PDB-5ds6: Crystal structure the Escherichia coli Cas1-Cas2 complex bound to...

ID or keywords:

Entry

Database: PDB / ID: 5ds6

Title

Crystal structure the Escherichia coli Cas1-Cas2 complex bound to protospacer DNA with splayed ends

Components

CRISPR-associated endonuclease Cas1
CRISPR-associated endoribonuclease Cas2
DNA (28-MER)
DNA (29-MER)

Keywords

Hydrolase/DNA / Adaptive Immunity / CRISPR-Associated Proteins / CRISPR-Cas Systems / Clustered Regularly Interspaced Short Palindromic Repeats / Integrases / Endodeoxyribonucleases / Endonucleases / DNA binding protein / Hydrolase-DNA complex

Function / homology

Function and homology information

CRISPR-cas system / crossover junction DNA endonuclease activity / 5'-flap endonuclease activity / maintenance of CRISPR repeat elements / endonuclease activity / defense response to virus / Hydrolases; Acting on ester bonds / DNA repair / DNA damage response / protein homodimerization activity ...
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Enterobacteria phage M13 (virus)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.352 Å

Authors

Nunez, J.K. / Harrington, L.B. / Kranzusch, P.J. / Engelman, A.N. / Doudna, J.A.

Funding support

United States, 1items

Citation

Journal: Nature / Year: 2015
Title: Foreign DNA capture during CRISPR-Cas adaptive immunity.
Authors: Nunez, J.K. / Harrington, L.B. / Kranzusch, P.J. / Engelman, A.N. / Doudna, J.A.

History

Deposition	Sep 16, 2015	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Oct 28, 2015	Provider: repository / Type: Initial release
Revision 1.1	Nov 11, 2015	Group: Database references
Revision 1.2	Dec 9, 2015	Group: Database references
Revision 1.3	Apr 6, 2016	Group: Source and taxonomy
Revision 1.4	Nov 20, 2019	Group: Author supporting evidence / Derived calculations / Category: pdbx_audit_support / pdbx_struct_oper_list Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.5	Sep 27, 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	5ds6.cif.gz	552.4 KB	Display	PDBx/mmCIF format
PDB format	pdb5ds6.ent.gz	456 KB	Display	PDB format
PDBx/mmJSON format	5ds6.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	5ds6_validation.pdf.gz	486.7 KB	Display	wwPDB validaton report
Full document	5ds6_full_validation.pdf.gz	501.4 KB	Display
Data in XML	5ds6_validation.xml.gz	42.7 KB	Display
Data in CIF	5ds6_validation.cif.gz	58 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ds/5ds6 ftp://data.pdbj.org/pub/pdb/validation_reports/ds/5ds6	HTTPS FTP

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Related structure data

Related structure data	5ds4C 5ds5C 4p6iS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	5ds4-d 5ds5-d 3wev-d 2ymw-d 5vvl-d 4hk7-d 5dqz-d 4jbs-d 2i4n-d 1ibr-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
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PDB pages

PDBj /

wwPDB /

NCBI

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Deposited unit

A: CRISPR-associated endonuclease Cas1

B: CRISPR-associated endonuclease Cas1

C: CRISPR-associated endonuclease Cas1

D: CRISPR-associated endonuclease Cas1

E: CRISPR-associated endoribonuclease Cas2

F: CRISPR-associated endoribonuclease Cas2

G: DNA (29-MER)

H: DNA (28-MER)

177 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	88.020, 123.006, 196.012
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

#1: Protein	CRISPR-associated endonuclease Cas1 Mass: 33322.496 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (strain K12) (bacteria) Strain: K12 / Gene: ygbT, cas1, b2755, JW2725 / Production host: Escherichia coli (E. coli) References: UniProt: Q46896, Hydrolases; Acting on ester bonds
#2: Protein	CRISPR-associated endoribonuclease Cas2 Mass: 11684.466 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (strain K12) (bacteria) Strain: K12 / Gene: ygbF, cas2, b2754, JW5438 / Production host: Escherichia coli (E. coli) References: UniProt: P45956, Hydrolases; Acting on ester bonds
#3: DNA chain	DNA (29-MER) Mass: 10180.602 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Enterobacteria phage M13 (virus)
#4: DNA chain	DNA (28-MER) Mass: 10067.478 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Enterobacteria phage M13 (virus)

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Experiment

Experiment	Method: X-RAY DIFFRACTION

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Sample preparation

Crystal	Density Matthews: 3 Å³/Da / Density % sol: 58.99 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 100 mM sodium citrate tribasic pH 5.6, 200 mM sodium acetate and 8% PEG 8000 (w/v)

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Data collection

Diffraction	Mean temperature: 80 K
Diffraction source	Source: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11587 Å
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 15, 2015
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.11587 Å / Relative weight: 1
Reflection	Resolution: 3.35→49.003 Å / Num. obs: 31049 / % possible obs: 99.6 % / Redundancy: 4.1 % / R_merge(I) obs: 0.216 / Net I/σ(I): 5
Reflection shell	Resolution: 3.35→3.42 Å / Redundancy: 4 % / R_merge(I) obs: 0.943 / Mean I/σ(I) obs: 1.3 / % possible all: 97.7

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Processing

Software

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

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 4P6I

4p6i

Resolution: 3.352→49.003 Å / SU ML: 0.5 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.89 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2751	1729	5.58 %	10
R_work	0.2309	-	-	-
obs	0.2333	30989	99.08 %	-

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 3.352→49.003 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9376	1165	0	0	10541

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.003	10851
X-RAY DIFFRACTION	f_angle_d	0.744	14957
X-RAY DIFFRACTION	f_dihedral_angle_d	15.755	4095
X-RAY DIFFRACTION	f_chiral_restr	0.03	1737
X-RAY DIFFRACTION	f_plane_restr	0.003	1714

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 (%)
3.3523-3.4509	0.4143	128	0.3509	2202	X-RAY DIFFRACTION	91
3.4509-3.5622	0.3506	141	0.3203	2389	X-RAY DIFFRACTION	99
3.5622-3.6895	0.3264	144	0.2998	2430	X-RAY DIFFRACTION	99
3.6895-3.8372	0.34	145	0.2915	2431	X-RAY DIFFRACTION	100
3.8372-4.0117	0.3173	142	0.2739	2411	X-RAY DIFFRACTION	100
4.0117-4.2231	0.3379	144	0.2332	2440	X-RAY DIFFRACTION	100
4.2231-4.4876	0.2669	144	0.2081	2425	X-RAY DIFFRACTION	100
4.4876-4.8338	0.2094	145	0.1919	2449	X-RAY DIFFRACTION	100
4.8338-5.3197	0.2722	146	0.2073	2464	X-RAY DIFFRACTION	100
5.3197-6.0882	0.2644	147	0.2268	2481	X-RAY DIFFRACTION	100
6.0882-7.6658	0.2711	149	0.2223	2515	X-RAY DIFFRACTION	100
7.6658-49.0082	0.206	154	0.1741	2623	X-RAY DIFFRACTION	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	5.4008	-0.4699	0.7307	2.9184	-2.3136	2.2263	-0.4363	-0.5082	-0.0686	0.3269	0.4686	0.5899	-0.4452	0.4791	-0.4953	1.7964	-0.1108	-0.1851	0.8592	0.087	0.5477	10.8992	127.8282	255.3102
2	3.6236	-1.5541	1.8658	1.7276	-0.3305	1.1595	0.4215	-1.5786	-0.5381	-0.0548	0.0025	0.5537	1.1181	0.2512	-0.2143	1.1113	-0.0967	0.0029	0.9136	0.1431	0.5863	7.1235	123.4886	254.149
3	2.4031	-2.6594	-0.1987	3.3993	1.2167	0.2736	0.6362	-1.0549	0.7321	0.5323	-0.0945	-0.0343	-0.5591	0.0443	-0.5781	0.9063	-0.0317	0.2448	0.6283	-0.0428	0.6978	0.5686	142.963	252.1456
4	5.1809	-1.0874	0.0337	2.332	-0.4134	2.2002	-0.1278	0.0611	1.0997	0.368	0.1667	-0.2156	-0.8104	0.1175	0.0312	1.0246	-0.1306	0.1722	0.6811	-0.0583	0.7463	11.4951	159.4545	256.7643
5	5.247	0.7071	4.4435	3.6386	-1.4709	4.9059	-2.5062	0.4076	2.8993	1.3167	0.7376	1.7479	0.1957	0.5594	1.5778	1.2133	-0.0311	0.1912	0.7573	-0.1502	0.6829	8.546	154.0571	255.3346
6	5.1195	0.4724	1.0164	4.0751	-1.7277	2.1427	-0.5458	1.8379	-1.4532	0.1639	-0.1578	-0.8014	0.0361	-0.1594	0.5226	0.8468	-0.1623	-0.0668	1.072	0.0064	0.9493	28.2036	152.1367	256.2597
7	3.4615	-0.5985	-0.8481	6.3003	-2.0459	7.4906	-0.1972	-0.9158	0.1966	0.4176	-0.197	-1.1947	1.1232	1.7082	0.2411	0.5935	-0.0528	-0.1154	0.8143	-0.0257	0.6369	23.2815	142.3523	255.439
8	2.8951	-1.6875	0.3929	4.0049	0.203	1.4949	0.6132	-0.8451	-0.3262	-0.2526	0.0565	0.4853	0.1958	-0.0557	-0.5946	1.2935	-0.2957	0.1732	0.9936	-0.0634	0.6307	0.1688	148.905	263.9399
9	5.7025	-0.3954	0.5831	3.4056	-2.2133	5.1811	-0.0384	0.2638	0.0164	0.3975	-0.0095	0.2167	-0.1705	0.0357	0.0376	0.4536	0.0659	0.0221	0.4665	-0.0109	0.4009	4.2957	130.2547	235.6475
10	3.6957	-0.5757	-0.0503	1.3117	1.8829	1.5113	0.0713	0.0196	0.2435	0.0912	-0.4412	0.7436	-0.5651	-0.8015	0.44	0.7229	0.1048	0.0966	0.9526	0.0907	0.8814	-25.3192	143.6361	241.1883
11	4.7978	1.9655	1.0946	6.7201	3.1928	4.0055	0.1445	-0.0211	-0.075	-0.0704	0.0823	0.4367	-0.2414	-0.6647	-0.318	0.4894	0.1047	0.0374	0.5709	0.2244	0.6177	-15.8577	133.2462	234.8829
12	2.3936	-2.1174	-1.2258	3.9313	-1.8996	4.5925	0.0002	-0.0318	0.1841	-1.5411	-0.2062	-1.3817	0.3778	0.028	0.1251	0.9007	0.0889	0.0283	0.5832	-0.0354	0.5101	25.3953	130.8854	168.6348
13	5.6852	0.148	-0.302	5.2073	0.8971	3.243	-0.0473	0.2017	0.2539	-1.3331	0.453	-0.8694	-1.3834	0.8034	-0.2354	1.0872	-0.0627	0.179	0.7734	0.0324	0.4934	23.4211	132.7963	169.3317
14	7.095	-0.5472	0.0664	0.532	0.7102	0.6323	1.201	0.5794	-0.3876	-0.7337	-0.7077	0.5484	-0.1464	-0.3041	-0.2514	1.0059	0.2525	-0.1339	0.729	-0.0077	0.6925	5.0849	129.4895	168.2163
15	3.1784	1.0304	1.4954	1.7745	-0.8711	1.4956	-0.1681	1.2552	-0.5001	0.3472	0.6392	0.1829	-0.2147	-0.5765	-0.3309	1.1438	0.3249	-0.3706	1.5818	-0.3326	1.3348	-10.7335	115.5584	155.9843
16	1.0576	0.6294	1.0266	2.0981	-1.161	2.7728	0.3811	0.0274	-0.5067	0.5817	-0.0607	0.8878	0.7601	-1.0443	-0.1257	0.8002	-0.0649	-0.0315	0.8173	-0.0736	1.0052	-0.0969	105.7572	168.1319
17	1.2365	-0.3361	0.7114	4.5972	-1.2943	2.2466	0.2034	-0.1476	-0.551	-0.895	0.2391	0.8548	0.1117	-0.5766	-0.4715	0.6758	0.2166	-0.3054	1.0583	-0.2213	0.8994	-1.6962	118.1739	166.8143
18	4.9618	0.3236	0.573	3.0532	1.7901	1.4358	-0.0222	-0.2239	-1.1299	0.4446	0.3183	-0.4097	0.4574	0.0649	-0.2741	0.8219	0.1354	-0.1454	0.5954	-0.1067	0.8544	14.2412	104.7707	170.6788
19	0.9618	0.7231	0.0763	2.169	-1.1057	0.7967	-0.0281	0.0283	-0.2457	-0.4849	-0.3413	0.9959	-0.9072	-0.2469	0.176	1.0315	0.0651	-0.307	1.0486	-0.1299	0.6737	1.3789	124.6003	156.0562
20	4.4616	-1.5775	-0.7645	4.8254	-0.3576	6.5066	-0.0302	-0.0383	0.095	-0.2512	0.1899	0.1174	-0.6455	0.2867	-0.0984	0.7164	0.0182	0.0006	0.6391	-0.0537	0.3962	14.0767	135.118	185.9324
21	1.8238	-1.2412	1.1348	1.8168	-1.6335	2.2396	0.068	-0.1017	0.2722	-0.295	-0.2548	0.5203	-1.1341	-0.5358	0.2906	1.145	0.231	-0.0497	0.9375	-0.0517	0.7975	-6.1633	152.4346	174.8737
22	5.0085	-0.8016	0.634	4.5105	1.8445	3.1658	0.0253	-0.2275	0.5341	0.0099	-0.1441	-0.5023	-0.7312	-0.1101	0.0195	1.4544	0.2119	-0.0366	0.8139	0.0267	0.7703	1.1506	150.2653	183.5299
23	4.2975	0.9197	1.6731	4.6257	-0.2661	2.1107	0.5967	-0.0625	0.1251	-0.4331	-0.3251	-0.5482	-0.4814	0.0275	-0.327	0.5792	0.0136	0.1306	0.6395	0.1356	0.4752	15.8212	135.0443	220.753
24	1.3548	0.7518	1.545	2.7544	-3.2157	9.3638	0.5341	-0.3748	0.1812	0.4185	-0.1884	0.144	-1.5289	0.4182	-0.1396	0.7514	-0.055	0.0664	0.4285	-0.0256	0.5088	11.6374	138.2178	220.0178
25	5.5499	0.0283	2.0063	2.7141	2.9757	5.2291	0.2088	0.6917	0.6712	-0.2905	-0.4516	0.0631	-0.8071	0.7024	0.3681	0.8087	-0.157	0.135	0.5001	0.1527	0.5984	14.4411	141.17	210.2289
26	3.5623	-5.21	2.3299	8.9568	-0.9432	4.3797	1.1308	0.3762	-1.3031	-0.4919	-0.3937	1.0308	-1.4154	1.0279	-0.5351	0.8875	-0.1401	0.2421	1.1337	-0.0982	0.7648	22.0213	139.5749	201.2617
27	7.645	-3.0998	2.0663	5.6609	1.0937	4.708	0.9702	0.5116	0.4092	-1.3746	-0.5104	-0.1244	-0.2163	0.6767	-0.5615	0.6233	0.0811	0.1511	0.4836	0.0949	0.4957	8.0483	129.0436	206.9125
28	3.8455	-0.8801	-1.9139	1.7096	-1.0964	4.8984	0.2463	0.5501	0.0151	-0.2406	-0.5356	-0.0858	0.7093	0.4583	0.3441	0.523	0.1072	0.0213	0.6431	0.0401	0.4246	13.6174	126.9418	201.156
29	6.4061	-1.4075	0.7472	4.5369	-0.953	3.9743	1.2333	0.6148	-0.5688	-0.2346	-1.0714	0.5403	1.1917	-2.1867	-0.2388	0.8042	-0.0734	-0.0791	0.9957	-0.0089	0.5785	3.3041	121.9446	200.553
30	4.5625	-1.2544	-0.441	4.8375	2.1872	6.6285	-0.0173	1.3721	-0.3693	0.6522	-0.5641	0.2097	0.8994	-1.5068	0.2353	0.5314	-0.159	-0.0106	0.7009	-0.0094	0.6231	4.3738	123.9506	211.4943
31	4.1276	0.3926	0.8009	3.4933	0.2176	6.0075	0.736	0.282	-0.0492	0.25	-0.6787	0.6066	1.4992	0.5132	-0.2782	1.0098	0.0883	0.0029	0.5426	0.0748	0.6514	8.0423	118.9873	221.992
32	4.4419	0.9171	1.8815	6.6879	-2.2557	2.2041	-0.5994	-0.2831	-1.3491	-0.2053	0.7971	-1.6342	1.9407	1.7687	-0.0595	0.9908	0.2923	-0.0235	0.8922	-0.2094	0.95	27.3607	117.8974	186.7069
33	-0.0296	1.2126	1.2844	1.7157	1.7137	4.4718	0.2386	0.1247	-0.2009	0.2939	0.9181	-0.6327	0.444	2.6883	-1.1877	1.1354	0.188	-0.054	1.684	0.0305	0.8357	31.3275	120.9035	220.6513
34	2.4511	0.1683	-3.6428	6.437	5.5816	6.0455	1.1315	-1.0738	1.6448	-2.1695	-0.2675	-1.7143	-0.7143	0.5954	-0.2725	0.8105	-0.0826	-0.0031	1.6946	-0.0471	1.0114	22.3724	142.7951	244.004
35	1.1406	-0.7352	-0.7576	3.4607	2.8386	3.8891	0.4857	-0.313	-0.4509	-0.616	0.5063	-0.8018	0.1984	2.1602	-0.6501	0.8946	0.1737	-0.1482	1.4605	-0.075	0.8361	28.6764	123.8573	230.6834
36	2.6002	-1.938	-0.2981	1.9392	1.2568	4.5088	0.7945	-0.2482	-0.3465	-0.3858	0.2004	-0.4541	-0.0372	2.0509	-1.0574	0.8886	0.1141	0.0199	1.3959	-0.0598	0.8488	29.7012	117.1628	193.9045
37	2.4913	0.8625	3.6106	3.9878	0.8108	5.4729	-0.2506	-2.6473	-2.256	0.4349	0.6552	0.7515	0.3037	-2.4663	-0.0887	1.6032	-0.01	0.0689	1.4944	0.3317	1.2368	5.7052	112.2779	180.6043

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 15 through 27 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 28 through 71 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 72 through 108 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 109 through 213 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 214 through 223 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 224 through 242 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 243 through 259 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 260 through 281 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 4 through 95 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 96 through 156 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 157 through 279 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 16 through 35 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 36 through 71 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 72 through 107 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 108 through 133 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 134 through 198 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 199 through 227 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 228 through 259 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 260 through 280 )
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 4 through 95 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 96 through 198 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 199 through 272 )
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 1 through 21 )
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 22 through 50 )
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 51 through 73 )
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 74 through 93 )
27	X-RAY DIFFRACTION	27	chain 'F' and (resid 1 through 9 )
28	X-RAY DIFFRACTION	28	chain 'F' and (resid 10 through 36 )
29	X-RAY DIFFRACTION	29	chain 'F' and (resid 37 through 50 )
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 51 through 73 )
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 74 through 94 )
32	X-RAY DIFFRACTION	32	chain 'G' and (resid 1 through 8 )
33	X-RAY DIFFRACTION	33	chain 'G' and (resid 9 through 21 )
34	X-RAY DIFFRACTION	34	chain 'G' and (resid 22 through 29 )
35	X-RAY DIFFRACTION	35	chain 'H' and (resid 2 through 13 )
36	X-RAY DIFFRACTION	36	chain 'H' and (resid 14 through 24 )
37	X-RAY DIFFRACTION	37	chain 'H' and (resid 25 through 29 )

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