PDB-7cvt: Crystal structure of the C85A/L194A/H234C mutant CLC-ec1 with Fab...

ID or keywords:

Entry

Database: PDB / ID: 7cvt

Title

Crystal structure of the C85A/L194A/H234C mutant CLC-ec1 with Fab fragment

Components

H(+)/Cl(-) exchange transporter ClcA
antibody Fab fragment heavy chain
antibody Fab fragment light chain

Keywords

TRANSPORT PROTEIN / CLC /

Chloride / Dimer interface

Function / homology

Chloride channel, ClcA /

Chloride channel, voltage gated /

Chloride channel, core /

Voltage gated chloride channel / voltage-gated chloride channel activity /

antiporter activity / chloride transmembrane transporter activity / plasma membrane => GO:0005886 / H(+)/Cl(-) exchange transporter ClcA

Function and homology information

Biological species

Escherichia coli MS 198-1 (bacteria)

Mus musculus (house mouse)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.9 Å

Authors

Park, K. / Mersch, K. / Robertson, J. / Lim, H.-H.

Funding support

Korea, Republic Of, 1items

Citation

Journal: J.Mol.Biol. / Year: 2021
Title: Altering CLC stoichiometry by reducing non-polar side-chains at the dimerization interface.
Authors: Mersch, K. / Ozturk, T.N. / Park, K. / Lim, H.H. / Robertson, J.L.

History

Deposition	Aug 27, 2020	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Sep 1, 2021	Provider: repository / Type: Initial release
Revision 1.1	Mar 16, 2022	Group: 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.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2	Nov 29, 2023	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/cv/7cvt ftp://data.pdbj.org/pub/pdb/validation_reports/cv/7cvt	HTTPS FTP

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Related structure data

Related structure data	7cvsC 4eneS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	7cvs-d 2ht2-d 4kka-d 4kjp-d 4kk6-d 6ad8-d 2htk-d 4kkc-d 4kjw-d 2r9h-d 4mqx-d 5hd8-d 4kkl-d 2ht3-d 4kk9-d 4kjq-d 4fg6-d 6k5f-d 3det-d 6k5a-d Search similar-shape structures by Omokage search (details) 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	#21 - Sep 2001 Antibodies similarity (1) #256 - Apr 2021 SARS-CoV-2 Spike and Antibodies similarity (1)

Deposited unit

A: H(+)/Cl(-) exchange transporter ClcA

B: H(+)/Cl(-) exchange transporter ClcA

C: antibody Fab fragment heavy chain

D: antibody Fab fragment light chain

E: antibody Fab fragment heavy chain

F: antibody Fab fragment light chain

hetero molecules

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

1

Idetical with deposited unit
defined by author
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	233.034, 98.305, 172.434
Angle α, β, γ (deg.)	90.00, 131.99, 90.00
Int Tables number	5
Space group name H-M	C121

#1: Protein	H(+)/Cl(-) exchange transporter ClcA Mass: 50281.254 Da / Num. of mol.: 2 / Mutation: C85A, L194A, H234C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli MS 198-1 (bacteria) / Gene: clcA, eriC, HMPREF9552_04837 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: D7XDR7
#2: Antibody	antibody Fab fragment heavy chain Mass: 23823.031 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse)
#3: Antibody	antibody Fab fragment light chain Mass: 23088.443 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse)
#4: Chemical	ChemComp-CL / CHLORIDE ION / Chloride Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl / Feature type: SUBJECT OF INVESTIGATION
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: 3.78 Å³/Da / Density % sol: 67.43 %
Crystal grow	Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 9.5 Details: 25% (w/v) PEG 400 100mM Glycine, pH 9.5 100mM Li2NO3

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Data collection

Diffraction	Mean temperature: 77.36 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 5C (4A) / Wavelength: 1 Å
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 27, 2018
Radiation	Monochromator: DCM Si (111) Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1 Å / Relative weight: 1
Reflection	Resolution: 2.9→50 Å / Num. obs: 63778 / % possible obs: 98.9 % / Redundancy: 5 % / CC_1/2: 0.98 / R_merge(I) obs: 0.126 / Net I/σ(I): 36.4
Reflection shell	Resolution: 2.9→2.95 Å / Redundancy: 4.7 % / R_merge(I) obs: 2.064 / Mean I/σ(I) obs: 1.87 / Num. unique obs: 3059 / CC_1/2: 0.516 / % possible all: 96

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Processing

Software

Name	Version	Classification
PHENIX	(1.13_2998: ???)	refinement
HKL-2000		data reduction
HKL-2000		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 4ENE

4ene

Resolution: 2.9→50 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 27.42 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2409	3294	5.17 %	random
R_work	0.2006	-	-	-
obs	0.2026	63725	98.96 %	-

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 2.9→50 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13245	0	3	0	13248

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.006	13571
X-RAY DIFFRACTION	f_angle_d	0.965	18478
X-RAY DIFFRACTION	f_dihedral_angle_d	6.207	7932
X-RAY DIFFRACTION	f_chiral_restr	0.05	2123
X-RAY DIFFRACTION	f_plane_restr	0.006	2320

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 (%)
2.9-2.9499	0.3567	178	0.3192	2881	X-RAY DIFFRACTION	96
2.9499-3.0035	0.3321	164	0.3147	3046	X-RAY DIFFRACTION	100
3.0035-3.0613	0.3354	157	0.2757	3042	X-RAY DIFFRACTION	100
3.0613-3.1237	0.297	155	0.2656	3036	X-RAY DIFFRACTION	100
3.1237-3.1916	0.3096	191	0.2521	3019	X-RAY DIFFRACTION	100
3.1916-3.2658	0.2976	169	0.2614	3018	X-RAY DIFFRACTION	100
3.2658-3.3474	0.3097	161	0.2527	3036	X-RAY DIFFRACTION	100
3.3474-3.4378	0.3153	142	0.2486	3058	X-RAY DIFFRACTION	100
3.4378-3.5388	0.2832	204	0.2264	3001	X-RAY DIFFRACTION	100
3.5388-3.6529	0.3192	190	0.2195	3005	X-RAY DIFFRACTION	100
3.6529-3.7834	0.2435	160	0.2083	3062	X-RAY DIFFRACTION	100
3.7834-3.9346	0.2827	120	0.1967	3099	X-RAY DIFFRACTION	100
3.9346-4.1134	0.2563	179	0.1901	3016	X-RAY DIFFRACTION	100
4.1134-4.3299	0.2077	173	0.1737	3048	X-RAY DIFFRACTION	100
4.3299-4.6006	0.2095	160	0.1594	3057	X-RAY DIFFRACTION	100
4.6006-4.9548	0.2064	161	0.1633	3077	X-RAY DIFFRACTION	100
4.9548-5.4517	0.2112	164	0.1688	3049	X-RAY DIFFRACTION	100
5.4517-6.2364	0.2406	160	0.1968	3098	X-RAY DIFFRACTION	100
6.2364-7.8417	0.228	158	0.1974	3076	X-RAY DIFFRACTION	100
7.8417-50	0.1977	148	0.2064	2707	X-RAY DIFFRACTION	85

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	0.6096	0.2013	-0.3984	1.9811	1.0231	2.9484	-0.1856	-0.295	-0.531	-0.2896	-0.0365	-0.1549	0.3316	0.3879	0.2151	0.7152	0.3029	0.0818	1.0468	-0.0673	0.9819	161.5539	-4.3403	142.1202
2	1.6164	-0.1775	-0.0405	2.3469	-0.0801	2.6892	-0.1893	-1.1609	-1.3136	0.1938	0.0708	-0.1546	0.5871	0.7663	0.0875	0.7844	0.319	0.0601	1.2246	0.1744	1.0216	164.1314	-4.5405	154.8143
3	6.3338	0.5816	-0.0357	0.3892	0.2103	0.0331	-0.0466	-0.1569	-0.1497	0.1511	0.0896	0.2897	-0.1902	-0.288	0.006	0.9828	0.2749	0.0218	1.0659	-0.0053	0.9788	151.3265	8.5203	151.3329
4	1.4828	0.7998	-0.2946	0.6686	-1.2139	3.0056	0.0172	0.4729	-1.1275	-0.5853	-0.0862	0.7022	0.3125	-0.199	0.0152	0.9562	0.1727	-0.0175	0.5987	-0.0226	1.0432	143.6401	-12.7664	139.5123
5	0.3555	0.7764	-0.8481	1.9879	-0.8961	2.6439	-0.0497	0.0693	-0.5578	-0.1728	0.029	0.2544	0.0913	-0.2015	0.0144	0.6256	0.2711	-0.0141	0.7468	-0.0002	1.0111	138.1513	-6.8457	146.6638
6	2.5147	-1.0527	-0.1608	1.9346	0.5025	1.8044	-0.7077	-0.5246	-0.5835	0.2597	0.7534	0.044	0.6364	0.42	0.0121	0.7747	0.2533	0.0853	0.8711	0.1047	1.205	148.9853	-16.2817	154.2691
7	2.6386	-0.5681	-1.4457	1.6341	-0.5353	3.6629	-0.1327	-0.8533	-0.2946	0.2177	0.4806	0.128	-0.0352	0.0244	-0.2173	0.8264	0.2038	0.0171	1.1254	0.3479	1.0464	141.6371	-7.533	174.7242
8	1.8076	0.0326	-0.0252	2.7885	0.8089	2.2012	-0.0217	-1.5388	-0.9853	1.3563	0.4089	-0.2551	-0.4762	0.0699	0.8325	1.8267	0.7047	0.3313	1.8635	0.5945	0.3568	144.0445	5.7834	193.5475
9	0.7954	0.2213	0.8366	1.3476	-0.7086	2.3513	-0.6037	-1.3204	-0.8263	0.7237	0.6585	-0.2064	0.5097	0.4461	0.0106	1.1389	0.5489	0.1502	1.4372	0.4868	1.0459	146.1312	-6.5484	180.1164
10	0.8772	1.4356	-0.0638	3.7066	-1.6852	1.3073	-0.0661	-0.3145	0.1709	0.1892	0.0824	0.4062	-0.3294	-0.0531	-0.0946	1.032	0.3575	0.0609	1.1514	0.2543	0.8866	137.173	3.2857	167.5236
11	-0.0512	0.1379	-0.287	1.803	-0.6261	3.5439	-0.3175	-0.6952	0.0545	0.7998	0.1151	-0.1155	-0.7845	-0.3207	0.1438	1.149	0.4196	-0.1507	1.2924	0.0194	0.6712	153.1766	15.259	177.0116
12	4.7778	-0.8436	0.2365	2.9352	-0.663	0.9679	-0.4053	0.0808	0.6042	-0.4754	-0.266	-0.0568	-0.6066	-0.0448	0.6771	0.952	0.1565	-0.111	0.877	-0.1119	1.0019	104.1171	21.6649	150.4232
13	2.4485	-1.4353	1.1606	4.2262	-1.1631	3.7633	-0.421	-0.4948	-0.4595	0.1735	0.0291	-0.0617	-0.1241	0.6271	0.2648	0.601	0.2313	-0.0137	0.906	0.0757	0.8879	112.1023	12.3293	152.2041
14	9.3941	1.8863	1.6025	4.3974	-0.9222	8.3926	-0.0175	1.4202	-1.1923	-0.912	-0.5995	0.263	0.429	1.3104	0.536	0.8127	0.3801	0.0245	1.1987	-0.0723	0.9123	108.2258	8.4822	143.8938
15	7.3485	-1.8551	-0.2013	1.8655	-0.8273	4.1479	0.2308	0.7247	-1.1686	-0.2904	-0.5782	-0.3242	-0.0012	0.8873	0.2728	0.8335	0.2982	-0.1071	1.2254	-0.0093	0.7574	105.6674	15.5406	145.442
16	4.3856	-2.2235	-0.1404	1.7887	-0.842	1.4827	-0.3258	-0.5448	-0.4389	-0.0517	0.0982	0.2511	0.0021	0.1117	0.3122	0.6627	0.2004	-0.0698	0.8097	0.0424	0.8302	106.2396	14.7467	156.4923
17	2.6103	-0.3175	1.7009	1.665	-0.9788	3.7743	-0.7017	-0.4089	0.6034	0.5121	-0.5464	0.7619	0.2355	-1.0488	0.0871	0.8741	0.3628	0.0866	1.3896	-0.6596	0.9541	75.5291	38.3523	169.8576
18	1.6654	-0.7096	-1.3076	0.5409	0.0502	2.6918	-0.619	-1.75	0.2066	0.9014	0.1701	-0.4752	-0.0728	0.9579	0.572	0.9975	0.3838	-0.0582	1.5983	-0.2461	0.8003	87.2749	32.6216	165.1978
19	0.7335	1.706	1.3525	5.1729	4.3697	6.7198	-0.6646	-1.6527	-0.1386	0.5696	1.002	1.0672	-0.0455	-0.6052	0.6022	0.8389	0.4697	0.0684	1.1714	-0.1953	0.6218	82.9322	28.227	162.3322
20	2.1226	0.4299	-3.5815	2.5192	-0.1975	6.1291	-0.2982	-1.354	0.6306	1.0149	-0.6425	0.2693	-1.0577	-0.2726	0.2285	1.144	0.3463	-0.2559	1.7723	-0.5251	0.7884	86.3951	41.2681	166.8813
21	6.5945	-2.7504	-5.8568	3.9779	2.65	9.72	-0.2359	0.1443	1.4861	0.5266	0.2023	-0.0681	-0.3772	-0.0809	0.1627	0.9843	0.1309	-0.127	1.0643	-0.3094	1.0492	82.273	42.4948	161.8684
22	2.5514	-0.7527	-0.7607	3.708	1.5884	2.1618	-0.2425	-1.3922	-0.9373	1.4097	-0.1157	0.3973	0.0803	-2.5056	0.3265	0.9602	0.4769	0.1859	1.729	0.6224	1.3266	99.1436	3.0755	174.1551
23	1.9815	0.306	-0.1159	3.5162	-0.4055	3.8006	-0.4327	-1.3676	-1.2025	0.9143	0.4016	-0.4073	-0.0766	0.1938	0.1449	0.862	0.5487	0.0638	1.6813	0.3814	1.2033	109.5913	6.2549	172.0143
24	1.8533	-0.5976	-1.3161	0.5523	0.9355	1.5238	-0.5012	-1.5186	-0.8342	0.2674	0.2822	0.566	-0.0699	-0.5807	0.1135	1.0206	0.5564	0.0371	1.81	0.3295	1.1154	100.5561	9.4583	172.3212
25	1.4756	-0.2046	0.8532	3.1841	-0.3084	2.8735	-0.3395	-0.7192	-0.3766	0.0129	0.4093	0.4954	0.3064	-0.228	-0.1329	0.912	0.4987	0.0419	1.5598	0.1118	0.9596	73.0033	25.84	169.5446
26	3.401	-0.6178	0.3748	8.3215	-1.1625	1.9999	-0.2606	-0.2271	0.6549	-0.2606	-0.1488	0.2424	-0.6865	-0.3086	0.5193	1.126	-0.0856	0.0785	0.8373	-0.1141	1.1296	132.042	44.6417	141.8975
27	3.695	1.9211	-0.7063	2.2571	2.1617	5.6071	-0.0197	0.3631	-0.9927	0.7935	-0.5197	0.7114	-0.1536	-1.0986	0.5195	1.0449	0.0306	0.0866	0.6258	-0.1031	0.915	135.1645	31.1057	147.5029
28	4.5655	-1.0967	-0.4128	3.8093	-0.3893	4.0792	-0.4482	-0.5692	0.5884	0.7571	0.1985	-0.0093	-0.694	-0.0475	0.1974	0.9327	0.0291	-0.0125	0.4808	-0.0338	0.6872	140.2434	40.4055	149.8943
29	2.2612	-0.0195	0.3359	0.322	-0.9341	1.9669	-0.0854	0.0366	0.3302	-0.2309	-0.0172	0.1322	-0.0895	-0.0865	0.0896	1.0189	-0.0561	-0.0922	0.5731	-0.0085	0.8145	138.6522	42.6886	139.1722
30	4.265	-1.7271	-0.6546	5.8599	0.0622	0.1166	0.156	1.0186	0.1304	-1.0494	0.1716	-0.1403	-0.8326	0.4394	-0.024	0.8057	0.0417	-0.0653	0.9001	0.15	0.8635	127.2362	47.3138	109.2286
31	3.8761	0.1642	-0.6391	4.262	-0.0168	4.5209	-0.3798	0.6585	0.4934	0.5735	0.4724	-0.6047	0.0363	0.124	0.0526	0.7498	-0.0016	-0.0778	0.5999	0.0705	0.7863	131.1047	46.3347	120.739
32	3.0762	-0.3615	-0.0161	3.6239	2.1665	7.7658	0.0076	0.4641	-0.4009	0.0486	0.0181	0.8543	0.9848	-1.4103	-0.27	0.9092	-0.1416	-0.092	0.8889	0.0558	0.9993	121.0269	43.1979	116.1525
33	1.8766	0.1822	-0.4791	1.7472	-0.5476	4.2655	-0.3462	0.2634	0.0755	0.3356	0.0658	-0.3238	-0.0881	0.6967	0.2138	0.8107	-0.1418	-0.1768	0.6941	0.0666	0.8098	156.8018	33.0503	132.7688
34	2.5351	-0.8874	0.4741	1.4449	-0.8018	2.6914	-0.5495	0.3478	0.0975	0.1505	0.3701	-0.7269	-0.5004	0.7889	0.2727	0.9618	-0.2172	-0.1058	0.6385	0.0377	0.7329	153.8905	35.7112	134.382
35	1.3213	-0.7815	0.5672	1.5497	-0.542	1.1818	-0.0676	-0.1466	0.331	-0.4933	0.2996	0.2822	-0.4415	-0.3046	-0.0979	1.0551	-0.1078	-0.137	0.9253	0.2269	0.938	136.2296	49.1865	111.5857
36	2.8336	-1.917	0.1568	3.6196	0.5044	0.8042	0.2166	0.6279	1.0409	0.2345	-0.0337	-0.4907	-1.108	0.7453	0.0865	1.0434	-0.2218	0.223	0.63	0.5929	1.2685	139.9925	53.466	109.1553
37	3.8378	-0.8939	0.2041	3.886	-1.111	3.3786	-0.3554	-0.0219	0.377	0.4505	0.4967	-0.3299	-0.9666	-0.558	-0.1445	1.1047	-0.2453	-0.0735	1.0572	0.2699	0.8423	141.5147	52.3135	113.1441
38	2.729	-0.2976	0.061	3.2764	-0.5897	4.9299	0.5905	1.1685	1.9881	-1.7456	-0.6992	-0.1623	-2.5021	-1.2399	-0.0077	1.9013	0.1302	-0.257	0.9107	0.3852	1.322	130.7112	62.6543	108.0024
39	2.1234	-0.3334	1.2367	1.8881	-0.79	2.0789	0.3772	1.0618	0.5945	-0.4523	-0.5913	-0.6639	-1.5773	0.1525	0.2764	1.2229	0.194	0.0757	1.4243	0.3386	0.8973	138.4176	54.3024	100.4013

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 17 through 146 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 147 through 214 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 215 through 248 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 249 through 329 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 330 through 418 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 419 through 460 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 17 through 70 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 71 through 123 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 124 through 214 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 215 through 248 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 249 through 458 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 1 through 17 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 18 through 60 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 61 through 73 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 74 through 91 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 92 through 127 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 128 through 142 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 143 through 176 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 177 through 192 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 193 through 210 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 211 through 222 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 1 through 25 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 26 through 74 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 75 through 112 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 113 through 211 )
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 2 through 17 )
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 18 through 33 )
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 34 through 83 )
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 84 through 132 )
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 133 through 153 )
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 154 through 192 )
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 193 through 222 )
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 1 through 74 )
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 75 through 101 )
35	X-RAY DIFFRACTION	35	chain 'F' and (resid 102 through 127 )
36	X-RAY DIFFRACTION	36	chain 'F' and (resid 128 through 149 )
37	X-RAY DIFFRACTION	37	chain 'F' and (resid 150 through 173 )
38	X-RAY DIFFRACTION	38	chain 'F' and (resid 174 through 196 )
39	X-RAY DIFFRACTION	39	chain 'F' and (resid 197 through 211 )

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