PDB-5zyf: Crystal structure of Streptococcus pyogenes type II-A Cas2

ID or keywords:

Entry

Database: PDB / ID: 5zyf

Title

Crystal structure of Streptococcus pyogenes type II-A Cas2

Components

CRISPR-associated endoribonuclease Cas2

Keywords

PROTEIN BINDING / CRISPR / Cas2 / CRISPR-associated / Streptococcus pyogenes

Function / homology

CRISPR-associated endonuclease Cas2 / Virulence-associated protein D / CRISPR associated protein Cas2 / CRISPR associated protein Cas2 / maintenance of CRISPR repeat elements / RNA endonuclease activity / defense response to virus / Hydrolases; Acting on ester bonds / metal ion binding / CRISPR-associated endoribonuclease Cas2

Function and homology information

Biological species

Streptococcus pyogenes serotype M1 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

SAD / Resolution: 1.76 Å

Authors

Ka, D. / Bae, E.

Funding support

Korea, Republic Of, 2items

Citation

Journal: Nucleic Acids Res. / Year: 2018
Title: Molecular organization of the type II-A CRISPR adaptation module and its interaction with Cas9 via Csn2
Authors: Ka, D. / Jang, D.M. / Han, B.W. / Bae, E.

History

Deposition	May 24, 2018	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Aug 15, 2018	Provider: repository / Type: Initial release
Revision 1.1	Oct 31, 2018	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation_author.name
Revision 1.2	Mar 27, 2024	Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	5zyf_validation.pdf.gz	495.1 KB	Display	wwPDB validaton report
Full document	5zyf_full_validation.pdf.gz	501.8 KB	Display
Data in XML	5zyf_validation.xml.gz	22.7 KB	Display
Data in CIF	5zyf_validation.cif.gz	32.9 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/zy/5zyf ftp://data.pdbj.org/pub/pdb/validation_reports/zy/5zyf	HTTPS FTP

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Related structure data

Similar structure data	1hlb-d 5oc6-d 3bkt-2 1vkf-2 3bku-2 4xqn-4 4e2t-1 7a8s-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

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#181 - Jan 2015 Cascade and CRISPR similarity (2)

Deposited unit

A: CRISPR-associated endoribonuclease Cas2

B: CRISPR-associated endoribonuclease Cas2

C: CRISPR-associated endoribonuclease Cas2

D: CRISPR-associated endoribonuclease Cas2

E: CRISPR-associated endoribonuclease Cas2

F: CRISPR-associated endoribonuclease Cas2

hetero molecules

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

1

A: CRISPR-associated endoribonuclease Cas2

B: CRISPR-associated endoribonuclease Cas2

hetero molecules

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

2

C: CRISPR-associated endoribonuclease Cas2

D: CRISPR-associated endoribonuclease Cas2

hetero molecules

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

3

E: CRISPR-associated endoribonuclease Cas2

F: CRISPR-associated endoribonuclease Cas2

hetero molecules

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

Unit cell

Length a, b, c (Å)	50.771, 75.292, 145.702
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 endoribonuclease Cas2 / Cas2 protomer Chain A Mass: 10646.388 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus pyogenes serotype M1 (bacteria) Gene: cas2, SPy_1048 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: Q99ZW0, Hydrolases; Acting on ester bonds
#2: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO₄
#3: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C₂H₆O₂
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 292 / 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: 2.18 Å³/Da / Density % sol: 43.57 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, sitting drop Details: 22.0% (w/v) PEG 4000, 325 mM ammonium sulfate, 0.1 M sodium acetate pH 4.6

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 7A (6B, 6C1) / Wavelength: 0.9793 Å
Detector	Type: ADSC QUANTUM 270 / Detector: CCD / Date: Jul 29, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9793 Å / Relative weight: 1
Reflection	Resolution: 1.76→50 Å / Num. obs: 56417 / % possible obs: 99.7 % / Redundancy: 7.2 % / R_merge(I) obs: 0.071 / R_pim(I) all: 0.029 / R_rim(I) all: 0.077 / Χ²: 1.012 / Net I/σ(I): 22.45
Reflection shell	Resolution: 1.76→1.82 Å / Redundancy: 6.5 % / R_merge(I) obs: 0.547 / Mean I/σ(I) obs: 3.417 / Num. unique obs: 5499 / CC_1/2: 0.903 / R_pim(I) all: 0.228 / R_rim(I) all: 0.594 / Χ²: 1 / % possible all: 98.6

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Processing

Software

Name	Version	Classification
PHENIX	1.9_1692	refinement
HKL-2000		data collection
PHENIX		model building
HKL-2000		data scaling
PHENIX		phasing
HKL-2000		data reduction

Refinement

Method to determine structure:

SAD / Resolution: 1.76→36.448 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 23.57

	R_factor	Num. reflection	% reflection
R_free	0.2336	2000	3.55 %
R_work	0.1971	-	-
obs	0.1984	56344	99.67 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 1.76→36.448 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	4138	0	66	292	4496

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	4261
X-RAY DIFFRACTION	f_angle_d	1.018	5661
X-RAY DIFFRACTION	f_dihedral_angle_d	13.638	1645
X-RAY DIFFRACTION	f_chiral_restr	0.045	603
X-RAY DIFFRACTION	f_plane_restr	0.005	704

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 (%)
1.7569-1.8008	0.3119	137	0.269	3704	X-RAY DIFFRACTION	97
1.8008-1.8495	0.3335	141	0.2563	3840	X-RAY DIFFRACTION	100
1.8495-1.9039	0.2907	140	0.2333	3810	X-RAY DIFFRACTION	100
1.9039-1.9654	0.2332	142	0.2044	3858	X-RAY DIFFRACTION	100
1.9654-2.0356	0.2193	143	0.2041	3880	X-RAY DIFFRACTION	100
2.0356-2.1171	0.2228	142	0.2081	3856	X-RAY DIFFRACTION	100
2.1171-2.2134	0.2213	142	0.1946	3872	X-RAY DIFFRACTION	100
2.2134-2.3301	0.2423	142	0.1977	3853	X-RAY DIFFRACTION	100
2.3301-2.4761	0.2578	142	0.2012	3865	X-RAY DIFFRACTION	100
2.4761-2.6672	0.2446	144	0.2027	3899	X-RAY DIFFRACTION	100
2.6672-2.9355	0.248	144	0.2124	3908	X-RAY DIFFRACTION	100
2.9355-3.36	0.2589	144	0.1979	3941	X-RAY DIFFRACTION	100
3.36-4.2322	0.2087	147	0.1794	3973	X-RAY DIFFRACTION	100
4.2322-36.4555	0.2082	150	0.1831	4085	X-RAY DIFFRACTION	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	4.1853	-1.8462	0.3023	7.6704	-0.3248	4.931	0.143	0.25	0.2797	-0.0035	-0.2521	-0.026	-0.4289	-0.2993	0.057	0.1599	0.0082	0.0094	0.2232	0.028	0.1579	7.436	26.5858	112.3322
2	3.1635	-2.2907	0.1313	7.9797	0.0535	2.9212	0.099	0.3738	-0.417	-0.2015	-0.0399	0.5513	0.1881	-0.2957	-0.0132	0.1066	-0.0378	-0.0144	0.249	0.0245	0.2234	7.9561	11.8666	110.6948
3	5.9961	-1.2801	-4.9956	6.7119	0.6196	4.1824	0.0706	0.1582	-0.0224	-0.6188	0.1284	-0.0128	0.0317	-0.2478	-0.1164	0.2551	0.0531	-0.0218	0.276	0.0464	0.1644	7.7692	23.5509	104.859
4	1.4364	-1.2438	-2.1388	3.3436	1.7906	3.4429	-0.0254	-0.2979	0.2076	0.2333	0.4577	1.0739	-0.2158	-1.1185	0.3597	0.2358	0.2061	0.1316	0.5357	0.1209	0.4786	-0.7598	30.0454	112.723
5	6.8808	-5.2855	-1.4901	5.1478	2.5115	2.0641	0.2305	-0.4238	-0.3374	0.6406	0.0206	0.6899	-0.3863	-0.7176	-0.0462	0.2529	0.0668	0.1442	0.401	0.0625	0.2693	1.0705	22.8934	120.4865
6	1.5747	-0.4602	1.1868	3.8303	-4.2429	5.1858	-0.0736	0.0427	0.0865	0.8533	-0.0354	-0.2949	-0.3442	-0.1285	0.0481	0.0744	0.0037	0.0063	0.1945	0.0237	0.1656	10.4296	24.3414	116.2584
7	8.9289	-1.7172	-1.7868	6.1098	3.3718	7.2466	0.5177	0.6076	0.4126	-0.3523	-0.15	0.329	0.2161	-0.3402	-0.3571	0.2956	0.0935	0.001	0.278	0.0949	0.2689	6.9747	39.6649	105.6855
8	3.3229	-3.5054	2.7486	3.8256	-2.8623	3.0718	0.0503	0.3857	-0.8068	-0.6845	0.1041	0.7706	0.5248	-0.1473	-0.1248	0.3053	0.0292	0.0124	0.2393	-0.0187	0.3168	18.0359	28.3728	99.9217
9	5.028	-3.6742	-1.3689	2.5087	0.7237	1.3423	-0.0067	-0.0834	-0.2393	0.1669	0.0255	0.1111	-0.0647	-0.0209	-0.0341	0.1749	0.0082	0.0009	0.1417	0.0043	0.1489	20.6421	26.786	110.0725
10	4.5702	2.8328	0.1213	7.9729	1.7483	3.3754	0.0044	-0.0678	-0.2251	0.1786	0.0552	-0.3787	-0.0238	0.2706	-0.0849	0.1538	-0.0003	-0.0035	0.2241	-0.0079	0.2441	30.1461	24.5168	109.3899
11	2.0638	-0.1848	0.4799	9.049	-3.9932	3.1865	-0.0223	-0.0526	0.1641	0.2154	0.0022	-0.2578	-0.1159	0.0835	0.0491	0.1384	-0.0099	-0.034	0.1816	-0.0239	0.1955	23.0708	35.2459	113.4197
12	4.3453	0.0155	-0.8112	6.0572	-3.6602	2.8597	-0.0493	0.3888	-0.1423	-0.2398	-0.0799	-0.3213	0.0912	0.1081	0.151	0.1494	-0.0326	0.0041	0.2248	-0.0328	0.1544	25.2387	32.6335	100.9841
13	1.2612	-0.2688	-0.5421	5.7793	-1.5756	2.1007	0.0471	-0.1526	0.0612	0.6973	0.2165	0.1567	-0.3096	-0.1537	-0.2586	0.1885	0.0178	0.0017	0.1894	-0.0042	0.1465	13.2233	32.0398	117.3811
14	4.8185	3.8639	-2.8205	4.2341	-2.7016	5.1283	0.2803	0.3048	-0.0931	0.3386	-0.1881	0.2432	0.1549	0.2048	-0.0191	0.3187	0.0322	-0.0145	0.2565	-0.0242	0.2443	-2.6426	37.8164	87.52
15	6.799	3.9555	-2.184	2.6065	-1.7386	4.4266	0.1782	0.6417	-0.4876	-0.4709	-0.0697	0.8494	0.6704	-0.352	-0.1242	0.3447	0.0162	-0.12	0.3428	-0.0998	0.5403	-15.8302	32.0184	87.0366
16	6.5685	-1.7442	-2.7493	6.6522	0.9216	2.5476	0.0891	0.8024	0.0556	-0.1183	-0.209	0.3068	0.1667	-0.7478	0.1933	0.296	0.0136	-0.0175	0.4057	0.0179	0.2155	-4.1931	40.8423	83.0583
17	6.6028	0.1039	0.0858	6.8452	0.7701	7.5648	-0.0734	-0.345	-0.188	-0.1609	0.3108	0.7551	0.0073	-0.128	-0.0907	0.1497	0.0376	0.0207	0.242	-0.0159	0.2425	-10.8696	39.4637	95.2965
18	2.607	1.7997	-2.678	6.4511	-0.611	6.0879	-0.0531	0.3546	0.1506	-0.8879	0.008	-0.1116	-0.6678	0.4098	0.031	0.3038	-0.0202	-0.0122	0.3088	0.0428	0.1781	5.6798	41.5525	85.0046
19	7.0196	2.6376	-0.3876	4.5046	-1.3497	5.9554	0.2516	0.5397	-0.4398	-1.4045	0.215	0.442	0.2863	0.2111	-0.3849	0.3657	0.0358	-0.0427	0.3265	-0.0395	0.2264	4.989	28.3628	79.1993
20	3.7478	0.8056	-0.4744	7.0484	-1.2767	4.3845	0.3548	-0.693	-0.6073	-0.3318	-0.4008	0.0561	0.0869	-0.5785	0.0349	0.2154	-0.057	-0.0956	0.3725	0.0678	0.2539	6.0975	28.1494	89.8651
21	8.6796	4.1118	0.5521	9.0235	1.571	6.2741	0.0386	-0.5248	-1.2538	0.0391	0.0425	0.2599	1.4333	-0.3688	-0.1611	0.4439	-0.0502	-0.0465	0.2727	0.0987	0.3934	6.3154	16.6858	91.4047
22	4.6115	-1.8042	4.1313	4.0321	0.2066	4.7707	-0.1831	-0.3982	0.1352	0.14	0.0541	0.1295	-0.271	-0.1802	0.1514	0.1978	-0.0205	-0.0253	0.2846	0.0432	0.2134	9.6635	28.9248	93.6903
23	0.7567	-1.0897	0.8896	8.1538	0.2034	4.5067	0.4631	0.3708	-0.0718	-1.5518	-0.4708	0.1655	1.6235	0.4881	-0.2519	0.5862	0.1053	-0.0358	0.4177	-0.0347	0.276	9.5982	21.3381	82.1755
24	3.2266	0.7892	0.4604	2.454	2.7466	7.8185	0.0375	0.0624	0.156	-0.0463	-0.0177	-0.08	-0.4743	0.2983	0.0152	0.2079	-0.0101	-0.0309	0.2703	0.0406	0.1739	9.1909	38.8609	91.4533
25	4.8332	4.8074	-2.6193	4.7414	-2.606	2.5506	0.0571	-0.6839	-0.2936	0.1919	0.1137	0.2051	0.5498	0.1905	0.0057	0.2904	0.0377	0.0364	0.3729	-0.0169	0.2834	-4.2532	35.5462	98.1082
26	1.0109	-0.8974	2.0225	4.3068	-1.5199	3.9303	0.1188	-0.7547	0.0696	0.8491	0.2059	1.35	-0.3989	-0.6428	-0.1098	0.486	0.0404	0.2486	0.4304	0.0403	0.5368	-3.3071	50.6364	56.6272
27	2.7754	-3.7839	-2.0972	5.2634	2.6771	3.3361	0.1489	-0.4617	-0.0052	0.5328	-0.3093	0.0507	-0.5649	-0.0726	-0.1985	0.4482	-0.09	0.0329	0.324	0.0059	0.1834	6.4216	47.5564	56.0209
28	2.9644	1.5443	-0.9468	4.4501	-2.0592	4.6637	0.7149	-0.3482	0.1159	0.5565	-0.4599	-0.199	-0.5625	0.0888	0.5367	0.7323	-0.0464	0.2057	0.4	-0.0577	0.1815	5.1486	45.3309	60.9288
29	1.9509	1.0776	3.1211	5.8665	-0.8095	7.0409	-0.201	0.2734	0.2004	-0.4188	-0.4171	0.7233	0.0751	0.3085	0.5874	0.5168	0.0223	-0.0066	0.3274	-0.0706	0.31	-2.1349	35.0602	64.8775
30	3.4524	-2.1032	2.9729	7.4142	-0.6796	3.0672	0.3966	-0.3408	-0.792	1.568	-0.3818	0.9375	0.8951	-0.3855	0.0398	0.7345	-0.2583	0.0303	0.4702	-0.0597	0.4757	-7.8658	28.8	69.8383
31	6.2629	6.0342	0.9837	8.0209	2.8871	3.2505	0.9102	0.0689	-0.4172	-0.8084	-0.755	1.0645	-0.2745	-1.4862	-0.3856	0.6422	0.1163	-0.1128	0.5005	0.0249	0.3094	-1.4272	37.2171	71.0127
32	1.9713	0.7844	0.9499	8.5616	2.6734	2.3038	0.2274	-0.2982	-0.376	-1.1751	-0.1581	-0.2216	0.8087	0.8133	-0.0384	0.469	0.0934	0.0331	0.5188	0.0615	0.2242	5.6999	31.2231	71.1513
33	0.1837	0.1024	0.6294	0.0482	0.3138	2.0542	-1.0981	-0.7349	-0.8966	0.5256	-0.1079	-0.4391	0.2527	0.7652	0.0186	0.9438	0.2163	0.2379	0.9639	0.0826	1.0791	11.7822	22.5296	64.8505
34	6.825	1.2492	-0.5492	2.2114	-1.3624	8.0991	-0.5334	0.7749	-0.7162	-1.35	0.437	0.8332	1.5385	-0.5599	0.1891	0.7044	-0.1686	-0.0931	0.38	-0.0242	0.3423	-3.1095	26.0748	60.4246
35	2.5628	1.3934	0.0985	6.2326	0.4833	6.4371	-0.1303	-0.9393	-0.0061	0.3186	-0.5191	-0.1803	-0.1337	1.7549	-0.3947	0.5488	-0.1226	-0.0499	0.9127	0.153	0.1174	10.8544	38.3344	67.8251
36	2.518	-2.2084	3.2524	6.4262	-2.7553	4.2482	0.3197	-0.8745	-0.1471	1.169	0.0329	1.055	-0.3123	-1.6329	-0.4201	1.104	-0.1686	0.3179	0.7425	-0.0463	0.3985	1.4676	49.0103	69.443

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 5 through 14 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 15 through 35 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 36 through 44 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 45 through 52 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 53 through 66 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 67 through 78 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 79 through 84 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 85 through 91 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 6 through 19 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 20 through 35 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 36 through 52 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 53 through 71 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 72 through 92 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 6 through 14 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 15 through 35 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 36 through 55 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 56 through 71 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 72 through 84 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 85 through 90 )
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 2 through 19 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 20 through 35 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 36 through 57 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 58 through 71 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 72 through 84 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 85 through 92 )
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 7 through 35 )
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 36 through 57 )
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 58 through 90 )
29	X-RAY DIFFRACTION	29	chain 'F' and (resid 6 through 22 )
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 23 through 36 )
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 37 through 44 )
32	X-RAY DIFFRACTION	32	chain 'F' and (resid 45 through 49 )
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 50 through 56 )
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 57 through 71 )
35	X-RAY DIFFRACTION	35	chain 'F' and (resid 72 through 84 )
36	X-RAY DIFFRACTION	36	chain 'F' and (resid 85 through 90 )

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