PDB-4wsc: Crystal structure of a GroELK105A mutant

ID or keywords:

Entry

Database: PDB / ID: 4wsc

Title

Crystal structure of a GroELK105A mutant

Components

60 kDa chaperonin

Keywords

CHAPERONE / chaperonin / helix dipole / negative cooperativity

Function / homology

Function and homology information

GroEL-GroES complex / chaperonin ATPase / virion assembly / ATP-dependent protein folding chaperone / response to radiation / protein refolding / response to heat / protein folding / magnesium ion binding / ATP hydrolysis activity ...
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.04 Å

Authors

Lorimer, G.H. / Ye, X. / Fei, X. / Yang, D. / Corsepius, N. / LaRonde, N.A.

Citation

Journal: To Be Published
Title: Crystal structure of a GroELK105A mutant
Authors: Lorimer, G.H. / Ye, X. / Fei, X. / Yang, D. / Corsepius, N. / LaRonde, N.A.

History

Deposition	Oct 26, 2014	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Nov 11, 2015	Provider: repository / Type: Initial release
Revision 1.1	Sep 27, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_oper_list Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4wsc.cif.gz	2.6 MB	Display	PDBx/mmCIF format
PDB format	pdb4wsc.ent.gz	2.2 MB	Display	PDB format
PDBx/mmJSON format	4wsc.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ws/4wsc ftp://data.pdbj.org/pub/pdb/validation_reports/ws/4wsc	HTTPS FTP

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Related structure data

Related structure data	1xckS S: Starting model for refinement
Similar structure data	6kfv-d 5w0s-d 4hel-d 2nwc-d 1xck-d 5opw-d 2ynj-d 2yey-d 1oel-1 4wgl-d 4v43-2 1ss8-1 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	#32 - Aug 2002 Chaperones similarity (11)

Deposited unit

A: 60 kDa chaperonin

B: 60 kDa chaperonin

C: 60 kDa chaperonin

D: 60 kDa chaperonin

E: 60 kDa chaperonin

F: 60 kDa chaperonin

G: 60 kDa chaperonin

H: 60 kDa chaperonin

I: 60 kDa chaperonin

J: 60 kDa chaperonin

K: 60 kDa chaperonin

L: 60 kDa chaperonin

M: 60 kDa chaperonin

N: 60 kDa chaperonin

803 kDa, 14 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)	135.640, 259.390, 143.310
Angle α, β, γ (deg.)	90.00, 105.12, 90.00
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	60 kDa chaperonin / GroEL protein / Protein Cpn60 Mass: 57333.609 Da / Num. of mol.: 14 / Mutation: K105A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: groL, groEL, mopA, b4143, JW4103 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P0A6F5

#1: Protein

60 kDa chaperonin / GroEL protein / Protein Cpn60

Mass: 57333.609 Da / Num. of mol.: 14 / Mutation: K105A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli) / Strain: K12 / Gene: groL, groEL, mopA, b4143, JW4103 / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P0A6F5

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Experiment

Experiment	Method: X-RAY DIFFRACTION

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Sample preparation

Crystal	Density Matthews: 3.03 Å³/Da / Density % sol: 59.43 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: PEG 4000, HEPES / PH range: 6.5-7.5

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.9792 Å
Detector	Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 23, 2014
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9792 Å / Relative weight: 1
Reflection	Resolution: 3.04→84.15 Å / Num. obs: 180177 / % possible obs: 98.5 % / Redundancy: 4.9 % / R_merge(I) obs: 0.19 / Net I/σ(I): 6.9
Reflection shell	Resolution: 3.04→3.09 Å / Redundancy: 4.4 % / R_merge(I) obs: 0.758 / Mean I/σ(I) obs: 2 / % possible all: 95.2

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Processing

Software

Name: PHENIX / Version: (phenix.refine: 1.8.4_1496) / Classification: refinement

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1xck

1xck

Resolution: 3.04→80.523 Å / SU ML: 0.47 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 26.82 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.256	2001	1.11 %
R_work	0.19	-	-
obs	0.1908	180102	98.4 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 3.04→80.523 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	53914	0	0	0	53914

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.01	54306
X-RAY DIFFRACTION	f_angle_d	1.422	73346
X-RAY DIFFRACTION	f_dihedral_angle_d	14.717	20440
X-RAY DIFFRACTION	f_chiral_restr	0.059	8932
X-RAY DIFFRACTION	f_plane_restr	0.007	9618

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 (%)
3.04-3.116	0.3388	140	0.2724	12318	X-RAY DIFFRACTION	95
3.116-3.2003	0.372	129	0.2644	12310	X-RAY DIFFRACTION	96
3.2003-3.2945	0.32	145	0.2556	12452	X-RAY DIFFRACTION	97
3.2945-3.4008	0.3267	146	0.2482	12534	X-RAY DIFFRACTION	97
3.4008-3.5224	0.3041	141	0.2185	12598	X-RAY DIFFRACTION	98
3.5224-3.6634	0.2671	135	0.2072	12633	X-RAY DIFFRACTION	98
3.6634-3.8301	0.26	154	0.1929	12751	X-RAY DIFFRACTION	99
3.8301-4.032	0.2414	140	0.1732	12804	X-RAY DIFFRACTION	99
4.032-4.2846	0.2252	145	0.1669	12870	X-RAY DIFFRACTION	100
4.2846-4.6154	0.2279	148	0.1599	12956	X-RAY DIFFRACTION	100
4.6154-5.0798	0.2284	144	0.1579	12925	X-RAY DIFFRACTION	100
5.0798-5.8147	0.2527	141	0.1758	12940	X-RAY DIFFRACTION	100
5.8147-7.3252	0.2367	146	0.1815	12953	X-RAY DIFFRACTION	100
7.3252-80.5514	0.191	147	0.1497	13057	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	2.1133	-0.0699	-0.2387	0.3204	0.0454	0.2431	-0.0207	0.1011	0.103	0.0086	0.0617	0.1413	-0.0564	-0.0596	-0.0373	0.1642	0.0431	-0.0224	0.1526	-0.0142	0.1992	54.4717	10.8126	7.1611
2	1.3662	0.1835	0.0301	3.2458	0.1259	0.5418	0.2943	0.3376	0.5455	-0.7122	-0.1893	1.4981	-0.0005	-0.0335	-0.0972	0.5372	0.1718	-0.0858	0.4426	-0.0647	0.9694	60.1238	7.2588	-26.3413
3	1.0412	-0.365	-0.4169	1.3928	0.3553	0.8498	-0.0209	0.0014	-0.0811	0.0602	0.0664	-0.1186	0.1396	-0.052	-0.0269	0.1398	-0.0015	-0.0086	0.1637	0.0245	0.2879	66.4959	3.154	6.9096
4	0.8612	0.1882	0.1024	0.9247	0.1073	0.4274	0.1108	0.0359	0.0873	-0.0814	-0.0642	-0.0923	0.0524	0.0298	-0.0412	0.1394	0.0077	-0.0059	0.1791	0.0022	0.2071	32.9923	-23.0558	2.6855
5	4.2903	0.8741	0.2481	3.5361	-0.2408	1.8267	0.101	0.1514	0.4088	-0.2724	0.1118	-0.2969	-0.1674	0.2171	-0.182	0.3768	-0.0138	0.0594	0.3373	-0.0295	0.2321	34.5056	-17.8321	-27.3066
6	0.6924	0.6283	0.1393	0.9732	-0.1267	0.2886	0.094	-0.0021	-0.0369	0.0732	-0.0381	-0.0236	0.0606	0.0515	-0.0492	0.1327	0.0116	-0.0086	0.1952	-0.0163	0.1932	36.5197	-31.2599	2.1561
7	3.1165	-0.3963	0.256	0.1245	-0.2067	0.7799	0.1677	0.3404	0.1701	0.0494	-0.1787	0.3217	-0.2756	0.23	0.006	0.1249	-0.0425	0.0414	0.0782	-0.0502	0.348	-2.0787	-9.2272	7.6464
8	0.1955	-0.2742	0.0828	1.039	0.3453	0.8855	0.0665	0.1411	-0.165	-0.0511	-0.0429	-0.0052	-0.0075	0.1744	-0.0136	0.1176	0.0353	-0.0086	0.1826	0.0397	0.1877	-8.1794	-26.8731	0.401
9	3.1183	0.0901	-0.727	1.744	0.4373	0.9288	0.0664	0.2639	0.5738	-0.1385	0.0813	-0.122	-0.2388	0.0593	-0.043	0.3396	0.0208	0.0651	0.1795	0.0183	0.3058	-2.3317	-20.4067	-27.1237
10	1.2023	-0.0596	0.6273	0.7886	0.1343	1.1824	0.0168	-0.113	0.0363	-0.0147	0.0005	0.1715	0.0411	-0.1586	-0.0188	0.1399	-0.0184	0.0424	0.1268	-0.0261	0.1757	-10.637	-27.2397	8.0629
11	0.8469	-1.1384	0.0562	1.7176	-0.5014	0.8204	-0.0568	0.1203	0.2342	-0.0638	0.1857	-0.1809	-0.1433	0.2393	0.0784	0.0959	-0.0296	-0.0171	0.122	-0.0356	0.5065	-17.4181	15.2141	8.1583
12	0.8362	-0.2687	0.294	0.8697	0.5083	0.6931	0.1714	0.4354	-0.1085	-0.2148	-0.101	0.2918	-0.0278	0.1772	-0.0327	0.2141	0.0963	0.019	0.2202	0.0734	0.4283	-35.0436	8.3255	1.461
13	3.5013	-0.8046	-0.5302	3.9573	1.312	0.6326	0.3237	0.493	0.1721	-0.4588	-0.1784	-0.9511	-0.0849	0.0361	-0.0403	0.5874	0.1482	0.0673	0.4517	0.1649	0.4738	-27.1554	7.979	-27.1248
14	2.4805	-0.4011	-0.3106	0.8502	0.3856	1.1534	-0.1806	-0.134	0.051	-0.0828	0.1788	0.2272	-0.0733	-0.1228	0.1075	0.1138	0.0172	-0.0183	0.138	-0.0145	0.2372	-36.7297	10.1654	9.1948
15	1.6732	0.8091	-0.9576	2.9126	-0.3791	0.9627	0.1891	0.0456	-0.0358	-0.2136	-0.2223	-0.1523	0.121	0.1631	0.0028	0.1844	-0.0391	-0.0736	0.1211	0.0228	0.2972	-12.2136	41.873	8.1919
16	2.7381	1.346	0.4741	0.9546	0.0246	0.2378	-0.0844	2.0181	-0.4187	-0.5881	0.1486	-0.0167	-0.0548	0.4214	-0.1529	0.5657	-0.2725	-0.0615	0.4478	0.2007	0.8435	-22.1373	47.7876	-20.5433
17	0.968	-0.1571	0.5212	2.0993	-0.0853	0.4804	-0.0507	0.1887	0.2582	-0.121	-0.0222	0.3644	-0.1276	-0.0081	0.0442	0.237	0.009	-0.0074	0.2186	0.122	0.5284	-25.072	54.2445	4.3735
18	1.7157	0.1054	-0.1332	1.3747	0.0117	0.5739	0.0024	-0.0394	-0.2799	0.0488	0.0035	0.0304	0.0716	-0.0127	-0.0145	0.1217	-0.0146	0.0207	0.1689	0.0496	0.2749	14.0431	57.7548	8.2008
19	2.2581	-1.0485	0.3387	1.6916	0.0745	0.6176	-0.1439	0.2563	-1.0522	-0.0757	0.0973	0.1488	0.2286	0.0776	-0.0122	0.3901	0.0448	0.158	0.3807	-0.0512	0.6855	15.6855	63.9441	-24.6771
20	1.1587	-0.1065	0.2188	1.3591	-0.0642	0.9594	0.0752	-0.0693	-0.0542	-0.0615	-0.0888	-0.0599	-0.0377	0.1354	0.0117	0.1333	0.0642	-0.0085	0.1254	0.0541	0.285	18.964	71.0181	8.0916
21	1.8701	-0.4908	-0.0416	1.3732	0.2688	0.6186	-0.2127	0.0524	-0.2131	-0.0736	0.297	0.1981	-0.1348	0.0791	0.0696	0.1187	0.0528	0.0493	0.1728	0.0778	0.3416	44.3975	39.8226	6.6868
22	0.4468	0.2851	0.1153	0.2071	0.4843	1.9909	0.0243	0.1282	0.3363	-0.1573	0.2035	-0.358	-0.3059	0.5557	-0.1221	0.2755	0.1234	0.0749	0.3847	0.0425	0.4612	63.3333	51.7211	-4.1987
23	3.9403	-0.4392	0.4336	2.1964	-0.2469	0.8934	0.3139	0.359	-0.1841	-0.0995	-0.1327	0.5446	-0.1726	-0.0717	-0.1547	0.4496	0.2032	0.0954	0.533	0.0727	0.5864	48.0617	46.9044	-28.0451
24	1.7698	-0.9938	-0.6184	1.6103	0.1064	0.6289	0.0038	-0.1379	0.2311	-0.1773	0.0807	-0.3149	0.0197	0.2096	-0.0422	0.2091	0.0117	0.0204	0.2107	0.0747	0.359	59.194	48.5943	7.2479
25	2.883	0.8014	-0.7117	1.2057	-0.3277	0.3218	-0.1498	-0.0643	-0.1403	0.1641	0.0612	0.1186	0.0784	-0.0004	0.0477	0.1313	-0.0247	0.0257	0.2652	-0.0376	0.2805	-2.8168	48.7369	46.1448
26	0.8422	0.4499	-1.1564	0.8769	-1.3358	2.0422	-0.0824	-0.0043	0.1557	0.3734	0.3352	0.2273	-0.1294	-0.2477	-0.1959	0.3615	0.0344	0.172	0.3965	0.015	0.6256	-16.4071	66.3082	58.0004
27	4.6613	1.9382	-0.092	3.6139	0.055	0.509	0.5701	-0.4387	0.4173	0.5121	-0.1473	-0.2833	-0.2768	0.3841	-0.3693	0.6034	-0.1821	0.1049	0.7509	-0.1309	0.4411	-2.8119	55.6213	80.1656
28	1.9711	0.7214	-0.4036	0.6568	0.2788	1.4441	0.0574	-0.0105	0.1307	0.1232	-0.0325	0.3655	-0.1274	-0.2254	-0.0543	0.2227	0.0228	0.091	0.2153	-0.0135	0.4116	-13.6484	62.0395	45.9969
29	1.3943	1.481	-0.3652	3.9947	-0.3632	1.0058	-0.0407	-0.3147	0.1523	-0.0192	0.2111	0.2567	-0.0102	0.0652	-0.0567	0.1226	-0.0253	-0.0054	0.2917	0.0216	0.271	-16.9382	18.941	46.1323
30	1.3376	-0.3418	-0.7697	1.045	0.0341	1.7711	-0.0953	0.0387	0.0089	0.1119	0.2278	0.0445	-0.021	-0.2624	-0.127	0.1556	-0.037	-0.0049	0.25	0.0261	0.1516	-34.7404	24.3276	53.368
31	2.3288	0.331	-0.0982	2.606	0.3451	1.0817	0.203	-0.1605	0.1195	0.3832	-0.0834	-0.2794	0.0992	0.0534	-0.096	0.4001	-0.0068	-0.0115	0.5664	0.0788	0.2748	-25.4825	25.126	80.9209
32	1.7191	0.3968	-0.0992	1.2349	0.6227	0.7828	-0.0584	0.0954	0.1236	0.0088	0.0296	0.1502	-0.0121	-0.0106	0.0018	0.1533	0.0375	0.0118	0.2385	0.0324	0.1744	-36.6207	22.3393	45.7548
33	1.5313	-1.9652	-0.0027	4.15	0.0098	0.4502	0.1353	0.0649	0.1917	-0.0816	-0.1398	-0.167	0.1261	0.1118	0.0273	0.1528	-0.0024	0.0371	0.2752	0.0387	0.1992	-5.2835	-7.4086	45.6468
34	1.0949	0.1756	-0.4449	0.6102	0.0434	1.2651	0.0087	-0.2498	0.0289	0.1958	0.0084	0.2095	0.0474	-0.2372	0.03	0.3055	-0.0159	-0.0159	0.2793	0.0088	0.1747	-20.9589	-18.3679	52.517
35	2.0535	0.1137	0.1809	2.3559	0.6024	1.5566	-0.091	-0.0224	0.318	0.1095	0.1772	0.064	0.0598	-0.009	-0.0366	0.4539	0.0382	0.0379	0.5395	0.2005	0.2692	-17.0628	-11.6141	80.4409
36	1.5736	0.1507	-0.1738	1.8133	0.3426	0.8973	-0.0689	-0.0515	-0.2341	-0.0412	0.0911	0.2918	0.2438	-0.1587	-0.0111	0.1918	-0.0344	0.0202	0.2156	0.0157	0.2211	-20.3541	-20.7407	44.9206
37	1.6458	-0.3634	-0.6465	1.7066	0.0545	0.2982	0.137	-0.0825	0.1515	0.1512	-0.0615	0.0027	0.0962	-0.1371	-0.0318	0.1929	0.0318	-0.0341	0.2543	-0.0148	0.2333	17.8429	-21.4993	44.7291
38	1.8692	-0.5009	-1.0047	1.1381	1.0755	1.5745	-0.0859	-0.1636	0.3318	0.1967	0.0957	-0.0133	0.1927	-0.0478	-0.0275	0.3724	0.023	-0.036	0.5381	0.1047	0.431	20.8004	-29.817	78.4359
39	1.4416	-0.362	-0.2706	0.993	-0.3252	0.4104	-0.0891	-0.0916	-0.2168	0.1457	-0.0401	0.0088	0.0254	0.0976	0.0775	0.238	-0.0195	0.0103	0.2129	0.0175	0.1984	23.7246	-34.4705	44.6473
40	2.3565	0.4675	-0.3295	1.9972	0.4727	0.9823	-0.0637	0.047	0.1975	0.1888	0.1486	0.1514	0.2406	0.0197	-0.0847	0.2032	-0.033	0.0263	0.2513	0.0016	0.1898	48.1765	-5.2754	44.3152
41	1.9572	2.0869	0.3655	3.1386	-0.049	1.0272	0.8208	-1.0592	0.4018	0.8458	-0.8363	1.1618	0.0212	-0.2154	-0.0257	0.6595	-0.2922	0.1064	1.1204	-0.1738	1.0557	55.5728	-8.131	77.8007
42	2.5777	0.799	-0.0807	1.6208	0.2498	1.1011	-0.1645	0.0658	-0.3759	0.0552	0.1844	-0.3659	0.1001	0.2135	-0.0012	0.2065	0.0426	0.0071	0.2152	0.0082	0.3202	61.9292	-8.7808	44.2001
43	2.4208	-0.1155	0.2262	1.4712	-0.5176	0.4183	0.016	-0.1484	-0.1061	-0.0056	0.0412	0.3067	0.039	-0.0204	-0.0491	0.1961	-0.01	-0.0142	0.2403	-0.0612	0.2259	54.3753	28.5791	44.2249
44	1.5821	-0.9454	-0.0936	2.6695	-0.8869	1.3164	-0.1486	-0.5958	-0.1634	0.5184	0.3706	0.5689	-0.2377	-0.2127	-0.1608	0.4684	0.1703	0.0498	0.7622	-0.05	0.3774	60.5718	32.7065	77.1291
45	1.0703	0.1052	-0.0092	1.4134	0.4788	1.2015	-0.0286	-0.1977	0.2086	0.0284	0.1705	-0.1033	-0.1487	0.0845	-0.173	0.2154	0.0158	-0.0011	0.3012	-0.0524	0.2056	65.7884	37.1943	43.9975
46	1.9439	0.6446	0.1732	2.1611	-0.5025	0.7422	0.0253	-0.1372	0.0643	0.1505	0.0572	-0.0425	0.0217	0.2028	-0.0198	0.1561	0.0509	0.0057	0.3012	-0.0657	0.2056	31.8915	54.6804	44.7028
47	2.3482	-0.5531	0.6386	1.416	0.0274	1.0739	-0.1888	-0.5027	-0.5407	0.6521	0.2922	0.5975	0.0097	-0.1224	-0.1082	0.669	0.1234	0.28	0.6508	-0.0525	0.693	31.3466	59.7423	76.878
48	1.5513	-0.43	0.4654	1.166	0.3095	0.9378	-0.0217	-0.214	0.4117	0.1719	0.0007	-0.0471	-0.1434	0.007	-0.0847	0.2292	-0.0477	0.1321	0.2829	-0.0803	0.5025	34.8532	69.6242	53.7349

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 2 through 134 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 135 through 385 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 386 through 525 )
4	X-RAY DIFFRACTION	4	chain 'B' and (resid 2 through 179 )
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 180 through 355 )
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 356 through 525 )
7	X-RAY DIFFRACTION	7	chain 'C' and (resid 2 through 64 )
8	X-RAY DIFFRACTION	8	chain 'C' and (resid 65 through 179 )
9	X-RAY DIFFRACTION	9	chain 'C' and (resid 180 through 385 )
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 386 through 525 )
11	X-RAY DIFFRACTION	11	chain 'D' and (resid 2 through 64 )
12	X-RAY DIFFRACTION	12	chain 'D' and (resid 65 through 179 )
13	X-RAY DIFFRACTION	13	chain 'D' and (resid 180 through 385 )
14	X-RAY DIFFRACTION	14	chain 'D' and (resid 386 through 525 )
15	X-RAY DIFFRACTION	15	chain 'E' and (resid 2 through 109 )
16	X-RAY DIFFRACTION	16	chain 'E' and (resid 110 through 358 )
17	X-RAY DIFFRACTION	17	chain 'E' and (resid 359 through 525 )
18	X-RAY DIFFRACTION	18	chain 'F' and (resid 2 through 134 )
19	X-RAY DIFFRACTION	19	chain 'F' and (resid 135 through 385 )
20	X-RAY DIFFRACTION	20	chain 'F' and (resid 386 through 525 )
21	X-RAY DIFFRACTION	21	chain 'G' and (resid 2 through 108 )
22	X-RAY DIFFRACTION	22	chain 'G' and (resid 109 through 179 )
23	X-RAY DIFFRACTION	23	chain 'G' and (resid 180 through 385 )
24	X-RAY DIFFRACTION	24	chain 'G' and (resid 386 through 525 )
25	X-RAY DIFFRACTION	25	chain 'H' and (resid 2 through 109 )
26	X-RAY DIFFRACTION	26	chain 'H' and (resid 110 through 179 )
27	X-RAY DIFFRACTION	27	chain 'H' and (resid 180 through 385 )
28	X-RAY DIFFRACTION	28	chain 'H' and (resid 386 through 525 )
29	X-RAY DIFFRACTION	29	chain 'I' and (resid 2 through 64 )
30	X-RAY DIFFRACTION	30	chain 'I' and (resid 65 through 179 )
31	X-RAY DIFFRACTION	31	chain 'I' and (resid 180 through 385 )
32	X-RAY DIFFRACTION	32	chain 'I' and (resid 386 through 525 )
33	X-RAY DIFFRACTION	33	chain 'J' and (resid 2 through 64 )
34	X-RAY DIFFRACTION	34	chain 'J' and (resid 65 through 179 )
35	X-RAY DIFFRACTION	35	chain 'J' and (resid 180 through 385 )
36	X-RAY DIFFRACTION	36	chain 'J' and (resid 386 through 525 )
37	X-RAY DIFFRACTION	37	chain 'K' and (resid 2 through 134 )
38	X-RAY DIFFRACTION	38	chain 'K' and (resid 135 through 385 )
39	X-RAY DIFFRACTION	39	chain 'K' and (resid 386 through 525 )
40	X-RAY DIFFRACTION	40	chain 'L' and (resid 2 through 134 )
41	X-RAY DIFFRACTION	41	chain 'L' and (resid 135 through 385 )
42	X-RAY DIFFRACTION	42	chain 'L' and (resid 386 through 525 )
43	X-RAY DIFFRACTION	43	chain 'M' and (resid 2 through 134 )
44	X-RAY DIFFRACTION	44	chain 'M' and (resid 135 through 385 )
45	X-RAY DIFFRACTION	45	chain 'M' and (resid 386 through 525 )
46	X-RAY DIFFRACTION	46	chain 'N' and (resid 2 through 134 )
47	X-RAY DIFFRACTION	47	chain 'N' and (resid 135 through 338 )
48	X-RAY DIFFRACTION	48	chain 'N' and (resid 339 through 525 )

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