gene: KEK_07967 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta II / References: UniProt: G7CF24, epoxide hydrolase
#2: Chemical	ChemComp-BSU / 1,3-DIPHENYLUREA / DIPHENYLCARBAMIDE / 1,3-Diphenylurea Mass: 212.247 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₃H₁₂N₂O / Comment: hormone*YM
#3: Chemical	ChemComp-NA / SODIUM ION Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#4: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 408 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION

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Sample preparation

Crystal	Density Matthews: 2.48 Å³/Da / Density % sol: 50.49 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1M BisTris pH 7.5, 2.15 M (NH4)2SO4, 4.5% (v/v) PEG 400, 1-3% (v/v) 2,3-butanediol

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Data collection

Diffraction	Mean temperature: 100 K / Ambient temp details: MASSIF automated DC
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-1 / Wavelength: 0.9752 Å
Detector	Type: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Nov 19, 2014
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9752 Å / Relative weight: 1
Reflection	Resolution: 2→47.82 Å / Num. obs: 93380 / % possible obs: 99.47 % / Redundancy: 3.4 % / R_merge(I) obs: 0.1145 / Net I/σ(I): 7.68
Reflection shell	Resolution: 2→2.071 Å / Redundancy: 3.5 % / R_merge(I) obs: 0.5224 / Mean I/σ(I) obs: 2.42 / % possible all: 99.66

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Processing

Software

Name	Version	Classification
PHENIX	1.9_1692	refinement
XDS		data reduction
XSCALE		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2→47.819 Å / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 38.23 / Stereochemistry target values: TWIN_LSQ_F

	R_factor	Num. reflection	% reflection
R_free	0.2508	4703	5.04 %
R_work	0.2086	-	-
obs	0.2129	93380	99.47 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 2→47.819 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9892	0	65	408	10365

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.014	10239
X-RAY DIFFRACTION	f_angle_d	1.5	13983
X-RAY DIFFRACTION	f_dihedral_angle_d	16.339	3677
X-RAY DIFFRACTION	f_chiral_restr	0.058	1489
X-RAY DIFFRACTION	f_plane_restr	0.008	1882

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
2.0001-2.0346	0.2962	232	0.2634	4397	X-RAY DIFFRACTION	95
2.0346-2.0716	0.2934	234	0.2562	4456	X-RAY DIFFRACTION	95
2.0716-2.1115	0.2804	232	0.2532	4404	X-RAY DIFFRACTION	95
2.1115-2.1546	0.2855	233	0.2487	4430	X-RAY DIFFRACTION	95
2.1546-2.2014	0.275	234	0.244	4441	X-RAY DIFFRACTION	95
2.2014-2.2526	0.2891	232	0.2441	4397	X-RAY DIFFRACTION	95
2.2526-2.3089	0.2834	233	0.2356	4433	X-RAY DIFFRACTION	95
2.3089-2.3714	0.2485	234	0.2328	4439	X-RAY DIFFRACTION	94
2.3714-2.4411	0.2691	232	0.2352	4421	X-RAY DIFFRACTION	94
2.4411-2.5199	0.2731	233	0.2345	4415	X-RAY DIFFRACTION	95
2.5199-2.61	0.2616	233	0.2305	4443	X-RAY DIFFRACTION	95
2.61-2.7145	0.2686	234	0.2309	4433	X-RAY DIFFRACTION	95
2.7145-2.838	0.2631	234	0.225	4447	X-RAY DIFFRACTION	95
2.838-2.9876	0.2694	232	0.2154	4403	X-RAY DIFFRACTION	94
2.9876-3.1748	0.2537	231	0.2107	4404	X-RAY DIFFRACTION	94
3.1748-3.4198	0.2636	236	0.2041	4482	X-RAY DIFFRACTION	95
3.4198-3.7638	0.2309	233	0.1951	4428	X-RAY DIFFRACTION	95
3.7638-4.3082	0.2111	233	0.1622	4422	X-RAY DIFFRACTION	94
4.3082-5.4266	0.2097	235	0.1619	4466	X-RAY DIFFRACTION	94
5.4266-47.3122	0.23	239	0.209	4531	X-RAY DIFFRACTION	94

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	0.003	0.0005	-0.0009	-0.0014	0.0029	0.0003	-0.017	0.0013	0.0047	0.0187	-0.0055	0.0237	-0.0096	-0.0021	-0	0.0622	-0.0054	0.0016	0.0464	0.0135	0.0703	-10.5509	-14.7581	-9.1714
2	0.0006	-0.0003	-0	0.0003	-0.0003	0.0001	-0.0049	0.0112	-0.0022	-0.0009	-0.0003	0.0024	0.0002	-0	0	0.0081	-0.0024	-0.0348	0.028	0.0161	0.0312	-12.8926	-9.0736	-18.7311
3	0.0001	0.0008	-0.0008	-0.0005	-0.0008	-0.0005	-0.0034	-0.0025	0.0029	0.0024	-0.0096	0.0013	-0.0039	-0.0032	0	-0.0135	-0.0551	-0.0627	0.0046	0.1183	-0.0374	-2.5233	-10.3558	-19.0904
4	0.0001	-0.0026	-0.0008	0.0009	0.0019	0.0009	0.0027	0.0202	-0.0234	0.0149	-0.0055	0.0089	0.0025	0.0004	0	0.0314	0.0153	-0.0151	0.036	0.0325	0.0392	5.3326	-33.0415	-18.7784
5	0	0	0.0004	0.0003	-0.0008	0.0003	-0.0051	0.0033	-0.0064	0.0191	-0.0027	0.0087	0.0007	-0.0044	-0	0.053	-0.0093	0.0029	0.0459	0.0146	0.053	-1.5635	-29.8393	-1.3937
6	0.001	-0.0022	-0.0018	0.0001	-0.0012	-0.0006	-0.0085	0.0053	-0.0018	0.0018	-0.0139	0.0106	0.0002	-0.0052	-0	0.0103	0.014	0.0146	0.0624	0.0327	0.0601	-4.51	-22.948	-27.4052
7	0.0016	0.0005	-0.0016	-0.0002	-0.0011	-0.0003	0.0082	-0.0028	-0.001	0.0011	0.002	-0.0052	0.0002	0.0052	-0	0.0368	-0.0376	-0.0109	0.0461	0.0646	0.0543	9.2272	-14.2808	-20.0437
8	0.0018	0.0009	0.0007	-0	-0.0005	-0.0002	0.0094	-0.0045	0.0198	0.0039	0.0038	-0.0048	0.0007	0.002	-0	0.0562	-0.0448	-0.0436	0.0598	0.0972	0.0475	9.6981	-13.1469	-12.7645
9	0.0001	0.0016	0.0014	0.0006	-0.0001	-0.0004	0.0041	-0.0027	0.001	-0.0043	0.0042	-0.0006	-0.0054	-0.0006	0	0.049	-0.0103	-0.0814	0.0337	0.0155	0.0775	2.9556	-2.9881	-7.0369
10	0.0009	0.0009	-0.0001	-0.0019	-0.0032	0.0005	-0.0239	0.0066	-0.0043	-0.0075	-0.0245	-0.0117	-0.0112	-0.0052	-0	0.0476	0.0081	-0.0127	0.028	-0.0031	0.0273	35.7527	-14.7083	8.436
11	-0	0.0001	0	0.0001	0.0001	0	-0.0063	-0.0014	0.0003	0.0007	-0.0034	-0.001	-0.0022	-0.0018	-0	0.0349	0.0161	-0.0126	0.0316	-0.0017	0.0537	38.1567	-8.8538	17.9611
12	0.0005	-0.0005	-0.0013	-0.0001	0.0008	-0.0001	0.0021	0.0038	0.0069	0.0035	-0.0128	-0.0045	-0.0048	0.0018	-0	0.0405	0.0429	-0.0218	0.0392	-0.0934	0.0129	27.6814	-10.126	18.2595
13	0.001	-0.0016	0.0006	-0.0001	0.0001	-0.001	0.0062	0.0005	-0.0038	0.0026	-0.0011	0.0047	-0.0062	0.0035	-0	0.0006	-0.0166	-0.0317	0.0268	-0.0439	0.0313	20.0148	-28.9421	25.9803
14	-0	0.0004	0.0009	0.0006	-0.0002	-0.0004	0.0031	0.0058	-0.0056	-0.0105	0.009	0.0058	0.0031	-0.0063	0	0.0129	0.0118	-0.0372	0.0159	-0.0147	0.0466	20.2087	-35.1271	9.8356
15	-0.0008	0.0017	0.0015	0	0.0007	0.0008	-0.0113	-0.0013	-0.0014	-0.0125	-0.0041	0.0074	-0.0037	0.0012	0	0.0706	-0.0123	-0.0376	0.041	-0.007	0.0332	18.3777	-34.9192	6.0741
16	-0	-0.0002	0.0006	-0.0002	0.0002	0.0003	-0.0006	0.0018	-0.003	-0.0048	0.0031	-0.0059	0.0016	-0.0012	-0	0.042	-0.0057	-0.0043	0.0355	-0.001	0.033	32.813	-29.1682	2.1814
17	0.0004	0.0019	-0.0014	0.0007	-0.0003	0	-0.0069	-0.0033	0.0019	-0.0029	-0.0147	-0.0086	0.0036	0.0045	-0	0.0456	-0.0352	-0.0033	0.0527	-0.0257	0.0298	29.6711	-22.7562	26.6564
18	0.0006	0.0005	-0.0015	-0.0005	0.0003	0	0.0015	0.0044	-0.0006	0.0029	-0.0055	0.006	-0.008	-0.0008	0	0.0126	0.0336	-0.0103	0.0434	-0.0542	0.0251	15.8722	-14.1193	19.1918
19	0.0012	-0.0008	0.0007	-0.0008	0.001	-0.0003	0.0102	0.0042	0.012	-0.0039	0.0098	0.0175	0.0045	0.0012	0	-0.0071	0.0454	-0.0268	0.0207	-0.0653	0.0192	15.6031	-12.9394	11.9974
20	-0.0001	-0.0009	0.001	0.0002	0.0001	-0.0001	0.0021	0.0035	0.002	0.0024	0.0003	-0.0001	-0.0051	0.0017	-0	0.0655	0.0203	-0.0336	0.0431	-0.004	0.0664	22.2331	-2.8382	6.1115
21	0.0006	0.0001	0.0008	-0.0003	0.0009	-0.0001	-0.0058	0.0018	0.0015	-0.0069	0.0004	0.0018	0.006	-0.0019	-0	-0.0123	-0.0229	0.002	0.0112	-0.0106	0.0171	14.8462	-40.9859	-47.5006
22	0.0025	0.0027	0.0008	-0.0004	0.0019	0.0004	-0.0362	-0.0187	0.0056	-0.0254	-0.0243	0.0126	0.0192	-0.0066	-0	0.0088	0.0094	0.0106	0.0188	0.0433	-0.0354	22.2645	-37.779	-42.819
23	-0.0042	0.0044	0.0038	-0.0019	-0.0005	-0	0.0118	-0.0117	0.0292	-0.0017	0.0109	-0.0179	0.0236	-0.0052	-0	-0.0508	0.0365	-0.0152	0.0358	0.0661	-0.0467	32.987	-30.3501	-30.8077
24	-0.0006	0.0005	-0.0018	0.0001	-0.0022	0.0009	-0.0043	-0.0052	0.0065	-0.0269	0.0038	-0.007	-0.0057	0.0093	0	0.0573	0.0211	0.0125	0.0283	0.0278	0.0375	36.69	-17.0682	-46.2475
25	0.0016	0.0018	0.0001	-0.0008	-0.0011	-0.0002	0.0056	-0.0128	-0.0034	-0.0155	-0.0132	0.0032	-0.0084	-0.0059	0	0.0291	0.015	-0.0001	0.0729	0.0066	0.0548	24.6942	-24.9574	-40.552
26	0.0009	-0.0005	0.0008	-0.0012	-0.0007	-0.0004	0.0065	0.0024	-0.0078	-0.0145	0.0047	-0.0204	-0.0048	-0.0003	0	0.0234	0.0792	0.002	0.0509	0.0918	0.0195	39.3198	-38.6753	-37.4738
27	-0.0002	-0.0003	-0.0006	0	0	-0	0.0024	0.0029	-0.0027	-0.0021	0.0003	-0.0009	0.0035	-0.0039	0	0.0355	-0.0016	0.0521	0.0091	0.0132	0.0498	34.0009	-48.9756	-48.4276
28	-0.0002	-0.0006	0.0003	-0.0002	0.0004	0.0003	-0.0058	0.008	0.0015	-0.005	0.0027	-0.0001	0.0016	0.0014	0	-0.0042	-0.0146	-0.0291	0.01	0.0381	-0.0023	-11.0654	14.6939	-45.8236
29	0.0001	0.0002	-0.0004	0.0001	-0	0.0006	-0.012	0.0046	-0.0057	0.0008	-0.0069	0.0008	-0.0065	0.0036	0	0.0316	-0.0523	0.0112	0.0303	0.0147	0.024	-1.4381	12.2259	-45.8065
30	0.0038	0.0032	-0.0007	-0.0007	0.0017	-0.0005	-0.0115	0.0024	0.0126	-0.0146	-0.0083	0.0067	0.0069	0.0004	0	0.0284	-0.0034	-0.0005	0.0313	-0.0047	0.0356	-2.739	16.949	-44.5488
31	0.0002	-0.0001	0	0.0001	0	0	0.0007	-0.0027	-0.0063	-0.0018	0.0005	0.0016	0.0032	0.0001	-0	0.0359	0.0244	0.008	0.032	-0.0186	0.0366	-7.1084	9.5536	-35.5112
32	-0.0039	0.0028	-0	-0.0017	0.001	-0.0029	0.0229	-0.019	0.037	0.0007	-0.0024	-0.0062	0.0136	0.0069	0	-0.0691	0.0314	0.0468	-0.0353	0.054	-0.1015	7.5708	21.3485	-30.9787
33	0	0.0021	-0.0026	0.0004	-0.0015	0.0009	-0.0075	0.0059	0.0025	-0.0132	0.011	0.0017	-0.0093	0.0034	-0	0.0573	-0.003	0.0044	0.0336	0.0344	0.0743	11.6902	35.5597	-45.5659
34	0.0013	0.0043	0.0007	0.0001	-0.0009	-0.0004	-0.0062	-0.0115	0.0054	-0.0098	-0.0025	0.0063	-0.0055	-0.0021	0	0.04	0.0085	-0.0103	0.0442	0.0286	0.0555	-0.3911	27.6922	-39.822
35	0.0003	0.0005	0.0001	0.0002	0.0005	0.0002	0.0037	0.0102	-0.0075	-0.0002	-0.0092	-0.0001	-0.001	0.004	-0	0.0439	0.0094	0.0101	0.0519	0.0195	0.0337	11.4286	13.3589	-32.2981
36	0.0003	-0.0005	0.0008	-0.0005	-0.0001	-0.0004	0.006	-0.0049	-0.0024	0.0005	0.0044	-0.0027	-0.0052	0.0025	-0	-0.0327	0.0485	0.0206	-0.0372	0.0663	0.0448	17.3533	11.9072	-33.663
37	-0.0007	-0.0007	-0.0019	0.0005	0.001	0.0008	0.0015	0.0107	-0.0123	0.001	0.0036	0.0027	0.004	0.0004	-0	0.0462	-0.022	0.0936	0.0144	0.0302	0.0222	10.9116	9.7635	-47.8638

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'C' and (resid 3 through 77 )
2	X-RAY DIFFRACTION	2	chain 'C' and (resid 78 through 96 )
3	X-RAY DIFFRACTION	3	chain 'C' and (resid 97 through 126 )
4	X-RAY DIFFRACTION	4	chain 'C' and (resid 127 through 203 )
5	X-RAY DIFFRACTION	5	chain 'C' and (resid 204 through 231 )
6	X-RAY DIFFRACTION	6	chain 'C' and (resid 232 through 251 )
7	X-RAY DIFFRACTION	7	chain 'C' and (resid 252 through 278 )
8	X-RAY DIFFRACTION	8	chain 'C' and (resid 279 through 303 )
9	X-RAY DIFFRACTION	9	chain 'C' and (resid 304 through 321 )
10	X-RAY DIFFRACTION	10	chain 'A' and (resid 3 through 77 )
11	X-RAY DIFFRACTION	11	chain 'A' and (resid 78 through 96 )
12	X-RAY DIFFRACTION	12	chain 'A' and (resid 97 through 126 )
13	X-RAY DIFFRACTION	13	chain 'A' and (resid 127 through 161 )
14	X-RAY DIFFRACTION	14	chain 'A' and (resid 162 through 193 )
15	X-RAY DIFFRACTION	15	chain 'A' and (resid 194 through 215 )
16	X-RAY DIFFRACTION	16	chain 'A' and (resid 216 through 231 )
17	X-RAY DIFFRACTION	17	chain 'A' and (resid 232 through 251 )
18	X-RAY DIFFRACTION	18	chain 'A' and (resid 252 through 278 )
19	X-RAY DIFFRACTION	19	chain 'A' and (resid 279 through 303 )
20	X-RAY DIFFRACTION	20	chain 'A' and (resid 304 through 321 )
21	X-RAY DIFFRACTION	21	chain 'B' and (resid 3 through 27 )
22	X-RAY DIFFRACTION	22	chain 'B' and (resid 28 through 103 )
23	X-RAY DIFFRACTION	23	chain 'B' and (resid 104 through 161 )
24	X-RAY DIFFRACTION	24	chain 'B' and (resid 162 through 215 )
25	X-RAY DIFFRACTION	25	chain 'B' and (resid 216 through 247 )
26	X-RAY DIFFRACTION	26	chain 'B' and (resid 248 through 303 )
27	X-RAY DIFFRACTION	27	chain 'B' and (resid 304 through 321 )
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 3 through 21 )
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 22 through 38 )
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 39 through 77 )
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 78 through 96 )
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 97 through 161 )
33	X-RAY DIFFRACTION	33	chain 'D' and (resid 162 through 215 )
34	X-RAY DIFFRACTION	34	chain 'D' and (resid 216 through 247 )
35	X-RAY DIFFRACTION	35	chain 'D' and (resid 248 through 272 )
36	X-RAY DIFFRACTION	36	chain 'D' and (resid 273 through 292 )
37	X-RAY DIFFRACTION	37	chain 'D' and (resid 293 through 321 )

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