PDB-6n1z: Importin-9 bound to H2A-H2B

ID or keywords:

Entry

Database: PDB / ID: 6n1z

Title

Importin-9 bound to H2A-H2B

Components

Histone H2A
Histone H2B 1.1
Importin-9

Keywords

TRANSPORT PROTEIN / Importin-9 / karyopherin / histone / H2A / H2B / histone chaperone / Ran GTPase / nucleosome / NLS / nuclear pore complex.

Function / homology

Function and homology information

proteasome localization / histone chaperone activity / nuclear import signal receptor activity / small GTPase binding / structural constituent of chromatin / protein import into nucleus / nucleosome / nuclear envelope / histone binding / protein heterodimerization activity ...
Similarity search - Function

Biological species

Homo sapiens (human)

Xenopus laevis (African clawed frog)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

SAD / Resolution: 2.7 Å

Authors

Tomchick, D.R. / Chook, Y.M. / Padavannil, A.

Funding support

United States, 6items

Organization	Grant number	Country
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	R01GM069909	United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	U01GM98256-01	United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	R01GM083960	United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	P41GM109824	United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	R01GM112108	United States
Welch Foundation	I-1532	United States

Citation

Journal: Elife / Year: 2019
Title: Importin-9 wraps around the H2A-H2B core to act as nuclear importer and histone chaperone.
Authors: Padavannil, A. / Sarkar, P. / Kim, S.J. / Cagatay, T. / Jiou, J. / Brautigam, C.A. / Tomchick, D.R. / Sali, A. / D'Arcy, S. / Chook, Y.M.

History

Deposition	Nov 12, 2018	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 20, 2019	Provider: repository / Type: Initial release
Revision 1.1	Mar 27, 2019	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2	Jan 1, 2020	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3	Mar 13, 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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Download

PDBx/mmCIF format	6n1z.cif.gz	1.3 MB	Display	PDBx/mmCIF format
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Validation report

Summary document	6n1z_validation.pdf.gz	478.6 KB	Display	wwPDB validaton report
Full document	6n1z_full_validation.pdf.gz	495.2 KB	Display
Data in XML	6n1z_validation.xml.gz	76.1 KB	Display
Data in CIF	6n1z_validation.cif.gz	104 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/n1/6n1z ftp://data.pdbj.org/pub/pdb/validation_reports/n1/6n1z	HTTPS FTP

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Related structure data

Similar structure data	4caf-d 4hzk-2 6nxg-d 2yne-d 6mb1-d 5o4v-d 4cae-d 6mb0-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

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#7 - Jul 2000 Nucleosome similarity (13) #85 - Jan 2007 Importins similarity (5) #205 - Jan 2017 Nuclear Pore Complex similarity (4) #241 - Jan 2020 Twenty Years of Molecules similarity (9)

Deposited unit

A: Importin-9

B: Histone H2A

C: Histone H2B 1.1

D: Importin-9

E: Histone H2A

F: Histone H2B 1.1

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

1

A: Importin-9

B: Histone H2A

C: Histone H2B 1.1

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

2

D: Importin-9

E: Histone H2A

F: Histone H2B 1.1

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

Unit cell

Length a, b, c (Å)	127.424, 223.289, 131.833
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	18
Space group name H-M	P2₁2₁2

Components on special symmetry positions

ID	Model	Components
1	1	A-1172- HOH

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID
1	1
2	1
1	2
2	2
1	3
2	3

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Selection details
1	1	1	(CHAIN A AND (RESID 15 THROUGH 233 OR RESID 236...
2	1	1	(CHAIN D AND (RESID 15 THROUGH 617 OR RESID 619...
1	1	2	(CHAIN B AND RESID 17 THROUGH 101)
2	1	2	CHAIN E
1	1	3	CHAIN C
2	1	3	(CHAIN F AND (RESID 26 THROUGH 28 OR RESID 31 THROUGH 82 OR RESID 85 THROUGH 121))

NCS ensembles :

ID
1
2
3

#1: Protein	Importin-9 / Imp9 / Ran-binding protein 9 / RanBP9 Mass: 116062.320 Da / Num. of mol.: 2 / Fragment: IMPORTIN-9 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: IPO9, IMP9, KIAA1192, RANBP9, HSPC273 / Plasmid: pGEX-4T3 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q96P70
#2: Protein	Histone H2A Mass: 14109.436 Da / Num. of mol.: 2 / Fragment: HISTONE H2A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xenopus laevis (African clawed frog) / Gene: hist1h2aj, LOC494591, XELAEV_18003602mg / Plasmid: pET3a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) plysS / References: UniProt: Q6AZJ8, UniProt: P06897*PLUS
#3: Protein	Histone H2B 1.1 / H2B1.1 Mass: 13655.948 Da / Num. of mol.: 2 / Fragment: HISTONE H2B 1.1 / Mutation: S33T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xenopus laevis (African clawed frog) / Plasmid: pET3a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) plysS / References: UniProt: P02281
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 355 / 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: 3.26 Å³/Da / Density % sol: 62.27 % / Mosaicity: 0.628 °
Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.04 M MES, 0.11 M potassium acetate, 2 mM magnesium acetate, 2 mM DTT, 3.0 M potassium formate, 25% glycerol

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97938 Å
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 22, 2015 / Details: monochromator
Radiation	Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97938 Å / Relative weight: 1
Reflection	Resolution: 2.7→50 Å / Num. obs: 103239 / % possible obs: 97.7 % / Redundancy: 10.1 % / R_merge(I) obs: 0.094 / Net I/σ(I): 7
Reflection shell	Resolution: 2.7→2.75 Å / Redundancy: 8.2 % / R_merge(I) obs: 2.086 / % possible all: 98.9

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Processing

Software

Name	Version	Classification
PHENIX		refinement
HKL-3000		data scaling
PDB_EXTRACT	3.24	data extraction
HKL-3000		data reduction
PHENIX		phasing

Refinement

Method to determine structure:

SAD / Resolution: 2.7→45.44 Å / SU ML: 0.28 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.3

	R_factor	Num. reflection	% reflection
R_free	0.238	1978	2.11 %
R_work	0.209	-	-
obs	0.21	93883	90.5 %

Solvent computation

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

Displacement parameters

B_iso mean: 57.12 Å²

Refinement step

Cycle: LAST / Resolution: 2.7→45.44 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	17795	0	0	355	18150

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Type
1	1	A	8758	X-RAY DIFFRACTION	POSITIONAL
1	2	D	8758	X-RAY DIFFRACTION	POSITIONAL
2	1	B	788	X-RAY DIFFRACTION	POSITIONAL
2	2	E	788	X-RAY DIFFRACTION	POSITIONAL
3	1	C	847	X-RAY DIFFRACTION	POSITIONAL
3	2	F	847	X-RAY DIFFRACTION	POSITIONAL

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 (%)
2.7001-2.7676	0.374	55	0.3	2186	X-RAY DIFFRACTION	31
2.7676-2.8424	0.2651	107	0.2986	5010	X-RAY DIFFRACTION	70
2.8424-2.926	0.2921	153	0.2673	6878	X-RAY DIFFRACTION	96
2.926-3.0205	0.2756	150	0.2491	7078	X-RAY DIFFRACTION	99
3.0205-3.1284	0.292	153	0.2466	7057	X-RAY DIFFRACTION	99
3.1284-3.2536	0.2689	155	0.2437	7116	X-RAY DIFFRACTION	99
3.2536-3.4016	0.2669	147	0.2288	7099	X-RAY DIFFRACTION	98
3.4016-3.5809	0.2308	151	0.2139	7056	X-RAY DIFFRACTION	98
3.5809-3.8052	0.2449	154	0.1975	7059	X-RAY DIFFRACTION	98
3.8052-4.0988	0.2571	148	0.1887	7049	X-RAY DIFFRACTION	97
4.0988-4.5109	0.1746	149	0.1675	7077	X-RAY DIFFRACTION	97
4.5109-5.1629	0.2172	152	0.168	7069	X-RAY DIFFRACTION	97
5.1629-6.5017	0.2313	149	0.2153	7068	X-RAY DIFFRACTION	96
6.5017-45.442	0.1903	155	0.1894	7103	X-RAY DIFFRACTION	93

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	1.0335	0.0311	-0.3015	0.6981	0.2304	2.8404	0.3749	0.4393	-0.1751	-0.4444	-0.2191	0.0391	0.3499	0.0723	-0.0935	0.7197	-0.0368	-0.0519	0.5845	-0.1102	0.2705	17.8375	-2.0119	-6.9845
2	2.5652	0.2947	0.2544	1.4203	0.0434	1.4939	0.0328	-0.0362	-0.0379	-0.0279	-0.1166	0.0659	0.0589	-0.2268	0.0748	0.1853	-0.0407	-0.0511	0.1795	0.0042	0.0738	33.7368	11.9742	27.9147
3	1.0011	-0.033	-0.0054	1.483	-1.0398	1.3565	-0.0619	0.2489	0.5433	-0.1398	0.0178	-0.0661	-0.0632	-0.0629	0.043	0.1506	-0.0331	-0.063	0.1914	0.1322	0.4012	54.4991	42.5597	15.0766
4	0.9167	-0.1443	-0.0765	0.2577	-0.1403	0.4937	0.0692	0.6301	0.7371	-0.0615	-0.0465	-0.1916	-0.2494	-0.0164	0.1677	0.4548	0.0031	-0.1895	0.4768	0.6896	1.0284	32.6055	63.7613	-4.8527
5	2.3541	-0.025	-0.19	3.3388	0.3897	2.7866	0.2502	-0.1492	0.6715	0.6334	-0.1244	-0.1011	-0.0202	-0.1805	-0.0376	0.4781	-0.0239	-0.1021	0.4226	0.1867	0.6416	10.2621	59.7675	8.0042
6	4.4665	0.0109	1.0572	1.5129	0.0469	4.6856	0.042	-0.5954	0.3578	0.6149	-0.0762	0.4963	-0.2076	-0.549	0.0467	0.8647	-0.0341	0.1851	0.4616	0.093	0.562	7.1229	33.7836	15.496
7	4.9364	-4.6293	-1.2544	4.9306	-0.4849	5.0139	0.2243	-0.9246	0.2789	0.6971	0.0395	-0.8287	-0.3372	0.4691	-0.2232	1.2474	-0.1879	-0.2163	0.6914	0.0827	0.6313	22.161	35.4026	20.2223
8	1.6764	0.3398	0.0737	5.4487	1.8963	1.6579	0.1771	0.2922	0.0384	-0.2584	0.0202	0.0503	-0.4314	0.0042	-0.1505	0.7707	-0.0996	0.0052	0.3559	0.1187	0.3364	12.9835	26.2734	-2.5838
9	5.7812	4.0769	0.2596	9.1583	3.9972	2.6806	0.237	0.1089	-0.1975	-0.635	0.2422	-0.1298	0.7803	0.0737	-0.4189	0.945	-0.1897	0.281	0.4702	0.0706	0.676	24.1325	32.9113	-4.9725
10	3.8834	-2.3317	-1.7737	1.4006	1.066	0.8103	0.1461	0.3658	0.1497	-0.1773	-0.0565	-0.0746	-0.4371	0.1817	-0.0775	1.0326	0.3056	-0.0666	0.951	0.0437	0.4865	24.9102	21.6099	14.0617
11	3.5081	1.4956	1.0915	3.6917	1.3082	6.3167	0.0555	-0.0156	0.2596	-0.1202	0.0261	0.6274	-0.198	-0.4822	-0.0644	0.674	-0.0496	-0.0576	0.3147	0.1204	0.4709	7.0755	23.8374	6.6816
12	2.3106	-1.0978	-0.4834	4.5723	0.5379	4.1461	0.0499	0.0734	0.5003	-0.203	0.2719	-0.5474	-0.6292	0.8772	-0.2579	0.7505	-0.1766	0.0041	0.4904	0.0749	0.4514	20.2831	28.3492	5.966
13	2.0024	-2.0351	-1.5699	2.8161	0.1851	4.8378	0.203	-0.2599	0.5208	0.4381	-0.1034	-0.4471	-1.0301	0.5014	-0.1568	1.4461	-0.238	0.2081	0.4226	0.0546	0.704	16.7353	43.6142	7.2901
14	1.1718	-0.3376	0.1086	1.4662	-0.1257	2.9719	0.1854	-0.37	-0.271	0.5436	0.0175	0.0286	0.4622	-0.2064	-0.1123	0.5678	-0.0126	-0.0911	0.5137	0.0756	0.2604	109.4463	-1.2836	76.8914
15	0.8836	-0.6086	0.9287	1.3089	0.2443	1.8293	0.1597	0.4548	-0.2129	0.0545	0.1048	-0.3777	0.3042	0.6951	-0.2139	0.2505	0.0901	-0.0219	0.5036	-0.0268	0.1975	108.2741	2.5302	45.9297
16	4.0026	-0.598	-0.4952	0.9247	-0.0235	1.7179	-0.0495	-0.1322	0.2594	0.2061	-0.0264	-0.0624	0.1274	0.4459	0.0166	0.209	0.0166	0.0037	0.279	-0.0086	0.0729	90.8464	12.6925	45.6096
17	0.9861	-0.2696	-0.0993	1.0944	0.4553	0.9902	-0.0582	-0.0258	0.4928	-0.1219	-0.0981	-0.0039	0.0568	0.147	-0.002	0.0252	-0.0497	-0.0684	0.2122	-0.0509	0.2968	76.0811	33.8318	46.0013
18	1.2786	0.5166	0.1545	0.9781	-0.017	0.7878	-0.1128	-0.6162	0.8512	0.2789	-0.0505	0.2644	-0.3964	0.0327	-0.026	0.3024	-0.0365	-0.0893	0.5265	-0.4461	0.9588	87.5408	64.4212	70.5938
19	1.6264	0.6411	0.7041	1.5093	-0.2153	1.835	-0.0024	-0.2538	0.7556	-0.0403	0.0053	-0.0631	0.0111	-0.0378	-0.1612	0.1743	-0.0905	-0.0596	0.3493	-0.3384	0.8368	111.6473	60.4727	66.4603
20	3.0248	-0.2941	-0.1276	3.7818	0.0751	4.7809	0.0357	0.5675	0.8034	-0.7146	0.1575	0.1844	0.0636	0.1733	-0.0493	0.344	-0.0398	-0.0516	0.3754	-0.0176	0.5281	117.1331	60.4007	52.0819
21	5.599	1.0005	1.9008	2.2505	1.8864	1.8005	0.056	0.712	0.2652	-0.764	0.1692	-0.5797	-0.2786	0.5252	-0.1675	0.7351	0.0114	0.302	0.4135	-0.0492	0.4537	120.3218	32.8214	52.1061
22	3.0215	3.0404	1.1085	3.0784	1.3948	4.6456	0.2182	0.8384	-0.7724	-0.4299	0.0823	0.22	0.4866	0.0105	-0.2519	0.8975	0.1967	0.0413	0.4281	-0.0345	0.4479	108.4397	31.1775	47.7416
23	5.6107	-3.2618	3.0716	2.6605	-0.4484	4.0214	-0.0858	1.387	1.5707	-0.8041	0.2959	1.3046	-0.6525	-0.9208	-0.2243	1.0027	0.2758	-0.1446	0.7231	0.1838	1.0749	100.8747	38.5662	46.6442
24	1.7203	-0.0647	-0.2189	3.3509	-0.0527	2.9646	0.2933	-0.0068	0.1653	0.1903	0.0016	-0.2746	-0.3118	0.1136	-0.2211	0.5743	0.0765	0.0601	0.287	-0.1249	0.2104	115.6741	30.5666	66.8329
25	8.0162	-1.0887	-4.0787	2.5562	-0.7533	2.8195	0.0174	-1.0707	0.211	0.8158	-0.0272	-0.8828	-0.2645	0.3684	0.0199	0.6816	-0.0013	-0.1397	0.4428	-0.0664	0.3386	118.8759	15.4057	75.652
26	4.7787	-1.6071	-0.6395	3.6807	-0.9053	9.1663	0.1839	-0.6197	0.3065	0.8297	0.1382	0.5303	-0.7498	-0.674	-0.3075	0.4991	0.1326	0.1406	0.4683	0.1175	0.298	109.1725	23.7322	77.1478
27	0.9877	0.4628	-0.0108	0.2173	-0.005	0.0002	0.0581	-0.6478	0.1908	1.3991	0.3519	-0.0891	0.5867	0.1252	-0.317	0.9983	0.2879	0.2349	0.4873	-0.0101	0.6421	103.9079	33.7976	72.8319
28	4.777	1.8743	0.9661	0.7354	0.3784	0.1951	0.1526	-0.8978	0.0558	0.4354	-0.2124	0.968	0.3377	-0.8193	0.0656	0.851	-0.2178	0.0786	0.731	-0.0186	0.7934	100.9286	21.0849	54.3764
29	0.1168	-0.2431	-0.3659	5.4029	-1.0948	1.8553	0.2413	0.0161	0.1611	0.0599	0.2516	0.3095	-0.8679	-0.6116	-0.3735	0.4932	0.157	0.1122	0.4249	0.0434	0.341	111.1221	26.409	62.313
30	5.9742	-2.611	-0.0161	1.1541	-0.0066	0.0145	0.0879	0.5146	1.8366	-0.3582	-0.1928	0.3926	-1.2992	-0.5869	0.0848	1.6412	0.4766	0.0804	0.8747	0.2184	0.9753	99.2908	47.1176	50.2162
31	1.0526	0.9145	-1.3252	1.492	0.0531	3.7531	0.2602	0.1903	0.4242	-0.1873	-0.0033	-0.06	-1.0824	-0.491	-0.4156	1.1792	0.1817	0.2929	0.3965	-0.0296	0.5913	112.9009	42.772	61.2154

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	CHAIN 'A' AND (RESID 15 THROUGH 228 )
2	X-RAY DIFFRACTION	2	CHAIN 'A' AND (RESID 229 THROUGH 491 )
3	X-RAY DIFFRACTION	3	CHAIN 'A' AND (RESID 492 THROUGH 706 )
4	X-RAY DIFFRACTION	4	CHAIN 'A' AND (RESID 707 THROUGH 852 )
5	X-RAY DIFFRACTION	5	CHAIN 'A' AND (RESID 853 THROUGH 1040 )
6	X-RAY DIFFRACTION	6	CHAIN 'B' AND (RESID 17 THROUGH 27 )
7	X-RAY DIFFRACTION	7	CHAIN 'B' AND (RESID 28 THROUGH 45 )
8	X-RAY DIFFRACTION	8	CHAIN 'B' AND (RESID 46 THROUGH 91 )
9	X-RAY DIFFRACTION	9	CHAIN 'B' AND (RESID 92 THROUGH 102 )
10	X-RAY DIFFRACTION	10	CHAIN 'C' AND (RESID 26 THROUGH 35 )
11	X-RAY DIFFRACTION	11	CHAIN 'C' AND (RESID 36 THROUGH 46 )
12	X-RAY DIFFRACTION	12	CHAIN 'C' AND (RESID 47 THROUGH 80 )
13	X-RAY DIFFRACTION	13	CHAIN 'C' AND (RESID 81 THROUGH 121 )
14	X-RAY DIFFRACTION	14	CHAIN 'D' AND (RESID 15 THROUGH 228 )
15	X-RAY DIFFRACTION	15	CHAIN 'D' AND (RESID 229 THROUGH 308 )
16	X-RAY DIFFRACTION	16	CHAIN 'D' AND (RESID 309 THROUGH 397 )
17	X-RAY DIFFRACTION	17	CHAIN 'D' AND (RESID 398 THROUGH 706 )
18	X-RAY DIFFRACTION	18	CHAIN 'D' AND (RESID 707 THROUGH 795 )
19	X-RAY DIFFRACTION	19	CHAIN 'D' AND (RESID 796 THROUGH 909 )
20	X-RAY DIFFRACTION	20	CHAIN 'D' AND (RESID 910 THROUGH 1041 )
21	X-RAY DIFFRACTION	21	CHAIN 'E' AND (RESID 17 THROUGH 27 )
22	X-RAY DIFFRACTION	22	CHAIN 'E' AND (RESID 28 THROUGH 37 )
23	X-RAY DIFFRACTION	23	CHAIN 'E' AND (RESID 38 THROUGH 45 )
24	X-RAY DIFFRACTION	24	CHAIN 'E' AND (RESID 46 THROUGH 74 )
25	X-RAY DIFFRACTION	25	CHAIN 'E' AND (RESID 75 THROUGH 80 )
26	X-RAY DIFFRACTION	26	CHAIN 'E' AND (RESID 81 THROUGH 91 )
27	X-RAY DIFFRACTION	27	CHAIN 'E' AND (RESID 92 THROUGH 101 )
28	X-RAY DIFFRACTION	28	CHAIN 'F' AND (RESID 25 THROUGH 35 )
29	X-RAY DIFFRACTION	29	CHAIN 'F' AND (RESID 36 THROUGH 79 )
30	X-RAY DIFFRACTION	30	CHAIN 'F' AND (RESID 80 THROUGH 88 )
31	X-RAY DIFFRACTION	31	CHAIN 'F' AND (RESID 89 THROUGH 121 )

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