PDB-7jve: Crystal structure of Salmonella enterica Typhimurium BcfH

ID or keywords:

Entry

Database: PDB / ID: 7jve

Title

Crystal structure of Salmonella enterica Typhimurium BcfH

Components

DsbA family protein

Keywords

OXIDOREDUCTASE / isomerase / fimbrial operon / virulence factor

Function / homology

DSBA-like thioredoxin domain / DSBA-like thioredoxin domain / Thioredoxin domain profile. / Thioredoxin domain / Thioredoxin-like superfamily / oxidoreductase activity / TRIETHYLENE GLYCOL / DsbA family protein

Function and homology information

Biological species

Salmonella typhimurium (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MAD / Resolution: 2.31 Å

Authors

Subedi, P. / Heras, B. / Hor, L. / Paxman, J.J.

Funding support

Australia, 2items

Citation

Journal: Antioxid.Redox Signal. / Year: 2021
Title: Salmonella enterica BcfH Is a Trimeric Thioredoxin-Like Bifunctional Enzyme with Both Thiol Oxidase and Disulfide Isomerase Activities.
Authors: Subedi, P. / Paxman, J.J. / Wang, G. / Hor, L. / Hong, Y. / Verderosa, A.D. / Whitten, A.E. / Panjikar, S. / Santos-Martin, C.F. / Martin, J.L. / Totsika, M. / Heras, B.

History

Deposition	Aug 21, 2020	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 21, 2021	Provider: repository / Type: Initial release
Revision 1.1	Jun 23, 2021	Group: Database references / Category: citation Item: _citation.journal_volume / _citation.page_first / _citation.page_last

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	7jve.cif.gz	597.7 KB	Display	PDBx/mmCIF format
PDB format	pdb7jve.ent.gz	512.3 KB	Display	PDB format
PDBx/mmJSON format	7jve.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	7jve_validation.pdf.gz	503.2 KB	Display	wwPDB validaton report
Full document	7jve_full_validation.pdf.gz	521.1 KB	Display
Data in XML	7jve_validation.xml.gz	63.2 KB	Display
Data in CIF	7jve_validation.cif.gz	90.1 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/jv/7jve ftp://data.pdbj.org/pub/pdb/validation_reports/jv/7jve	HTTPS FTP

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Related structure data

Similar structure data	1i1m-d 4pc6-1 4pc3-1 1xmx-2 4pc2-1 4pc3-2 4q40-3 1iyd-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) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search
Other databases	SASBDB: SASDJL7associated SAS data

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: DsbA family protein

B: DsbA family protein

C: DsbA family protein

D: DsbA family protein

E: DsbA family protein

F: DsbA family protein

hetero molecules

167 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: DsbA family protein

B: DsbA family protein

C: DsbA family protein

hetero molecules

defined by author&software
Evidence: SAXS, equilibrium centrifugation
83.7 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: DsbA family protein

E: DsbA family protein

F: DsbA family protein

hetero molecules

defined by author&software
83.7 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	103.012, 133.731, 146.750
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁

#1: Protein	DsbA family protein / Thiol-disulfide isomerase / Thioredoxin domain-containing protein Mass: 27662.166 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella typhimurium (bacteria) Gene: B9C96_12120, CC725_14640, D7O80_18050, DOC60_06685, DSM38_01995, ECA50_10820, SAMEA4398682_04006 Plasmid: pMCSG7 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A564XRN6
#2: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#3: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 19 / Source method: obtained synthetically / Formula: C₂H₆O₂
#4: Chemical	ChemComp-PGE / TRIETHYLENE GLYCOL Mass: 150.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₆H₁₄O₄
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 928 / Source method: isolated from a natural source / Formula: H₂O
Has ligand of interest	N

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.11 Å³/Da / Density % sol: 60.43 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion / pH: 6 Details: 0.2 M MgCl2, 0.1 mM Bis Tris propane, pH 6.0, 20% PEG 3350

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

Australian Synchrotron

/ Beamline: MX2 / Wavelength: 0.9537 Å

Detector

Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: May 11, 2018

Radiation

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

Radiation wavelength

Wavelength: 0.9537 Å / Relative weight: 1

Reflection

Resolution: 2.3→50 Å / Num. obs: 88024 / % possible obs: 99.1 % / Redundancy: 8.7 % / R_merge(I) obs: 0.072 / R_pim(I) all: 0.025 / R_rim(I) all: 0.077 / Χ²: 1.019 / Net I/σ(I): 13 / Num. measured all: 763336

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Χ²	% possible all
2.3-2.34	6.3	0.585	4177	0.805	0.245	0.638	0.8	94.7
2.34-2.38	6.4	0.501	4214	0.833	0.206	0.544	0.81	96.1
2.38-2.43	6.6	0.457	4309	0.864	0.186	0.496	0.828	98.2
2.43-2.48	6.5	0.404	4258	0.888	0.165	0.438	0.825	97.7
2.48-2.53	6.3	0.351	4249	0.911	0.146	0.382	0.809	96.6
2.53-2.59	6.8	0.303	4367	0.937	0.122	0.328	0.822	98.9
2.59-2.66	7.5	0.257	4389	0.956	0.099	0.276	0.838	99.8
2.66-2.73	7.7	0.216	4395	0.971	0.082	0.232	0.84	100
2.73-2.81	8	0.192	4399	0.979	0.072	0.206	0.857	99.8
2.81-2.9	8.3	0.166	4403	0.985	0.06	0.177	0.903	99.9
2.9-3	8.7	0.135	4422	0.99	0.048	0.143	0.941	100
3-3.12	9.2	0.113	4423	0.993	0.039	0.119	1.006	100
3.12-3.26	9.8	0.097	4426	0.996	0.032	0.102	1.118	100
3.26-3.44	10.2	0.081	4430	0.996	0.027	0.086	1.214	100
3.44-3.65	10.6	0.068	4475	0.998	0.022	0.072	1.298	100
3.65-3.93	10.5	0.058	4432	0.998	0.019	0.061	1.324	100
3.93-4.33	9.6	0.05	4455	0.998	0.016	0.053	1.315	99.9
4.33-4.95	10.6	0.046	4524	0.998	0.015	0.048	1.239	100
4.95-6.24	11.5	0.044	4540	0.998	0.013	0.046	1.012	100
6.24-50	11.3	0.034	4737	0.999	0.01	0.036	0.878	99.6

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Processing

Software

Name	Version	Classification
PHENIX	1.18.2_3874	refinement
HKL-2000		data scaling
PDB_EXTRACT	3.25	data extraction
Coot		model building
Auto-Rickshaw		phasing
HKL-2000		data reduction

Refinement

Method to determine structure:

MAD / Resolution: 2.31→42.65 Å / SU ML: 0.25 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 20.15 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2085	4312	4.97 %
R_work	0.1665	82494	-
obs	0.1686	86806	97.23 %

Solvent computation

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

Displacement parameters

B_iso max: 153.86 Å² / B_iso mean: 40.1789 Å² / B_iso min: 16.14 Å²

Refinement step

Cycle: final / Resolution: 2.31→42.65 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	11445	0	204	928	12577
B_iso mean	-	-	48.87	38.43	-
Num. residues	-	-	-	-	1487

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 (%)
2.31-2.34	0.2565	114	0.1825	1966	2080	70
2.34-2.36	0.26	121	0.195	2411	2532	87
2.36-2.39	0.2586	124	0.1941	2448	2572	88
2.39-2.42	0.2201	135	0.1952	2590	2725	92
2.42-2.46	0.2627	146	0.1967	2651	2797	95
2.46-2.49	0.2649	143	0.1929	2643	2786	96
2.49-2.52	0.2637	121	0.1947	2703	2824	96
2.52-2.56	0.2096	135	0.1972	2705	2840	97
2.56-2.6	0.2801	139	0.1911	2777	2916	99
2.6-2.65	0.2646	145	0.1865	2786	2931	100
2.65-2.69	0.2468	170	0.1854	2758	2928	100
2.69-2.74	0.2196	160	0.1855	2773	2933	100
2.74-2.79	0.2384	130	0.192	2835	2965	100
2.79-2.85	0.2439	157	0.1913	2799	2956	100
2.85-2.91	0.2587	145	0.1964	2802	2947	100
2.91-2.98	0.1987	130	0.1858	2833	2963	100
2.98-3.05	0.2505	174	0.1765	2799	2973	100
3.05-3.14	0.2216	156	0.1781	2804	2960	100
3.14-3.23	0.2179	153	0.1773	2803	2956	100
3.23-3.33	0.222	135	0.1723	2859	2994	100
3.33-3.45	0.2139	144	0.1733	2817	2961	100
3.45-3.59	0.2352	146	0.1636	2826	2972	100
3.59-3.75	0.2142	154	0.1633	2834	2988	100
3.75-3.95	0.1935	141	0.1449	2842	2983	100
3.95-4.2	0.1937	159	0.1389	2830	2989	100
4.2-4.52	0.1766	137	0.1301	2863	3000	100
4.52-4.98	0.1406	136	0.1315	2906	3042	100
4.98-5.7	0.1765	160	0.1498	2863	3023	100
5.7-7.17	0.2092	132	0.179	2940	3072	100
7.17-42.65	0.1492	170	0.1526	3028	3198	100

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	1.432	1.728	0.5535	3.0053	2.4129	3.6998	-0.215	-0.1926	-0.2301	-0.1227	0.2655	-0.6447	0.072	1.0841	0.3631	0.5166	-0.0783	-0.0542	0.6597	0.4705	0.7329	52.9816	33.8473	3.4063
2	1.2515	0.6213	-0.6971	0.54	-1.0492	1.6722	0.1264	-0.0506	0.2208	-0.0989	-0.2426	-0.2846	-0.0043	0.4024	0.096	0.2512	-0.0198	0.041	0.3029	0.1078	0.4429	33.4089	18.0567	17.3578
3	0.3459	0.4119	0.209	1.0727	-0.4474	3.2139	0.2211	-0.1386	0.4007	0.2787	0.1899	0.1845	-0.6314	-0.1519	-0.4323	0.3058	0.0659	0.0742	0.2181	-0.053	0.3655	2.2327	23.5689	38.4606
4	2.9863	-0.5055	-0.2838	3.1996	1.0205	2.7538	-0.0733	-0.222	-0.0817	0.312	-0.0457	-0.0238	-0.018	0.1765	0.1066	0.1912	-0.0179	0.0123	0.2619	0.0214	0.1836	7.2807	10.2547	38.8115
5	2.659	-0.1557	-0.3835	2.522	0.5679	3.797	-0.1145	-0.1005	-0.3133	0.0641	-0.0421	0.0409	0.2646	-0.1297	0.1251	0.1841	-0.006	0.0185	0.1972	0.0251	0.2371	-4.588	3.0534	37.3351
6	2.4779	1.6223	-0.9377	2.2872	-1.1218	1.8888	0.0636	-0.1322	0.1073	-0.0445	-0.0876	0.2003	0.0567	-0.1345	0.0076	0.2147	0.0308	-0.0172	0.2313	-0.0344	0.2364	-8.9212	9.8327	29.3605
7	3.5197	-0.2621	0.2851	2.5578	-0.5872	3.5153	-0.0149	-0.1999	0.631	-0.2521	0.0449	-0.395	-1.0229	0.1177	0.0394	0.3422	-0.0001	0.0705	0.157	-0.0174	0.3398	10.4848	21.6242	33.0671
8	4.2319	-0.3095	0.713	4.7334	-0.2138	7.2798	0.0731	-0.5757	0.4357	0.3443	0.1311	-0.8261	-0.5757	0.6141	-0.2002	0.2481	-0.0793	-0.0131	0.3599	-0.0787	0.3323	17.6678	18.9737	40.3314
9	0.5871	0.5653	0.3745	1.5799	-1.0326	0.8019	0.0422	0.2196	0.2187	0.159	-0.2433	-0.1978	-0.2155	0.2006	0.1395	0.3239	0.005	0.1049	0.3935	0.1505	0.4315	45.792	11.7522	13.194
10	2.8709	1.9692	0.2259	4.6141	-0.0462	2.0441	0.0373	-0.1266	0.1476	-0.0426	-0.1414	0.0665	0.0538	-0.0073	0.1009	0.2218	-0.0147	0.0145	0.1479	0.0243	0.2035	30.6869	-29.0631	28.7986
11	3.508	1.487	-3.4891	6.5195	-0.6853	6.7473	-0.1629	0.284	0.1071	-0.8281	0.1027	-1.1309	0.1424	0.5823	0.0339	0.344	-0.0333	0.1423	0.3103	0.0457	0.5081	46.8456	-22.403	18.3249
12	2.0462	1.8682	-0.334	3.4393	-0.2479	1.4417	-0.127	0.3936	0.1835	-0.232	-0.0475	-0.1301	0.0047	0.354	0.1058	0.3027	0.0787	0.0861	0.4699	0.2252	0.4379	42.0754	19.5386	7.9213
13	3.7896	0.4961	0.8025	2.6055	-0.2409	5.0942	-0.058	0.4706	-0.2557	-0.4044	-0.1183	0.3283	0.0625	0.1443	0.2372	0.2786	0.0538	0.0239	0.3213	-0.0339	0.3351	21.4001	-4.6037	9.3584
14	1.5516	-0.2575	-0.057	1.9546	-0.0711	2.2635	0.0128	-0.0133	-0.2145	0.0323	-0.0617	-0.0157	0.0567	0.0905	0.0343	0.1798	0.023	0.0433	0.2007	0.035	0.2816	22.967	-1.8623	24.2587
15	7.1144	0.9097	0.6518	3.1116	-0.1743	6.9731	-0.1292	0.9812	-0.369	-1.0365	-0.0697	0.282	0.1503	-0.4621	0.1466	0.4697	0.0412	-0.0233	0.4387	-0.0746	0.3405	16.3199	-4.9832	3.2182
16	0.0926	0.219	-0.1396	1.0206	0.4691	3.4275	0.1337	-1.8665	-0.4967	0.6645	-0.4247	0.1409	0.01	-0.3913	-0.0072	0.7363	-0.2893	0.066	1.6574	0.0371	0.367	50.4631	3.4482	43.9647
17	2.9821	2.3726	0.756	1.8278	0.2759	0.9782	0.0943	-0.6613	0.3826	0.0072	-0.2833	0.3753	-0.097	-0.3108	0.1197	0.2575	0.0369	0.0586	0.3245	-0.1184	0.3628	67.3427	16.2299	24.5183
18	3.2187	-0.9534	-0.0784	2.1043	-0.2035	3.2052	0.1084	0.1349	0.8804	-0.1856	-0.1357	-0.2053	-0.6979	0.3978	0.0092	0.3519	-0.0461	0.0028	0.1738	-0.0246	0.3621	90.1242	31.0964	14.4661
19	3.0429	-0.7867	-0.4137	1.9277	0.0301	1.7689	-0.0252	0.3853	0.1673	-0.269	-0.0473	-0.0022	-0.0868	0.0252	0.0964	0.2448	-0.0085	0.005	0.256	0.0461	0.1656	90.2305	19.0086	6.9913
20	3.7168	-0.3524	-0.549	2.1996	-0.005	2.3452	-0.189	0.8178	-0.181	-0.5455	-0.0563	-0.2445	0.3644	0.0861	0.1528	0.4079	0.0686	0.1136	0.4609	0.0036	0.2395	97.1798	13.9157	-0.1211
21	2.8322	1.6251	-2.6518	3.8016	-3.3415	6.9002	-0.0034	0.4928	0.0296	-0.4655	-0.0817	-0.7138	0.7095	0.619	0.3046	0.3296	0.1036	0.1071	0.4483	0.0581	0.3985	110.5479	14.826	5.7555
22	3.6136	-0.838	-0.0103	2.0756	-0.7663	2.2182	-0.1332	-0.1769	0.3895	-0.0071	0.0723	0.0792	-0.2484	-0.1361	0.0154	0.2857	0.0056	-0.0199	0.1626	-0.0299	0.2176	85.5039	22.2851	17.2951
23	4.2528	-0.8133	-1.6411	5.1659	0.6801	4.9714	-0.4598	0.4699	0.6273	-0.4102	-0.0578	0.9489	-0.5002	-0.7269	-0.1331	0.4334	0.1054	-0.1311	0.3473	0.111	0.4615	74.2254	29.5491	7.5745
24	0.2828	-0.1551	-0.7144	1.7119	-0.7145	3.1821	0.4503	-1.1152	0.3676	0.4306	-0.0257	0.5881	0.2422	-1.1148	-0.2151	0.623	-0.1213	0.1823	1.68	-0.1355	0.5324	46.3718	6.1679	40.4107
25	7.1065	-5.8923	4.2389	7.5478	-2.8651	8.2981	-0.1095	-0.7938	0.2944	0.5381	-0.2289	-1.1641	0.3139	0.2902	0.1624	0.4664	-0.2235	0.0064	0.7952	0.0126	0.3342	68.9245	1.1159	35.2656
26	4.3258	0.4724	1.0346	4.0373	-0.434	2.4213	0.5742	-0.5552	-1.4113	0.6005	-0.2264	-0.042	0.9373	-0.4475	-0.3683	0.6353	-0.1891	-0.2294	0.4003	0.2521	0.9039	72.1389	-18.2873	26.5832
27	5.2571	-0.9066	1.2117	2.1642	-0.8517	3.0642	0.296	-0.0495	-0.6409	-0.0669	0.2614	-0.102	0.4171	0.074	-0.2995	0.2224	-0.0103	-0.0622	0.2646	-0.0447	0.3943	76.7994	-6.4318	17.0952
28	4.9262	-0.4623	1.496	2.7459	-0.1537	2.7699	0.2716	0.36	-0.5098	-0.1049	-0.0376	-0.1702	0.1209	0.2665	-0.3144	0.2181	-0.022	-0.0112	0.1992	-0.0492	0.2359	79.1054	-4.6639	17.4356
29	3.3504	-0.2755	1.3346	5.7296	2.4087	3.7159	0.0249	0.1124	-0.3804	-0.1539	0.2735	-0.1387	0.085	0.1406	-0.2854	0.153	-0.0417	0.0243	0.2151	-0.0117	0.1776	72.785	2.034	9.873
30	2.7362	0.7499	1.0185	2.5994	-0.7899	3.4187	-0.1212	0.1114	-0.105	-0.1721	0.2526	0.1665	-0.3008	-0.2813	-0.1224	0.1863	0.0144	0.028	0.2571	-0.051	0.2211	65.3785	2.5098	8.4859
31	2.3917	1.0817	-1.9725	6.9824	0.6156	6.0239	0.0136	-0.2978	-1.5889	0.3888	0.0492	0.1219	1.2761	-0.153	-0.014	0.497	-0.0779	-0.2032	0.3052	0.0331	0.751	76.2583	-15.2384	23.2352
32	1.7653	-0.346	-1.8958	5.8186	-0.3364	2.2303	0.3529	-0.6961	-1.1478	0.2857	0.2449	-0.4584	1.0376	0.6595	-0.4159	0.4511	0.0576	-0.2464	0.4513	0.062	0.5852	85.1338	-13.2925	26.3646
33	1.9035	1.7329	-1.0513	3.1233	-1.3058	0.6282	0.4199	-0.4457	0.7975	0.7671	-0.6782	1.1086	-0.7552	-0.5005	-0.0288	0.6937	-0.1249	0.1483	1.63	-0.3366	0.5451	50.314	8.8899	42.227
34	0.9033	0.93	-0.5906	1.6651	1.959	5.331	0.2027	-0.171	0.0616	0.0044	-0.3359	0.0772	-0.151	-0.5128	0.2062	0.1851	0.0536	0.0348	0.3498	0.0017	0.2774	51.9522	-7.9578	9.1032
35	3.5144	1.0766	-1.2398	3.68	0.0027	4.7756	-0.2149	-0.5644	-0.4796	0.4109	0.1427	-0.0207	1.0223	0.4062	0.038	0.5277	0.1202	0.0642	0.3885	0.0303	0.2076	57.5656	-22.7761	-3.8252
36	2.0044	-0.9325	-0.9974	1.7252	0.1436	4.0067	-0.1636	-0.5386	-0.013	0.2682	0.1545	-0.225	0.7229	0.6082	-0.0071	0.3228	0.0927	-0.003	0.3283	-0.0134	0.1611	62.8269	-18.6493	-11.1358
37	0.4368	0.4059	0.1306	1.2968	0.3475	4.0478	-0.2028	-0.6923	0.0621	-0.0988	0.543	-0.6945	0.2569	1.1499	-0.108	0.3024	0.1853	-0.0276	0.5376	-0.0426	0.2907	72.1425	-17.733	-17.6362
38	1.9695	0.249	-1.2721	3.0674	-1.3182	6.5482	-0.1819	-0.3759	0.034	0.4582	0.1738	0.4356	0.2515	-0.3195	-0.0007	0.3531	0.0712	0.0581	0.3579	-0.0305	0.2255	51.8467	-14.656	-0.4937

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 19 )	A	2 - 19
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 20 through 64 )	A	20 - 64
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 65 through 83 )	A	65 - 83
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 84 through 124 )	A	84 - 124
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 125 through 181 )	A	125 - 181
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 182 through 210 )	A	182 - 210
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 211 through 229 )	A	211 - 229
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 230 through 254 )	A	230 - 254
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 4 through 64 )	B	4 - 64
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 65 through 223 )	B	65 - 223
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 224 through 254 )	B	224 - 254
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 7 through 51 )	C	7 - 51
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 52 through 100 )	C	52 - 100
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 101 through 210 )	C	101 - 210
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 211 through 254 )	C	211 - 254
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 11 through 35 )	D	11 - 35
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 36 through 64 )	D	36 - 64
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 65 through 83 )	D	65 - 83
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 84 through 145 )	D	84 - 145
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 146 through 181 )	D	146 - 181
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 182 through 193 )	D	182 - 193
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 194 through 241 )	D	194 - 241
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 242 through 254 )	D	242 - 254
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 9 through 35 )	E	9 - 35
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 36 through 52 )	E	36 - 52
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 53 through 69 )	E	53 - 69
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 70 through 100 )	E	70 - 100
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 101 through 127 )	E	101 - 127
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 128 through 164 )	E	128 - 164
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 165 through 210 )	E	165 - 210
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 211 through 229 )	E	211 - 229
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 230 through 253 )	E	230 - 253
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 9 through 36 )	F	9 - 36
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 37 through 77 )	F	37 - 77
35	X-RAY DIFFRACTION	35	chain 'F' and (resid 78 through 110 )	F	78 - 110
36	X-RAY DIFFRACTION	36	chain 'F' and (resid 111 through 160 )	F	111 - 160
37	X-RAY DIFFRACTION	37	chain 'F' and (resid 161 through 195 )	F	161 - 195
38	X-RAY DIFFRACTION	38	chain 'F' and (resid 196 through 254 )	F	196 - 254

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