PDB-6cnz: Crystal Structure of Chorismate Mutase from Burkholderia thailandensis

ID or keywords:

Entry

Database: PDB / ID: 6cnz

Title

Crystal Structure of Chorismate Mutase from Burkholderia thailandensis

Components

Chorismate mutase

Keywords

ISOMERASE / SSGCID / Chorismate mutase / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease

Function / homology

Function and homology information

chorismate metabolic process / chorismate mutase / chorismate mutase activity
Similarity search - Function

Biological species

Burkholderia thailandensis (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.15 Å

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Citation

Journal: Acta Crystallogr F Struct Biol Commun / Year: 2018
Title: Crystal structure of chorismate mutase from Burkholderia thailandensis.
Authors: Asojo, O.A. / Dranow, D.M. / Serbzhinskiy, D. / Subramanian, S. / Staker, B. / Edwards, T.E. / Myler, P.J.

History

Deposition	Mar 9, 2018	Deposition site: RCSB / Processing site: RCSB
Supersession	Mar 21, 2018	ID: 4OJ7
Revision 1.0	Mar 21, 2018	Provider: repository / Type: Initial release
Revision 1.1	May 9, 2018	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2	May 16, 2018	Group: Data collection / Database references / Category: citation Item: _citation.journal_abbrev / _citation.journal_volume ..._citation.journal_abbrev / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.3	Oct 4, 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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Validation report

Summary document	6cnz_validation.pdf.gz	499.5 KB	Display	wwPDB validaton report
Full document	6cnz_full_validation.pdf.gz	504.7 KB	Display
Data in XML	6cnz_validation.xml.gz	39 KB	Display
Data in CIF	6cnz_validation.cif.gz	56.1 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/cn/6cnz ftp://data.pdbj.org/pub/pdb/validation_reports/cn/6cnz	HTTPS FTP

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Related structure data

Related structure data	2fp2S S: Starting model for refinement
Similar structure data	6axo-d 1xot-1 1y2j-1 6wkc-1 3hwo-1 1y2j-2 5jy4-2 1zle-d 6hwo-2 6q4s-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) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search
Other databases	TargetTrack: SSGCID-ButhA.00160.a

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#124 - Apr 2010 Concanavalin A and Circular Permutation similarity (1)

Deposited unit

A: Chorismate mutase

B: Chorismate mutase

C: Chorismate mutase

D: Chorismate mutase

E: Chorismate mutase

F: Chorismate mutase

hetero molecules

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

1

A: Chorismate mutase

E: Chorismate mutase

hetero molecules

defined by author&software
Evidence: gel filtration, monomer
39.1 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Chorismate mutase

C: Chorismate mutase

hetero molecules

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

3

D: Chorismate mutase

F: Chorismate mutase

hetero molecules

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

Unit cell

Length a, b, c (Å)	51.710, 121.380, 88.670
Angle α, β, γ (deg.)	90.000, 99.990, 90.000
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Chorismate mutase Mass: 19360.779 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Burkholderia thailandensis (bacteria) / Gene: AQ477_14105, CRX59_12655 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A0A1B4JXW9, chorismate mutase
#2: Chemical	ChemComp-NO3 / NITRATE ION Mass: 62.005 Da / Num. of mol.: 19 / Source method: obtained synthetically / Formula: NO₃
#3: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C₂H₆O₂
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 470 / 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: 2.36 Å³/Da / Density % sol: 47.86 %
Crystal grow	Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: ButhA.00160.a.B2.PS01793 at 20 mg/ml was setup 1:1 with 0.8 M lithium sulfate monohydrate and 0.1 M sodium acetate Crystals were cryoprotected with 20% ethylene glycol

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 21-ID-G / Wavelength: 0.97876 Å

Detector

Type: RAYONIX MX-300 / Detector: CCD / Date: Jun 5, 2013 / Details: Beryllium Lenses

Radiation

Monochromator: Diamond [111] / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.97876 Å / Relative weight: 1

Reflection

Resolution: 2.15→31.226 Å / Num. obs: 57764 / % possible obs: 98.7 % / Redundancy: 3.835 % / B_iso Wilson estimate: 31.91 Å² / CC_1/2: 0.999 / R_merge(I) obs: 0.052 / R_rim(I) all: 0.061 / Χ²: 0.971 / Net I/σ(I): 18.47 / Num. measured all: 221537 / Scaling rejects: 8

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Mean I/σ(I) obs	Num. measured obs	Num. possible	Num. unique obs	CC_1/2	R_rim(I) all	% possible all
2.15-2.21	3.889	0.461	2.78	16462	4295	4233	0.846	0.535	98.6
2.21-2.27	3.864	0.354	3.68	16073	4219	4160	0.906	0.411	98.6
2.27-2.33	3.879	0.287	4.51	15658	4079	4037	0.934	0.332	99
2.33-2.4	3.871	0.235	5.56	15145	3965	3912	0.954	0.273	98.7
2.4-2.48	3.869	0.198	6.54	14892	3894	3849	0.967	0.23	98.8
2.48-2.57	3.864	0.166	7.83	14056	3678	3638	0.976	0.193	98.9
2.57-2.67	3.851	0.139	9.29	13703	3606	3558	0.98	0.162	98.7
2.67-2.78	3.839	0.113	11.21	13173	3476	3431	0.988	0.131	98.7
2.78-2.9	3.827	0.09	13.68	12591	3333	3290	0.992	0.105	98.7
2.9-3.04	3.821	0.066	18.2	12030	3191	3148	0.996	0.077	98.7
3.04-3.21	3.817	0.051	23.36	11306	3004	2962	0.997	0.059	98.6
3.21-3.4	3.804	0.043	27.56	10711	2861	2816	0.998	0.05	98.4
3.4-3.63	3.789	0.035	33.32	10014	2685	2643	0.998	0.04	98.4
3.63-3.93	3.785	0.029	39.01	9361	2499	2473	0.999	0.034	99
3.93-4.3	3.81	0.027	42.5	8767	2333	2301	0.999	0.032	98.6
4.3-4.81	3.818	0.024	45.29	7858	2073	2058	0.999	0.028	99.3
4.81-5.55	3.824	0.024	44.68	7033	1852	1839	0.999	0.028	99.3
5.55-6.8	3.789	0.023	44.11	5930	1575	1565	0.999	0.027	99.4
6.8-9.62	3.753	0.018	52.76	4511	1214	1202	1	0.021	99
9.62-31.226	3.487	0.019	54.81	2263	686	649	0.999	0.022	94.6

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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: 2FP2

2fp2

Resolution: 2.15→31.226 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 22.94

	R_factor	Num. reflection	% reflection
R_free	0.216	1967	3.41 %
R_work	0.1644	-	-
obs	0.1662	57741	98.73 %

Solvent computation

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

Displacement parameters

B_iso max: 112.77 Å² / B_iso mean: 43.2133 Å² / B_iso min: 15.85 Å²

Refinement step

Cycle: final / Resolution: 2.15→31.226 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7216	0	104	470	7790
B_iso mean	-	-	60.21	42.46	-
Num. residues	-	-	-	-	964

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 14

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.15-2.2037	0.2761	139	0.2179	3941	4080	98
2.2037-2.2633	0.2471	147	0.1957	3955	4102	99
2.2633-2.3299	0.2554	133	0.187	3986	4119	99
2.3299-2.4051	0.2404	126	0.1789	3976	4102	99
2.4051-2.491	0.2539	136	0.1852	3997	4133	99
2.491-2.5907	0.2588	141	0.182	4002	4143	99
2.5907-2.7085	0.2489	153	0.1862	3948	4101	99
2.7085-2.8512	0.2688	154	0.1919	3962	4116	99
2.8512-3.0297	0.2584	138	0.1887	3991	4129	99
3.0297-3.2634	0.2455	141	0.1808	3972	4113	98
3.2634-3.5914	0.2246	131	0.172	3968	4099	98
3.5914-4.1101	0.1837	165	0.1405	3980	4145	99
4.1101-5.1745	0.1749	120	0.132	4053	4173	99
5.1745-31.2296	0.1604	143	0.141	4043	4186	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	5.9585	-1.024	-1.6802	0.9393	0.6659	1.3435	-0.1196	-0.1189	-0.6297	0.0304	0.0804	0.0166	0.1598	-0.0743	0.0462	0.2524	0.0105	-0.0001	0.2333	0.0108	0.2679	5.6503	-42.7379	-26.4727
2	8.2198	-0.386	-0.8733	1.3014	0.4235	1.4022	-0.3133	-0.7878	-0.1652	0.1828	0.2443	0.0048	0.0691	0.1234	0.0674	0.3213	0.0135	-0.0148	0.2882	0.032	0.2398	7.325	-39.0409	-20.4507
3	6.5257	3.6786	0.0411	5.0312	0.4311	1.7815	-0.2571	0.4627	0.586	-0.2116	0.2327	0.8747	-0.1816	-0.238	-0.0264	0.2722	0.0045	-0.019	0.3022	0.0602	0.414	-8.3775	-29.0576	-29.6175
4	5.6596	2.4371	-2.7543	7.9663	-0.2098	4.0595	-0.2968	0.7596	-0.2323	-0.3627	0.3071	-0.2326	-0.0434	-0.0955	0.0641	0.2339	0.0166	-0.046	0.2734	0.032	0.1501	0.4469	-33.702	-32.7243
5	2.5046	1.3956	-0.6137	5.1748	-2.7524	2.2986	0.1689	-0.0095	0.1245	0.1334	-0.0215	0.2061	-0.0625	0.1077	-0.1817	0.1727	0.0038	0.0197	0.1888	-0.0014	0.1795	-13.0254	-1.6299	-45.361
6	3.4622	1.5109	-1.1318	7.7276	-4.0889	3.8626	0.0953	-0.5506	0.0016	0.8726	-0.1749	0.0025	-0.5642	0.048	0.1174	0.3384	-0.0588	-0.0599	0.3924	0.009	0.3588	-0.6447	-5.8122	-35.0154
7	1.7148	-0.0299	0.4159	1.9733	-0.9817	2.1102	0.0717	0.1417	0.0606	-0.1686	-0.0047	0.1684	-0.091	-0.0125	-0.0387	0.175	-0.0342	0.011	0.1699	0.0212	0.2517	-9.9679	1.2858	-48.3531
8	2.2579	-1.1321	1.1696	9.884	-1.9724	3.0976	0.0236	-0.2787	0.0443	0.7405	0.1751	-0.3351	-0.1592	-0.1302	-0.1769	0.2031	-0.0173	-0.0025	0.2721	-0.0196	0.3073	-11.0261	-8.8123	-36.0732
9	2.9085	-2.9774	-0.4299	3.2402	0.7167	2.6816	-0.0469	-0.05	0.0014	-0.2352	0.1215	-0.663	0.5926	0.3869	-0.4523	0.7313	0.382	-0.2741	0.1435	-0.1789	0.6452	-4.2161	-26.6253	-44.6747
10	2.4071	0.4031	-2.455	6.0384	4.5885	6.7192	-0.2241	0.329	-0.4253	0.3269	0.2293	0.4693	0.6681	-0.2949	-0.023	0.2648	-0.0686	-0.0502	0.2386	0.0189	0.3211	-17.2438	-19.334	-50.0169
11	4.2583	3.3776	0.5016	6.5897	-0.3344	2.3095	0.3352	0.5107	-0.2243	-0.7849	-0.0487	0.6086	0.2265	0.2039	-0.3187	0.2837	0.008	-0.0198	0.2693	-0.0099	0.2755	-11.3161	-11.1512	-51.5487
12	1.4883	-0.5609	0.159	5.6029	2.3589	2.0712	-0.0411	-0.0882	0.076	0.1671	0.1312	-0.0768	-0.0929	0.0169	-0.1	0.2415	-0.026	0.0427	0.2161	-0.0032	0.2267	-28.062	-0.652	-36.4865
13	1.9871	-1.6554	-1.6614	5.2191	5.6074	6.2861	0.1378	0.3709	-0.0315	-1.1945	-0.2145	0.3101	-0.6677	-0.18	0.1113	0.2971	0.0281	-0.0589	0.2393	-0.0113	0.2716	-40.2358	-4.7736	-47.0841
14	1.8577	1.334	1.2023	3.3956	2.3568	2.6127	-0.0199	-0.1715	-0.1112	0.038	0.0391	0.078	-0.2933	-0.1333	0.0135	0.2728	0.0165	0.0294	0.1865	0.0089	0.2652	-34.192	-2.0324	-32.7296
15	4.4197	0.4371	-5.8849	2.8351	-0.3252	7.8543	0.4567	-0.2006	0.2672	0.0028	0.2485	-0.3432	-0.4006	1.1758	-0.5902	0.3098	-0.0021	-0.0255	0.2366	-0.0615	0.4159	-22.3565	11.056	-34.7194
16	2.6231	2.1553	0.8691	7.2903	2.8673	2.9975	-0.0394	0.1667	0.0804	-0.313	0.2037	0.1528	-0.2453	-0.0678	-0.1487	0.161	0.0202	-0.0158	0.2049	0.0133	0.2134	-30.3664	-8.3106	-45.907
17	0.3996	0.6428	1.2227	1.0323	1.9582	3.7248	-0.2015	-0.2245	-1.0753	-0.2418	1.1892	0.908	0.7327	-0.4481	-0.7522	0.4794	-0.133	-0.1127	0.2824	0.1331	0.8036	-37.4199	-26.0808	-37.9731
18	8.4324	0.1857	1.8798	5.0296	0.2505	7.1703	0.0479	0.1836	-0.5818	0.4676	0.2594	-0.1566	0.4891	0.45	-0.3107	0.236	0.0509	-0.0262	0.1982	-0.0193	0.2777	-24.6119	-18.9976	-32.3271
19	8.7248	-6.3409	6.4958	5.0798	-5.2539	5.4365	-1.1359	-0.7588	0.3966	1.1281	0.3517	-1.2506	-0.9639	0.2635	0.5054	0.5306	-0.004	-0.0947	0.3327	0.0056	0.4689	-26.4701	-8.3339	-28.4069
20	2.0693	2.0418	-0.3965	3.1725	2.4891	7.1597	0.316	-1.0657	-1.2925	1.2846	-0.3685	1.722	0.8792	-0.525	0.0206	0.3285	-0.0683	0.0799	0.2783	0.1348	0.6249	-37.5317	-18.2457	-33.5559
21	8.4909	4.4043	-1.1723	3.5926	-1.0469	2.1202	-0.009	0.2559	-0.339	0.2217	0.2358	-0.2815	0.046	0.3254	-0.2441	0.3271	0.0179	-0.0163	0.2611	-0.0701	0.2431	9.0856	-35.0432	-65.034
22	7.7388	4.4673	-1.501	2.7501	-1.4923	2.306	-0.846	1.2771	-1.6189	-0.6936	0.2804	-0.4979	0.6504	0.3028	0.4618	0.6008	-0.0031	0.1999	0.5425	-0.2268	0.8377	22.2352	-44.4633	-69.741
23	2.7967	-0.3488	-3.2708	1.6865	0.4532	4.2482	0.0316	-0.8658	-0.6334	0.3563	0.0934	-0.346	0.2514	0.6083	-0.0978	0.4109	-0.0427	-0.0742	0.3014	-0.0334	0.3351	12.3039	-38.5021	-59.112
24	4.3692	2.0058	2.7365	3.5946	-1.7416	5.6514	-0.2896	0.8393	-0.1764	0.0646	-0.1342	0.305	-0.4522	-0.6367	0.3692	0.2139	-0.0318	-0.0237	0.1934	-0.0107	0.2215	-3.0597	-36.8159	-67.6739
25	3.3973	3.4251	3.0092	4.1576	3.3785	4.5946	-0.1813	1.2786	-0.7511	-0.0416	0.5993	-0.5422	-0.0491	1.1176	-0.2678	0.3737	-0.0372	0.0221	0.6728	-0.1447	0.3991	21.1326	-34.0944	-70.5485
26	6.4731	-2.1348	1.4262	2.0297	-0.0275	2.1355	-0.034	0.1905	0.5572	0.0166	0.0804	-0.4096	-0.2534	0.4823	-0.0609	0.4276	-0.119	0.0007	0.4265	-0.1433	0.4034	22.8798	-21.3726	-59.1181
27	4.8167	-2.3637	-1.2289	5.5522	0.154	4.3721	0.048	-0.5879	-0.1619	0.239	-0.0116	0.0674	-0.1267	0.0525	0.0534	0.4454	-0.0936	-0.0921	0.3671	-0.0837	0.3783	15.6825	-29.0215	-56.9995
28	4.7735	0.1528	2.5655	1.5965	-0.006	2.7737	0.1619	-0.4313	0.281	0.0789	-0.2112	-0.1087	-0.1606	0.1932	0.0463	0.3204	-0.0104	-0.0001	0.4547	-0.009	0.223	11.8219	-26.2616	-12.5912
29	4.5347	-1.8675	1.9317	4.7125	-2.5436	3.2484	-0.0976	-0.506	0.5295	0.2424	-0.1783	-0.0171	-0.5996	0.2579	0.3067	0.4589	-0.0501	-0.0361	0.4512	-0.1258	0.3001	12.4854	-16.7819	-11.6886
30	6.6804	-2.4141	1.3573	5.5107	-1.1493	3.2118	0.0296	0.2974	0.0369	0.0277	-0.2046	0.051	-0.0465	0.2308	0.1623	0.4128	-0.0399	-0.0121	0.3146	-0.092	0.2452	11.0664	-23.7555	-17.5863
31	3.5605	1.6186	0.5093	4.453	-0.2783	3.5328	0.1075	-0.8358	0.2336	0.7518	0.0813	0.1684	-0.1395	-0.446	-0.136	0.4204	0.0314	0.1033	0.5378	-0.0442	0.2651	-2.5297	-24.3647	-8.9639
32	3.7736	1.8753	2.5683	3.4892	2.0982	5.4465	-0.023	0.3059	0.3638	-0.2469	0.1659	0.1642	-0.8862	-0.3803	-0.1382	0.4063	-0.0124	0.0295	0.5421	0.0954	0.2307	3.7109	-24.0525	-78.6924
33	2.7295	0.0313	1.2999	6.6112	2.4655	4.3963	-0.2106	-0.1866	0.721	-0.1893	-0.1652	0.0278	-1.2084	-0.6838	0.3814	0.7157	0.0806	-0.1039	0.6048	0.0521	0.449	2.5636	-14.9604	-78.8683
34	2.0157	-0.4195	0.0002	2.9288	-0.1581	2.9863	-0.4516	0.1754	0.4454	-0.0727	0.2995	0.0473	-0.8542	0.0902	0.0932	0.5098	-0.0434	0.0036	0.455	0.0672	0.2422	4.5525	-21.4606	-73.0207
35	5.3523	-1.1095	0.7716	6.0209	-0.5883	4.7705	-0.0965	0.8033	0.46	-0.5371	0.2856	-0.3293	-0.6092	0.6931	-0.2061	0.6222	-0.1689	0.1005	0.772	0.0596	0.3756	18.57	-18.2573	-80.1943

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 35 through 118 )	A	35 - 118
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 119 through 154 )	A	119 - 154
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 155 through 175 )	A	155 - 175
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 176 through 195 )	A	176 - 195
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 33 through 69 )	B	33 - 69
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 70 through 90 )	B	70 - 90
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 91 through 132 )	B	91 - 132
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 133 through 154 )	B	133 - 154
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 155 through 159 )	B	155 - 159
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 160 through 175 )	B	160 - 175
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 176 through 194 )	B	176 - 194
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 35 through 69 )	C	35 - 69
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 70 through 90 )	C	70 - 90
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 91 through 118 )	C	91 - 118
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 119 through 132 )	C	119 - 132
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 133 through 154 )	C	133 - 154
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 155 through 159 )	C	155 - 159
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 160 through 175 )	C	160 - 175
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 176 through 189 )	C	176 - 189
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 190 through 197 )	C	190 - 197
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 35 through 69 )	D	35 - 69
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 70 through 90 )	D	70 - 90
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 91 through 118 )	D	91 - 118
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 119 through 132 )	D	119 - 132
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 133 through 156 )	D	133 - 156
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 157 through 175 )	D	157 - 175
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 176 through 194 )	D	176 - 194
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 34 through 69 )	E	34 - 69
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 70 through 118 )	E	70 - 118
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 119 through 156 )	E	119 - 156
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 157 through 193 )	E	157 - 193
32	X-RAY DIFFRACTION	32	chain 'F' and (resid 36 through 69 )	F	36 - 69
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 70 through 118 )	F	70 - 118
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 119 through 156 )	F	119 - 156
35	X-RAY DIFFRACTION	35	chain 'F' and (resid 157 through 193 )	F	157 - 193

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