PDB-7e1j: Crystal structure of Pr55Gag-matrix domain in complex with IP6 in...

ID or keywords:

Entry

Database: PDB / ID: 7e1j

Title

Crystal structure of Pr55Gag-matrix domain in complex with IP6 in space group C121

Components

Capsid protein p24

Keywords

VIRAL PROTEIN / HIV-1 / Matrix protein / Myo-inositol hexakisphosphate / Serial femtosecond X-ray crystallography / Ambient-temperature crystallography

Function / homology

Function and homology information

viral nucleocapsid / host cell cytoplasm / viral translational frameshifting / host cell nucleus / structural molecule activity / RNA binding / cytoplasm
Similarity search - Function

Biological species

Human immunodeficiency virus 1

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

FOURIER SYNTHESIS / Resolution: 2.72 Å

Authors

DeMirci, H. / Senda, T. / Destan, E.

Funding support

United States,

Turkey, 2items

Citation

Journal: to be published
Title: Crystal structure of Pr55Gag-matrix domain in complex with IP6 in space group C121
Authors: DeMirci, H. / Senda, T. / Destan, E.

History

Deposition	Feb 1, 2021	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Aug 4, 2021	Provider: repository / Type: Initial release
Revision 1.1	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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Download

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Validation report

Summary document	7e1j_validation.pdf.gz	3.7 MB	Display	wwPDB validaton report
Full document	7e1j_full_validation.pdf.gz	3.7 MB	Display
Data in XML	7e1j_validation.xml.gz	33.5 KB	Display
Data in CIF	7e1j_validation.cif.gz	41.7 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/e1/7e1j ftp://data.pdbj.org/pub/pdb/validation_reports/e1/7e1j	HTTPS FTP

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Related structure data

Similar structure data	7e1j-2 3oeq-1 1ylf-d 1pvh-2 2cns-d 4qik-2 4wi7-d 2e9s-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	#163 - Jul 2013 HIV Capsid similarity (2) #110 - Feb 2009 Auxin and TIR1 Ubiquitin Ligase similarity (1) #225 - Sep 2018 Phytase similarity (1) #218 - Feb 2018 EPSP Synthase and Weedkillers similarity (1) #88 - Apr 2007 Clathrin similarity (1)

Deposited unit

A: Capsid protein p24

B: Capsid protein p24

C: Capsid protein p24

D: Capsid protein p24

E: Capsid protein p24

F: Capsid protein p24

hetero molecules

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

1

A: Capsid protein p24

B: Capsid protein p24

C: Capsid protein p24

hetero molecules

defined by author
Evidence: native gel electrophoresis
41.9 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: Capsid protein p24

E: Capsid protein p24

F: Capsid protein p24

hetero molecules

defined by author
41.9 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	176.182, 67.414, 97.499
Angle α, β, γ (deg.)	90.000, 123.150, 90.000
Int Tables number	5
Space group name H-M	C121

#1: Protein	Capsid protein p24 / Matrix protein p17 / Nucleocapsid protein p7 Mass: 13303.257 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus 1 / Gene: gag / Production host: Escherichia coli (E. coli) / References: UniProt: T2CJ20
#2: Chemical	ChemComp-IHP / INOSITOL HEXAKISPHOSPHATE / MYO-INOSITOL HEXAKISPHOSPHATE / INOSITOL 1,2,3,4,5,6-HEXAKISPHOSPHATE Mass: 660.035 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₆H₁₈O₂₄P₆ / Feature type: SUBJECT OF INVESTIGATION
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 69 / Source method: isolated from a natural source / Formula: H₂O
Has ligand of interest	Y

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 3

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Sample preparation

Crystal	Density Matthews: 3.2 Å³/Da / Density % sol: 61.53 %
Crystal grow	Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: PEG 3350 and 100 mM MES

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

Photon Factory

/ Beamline: BL-1A / Wavelength: 1.1 Å

Detector

Type: DECTRIS EIGER X 4M / Detector: PIXEL / Date: May 2, 2017

Radiation

Monochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1.1 Å / Relative weight: 1

Reflection

Resolution: 2.72→48.75 Å / Num. obs: 25978 / % possible obs: 99.9 % / Redundancy: 6.8 % / CC_1/2: 0.998 / R_merge(I) obs: 0.099 / R_pim(I) all: 0.041 / R_rim(I) all: 0.107 / Net I/σ(I): 14.3 / Num. measured all: 177762 / Scaling rejects: 4

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. measured all	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Net I/σ(I) obs	% possible all
2.72-2.85	6.9	0.802	23881	3438	0.881	0.327	0.867	2.4	99.9
9.02-48.75	6.4	0.037	4854	754	0.999	0.015	0.04	44.6	99.1

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Processing

Software

Name	Version	Classification
XDS		data reduction
Aimless	0.5.31	data scaling
PHENIX	DEV-3318	refinement
PDB_EXTRACT	3.27	data extraction
PHENIX		phasing

Refinement

Method to determine structure:

FOURIER SYNTHESIS / Resolution: 2.72→44.414 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 28.42 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2723	1306	5.03 %
R_work	0.213	24651	-
obs	0.2159	25957	99.85 %

Solvent computation

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

Displacement parameters

B_iso max: 191.83 Å² / B_iso mean: 67.9589 Å² / B_iso min: 30 Å²

Refinement step

Cycle: final / Resolution: 2.72→44.414 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	5290	0	324	69	5683
B_iso mean	-	-	143.69	54.86	-
Num. residues	-	-	-	-	665

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / % reflection obs: 100 %

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work
2.7201-2.829	0.3603	131	0.3143	2732
2.829-2.9577	0.3139	170	0.2728	2698
2.9577-3.1136	0.279	128	0.2512	2711
3.1136-3.3086	0.3425	169	0.2614	2686
3.3086-3.5639	0.2975	144	0.2343	2743
3.5639-3.9224	0.2761	163	0.2007	2728
3.9224-4.4895	0.2527	160	0.1802	2743
4.4895-5.6545	0.2355	106	0.1917	2781
5.6545-44.4	0.2389	135	0.1986	2829

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	0.0411	0.0483	-0.1672	0.2686	0.2515	0.5518	-0.0703	0.3414	0.1703	0.1017	-0.3117	0.5355	0.4998	-0.4569	-0.0059	0.5925	0.0435	-0.0233	0.517	0.0246	0.5524	32.0681	13.5818	53.9086
2	0.7991	0.0374	-0.4385	0.1817	0.1318	0.585	0.0493	0.7254	0.1782	-0.2716	0.1797	0.1827	-0.0744	-0.2992	0.0118	0.6572	0.1042	-0.0334	0.3929	0.1113	0.4508	41.4779	12.9145	43.0467
3	0.2474	-0.0959	-0.1786	0.1322	0.101	0.1433	-0.1657	-0.129	-0.264	-0.7368	-0.2832	-0.1172	1.3185	0.4108	-0.0042	0.5301	0.0897	0.0001	0.446	0.0634	0.4229	42.6787	6.202	58.499
4	0.0241	0.0183	-0.116	0.1805	-0.0509	0.5974	-0.1538	-0.9712	0.0876	0.6785	0.044	-0.1283	-0.1084	-0.2457	0.0001	0.4879	0.1201	-0.0977	0.5189	-0.0874	0.5311	44.3725	17.0805	64.2851
5	0.345	0.0702	0.2677	0.3111	-0.4076	0.5254	-0.092	-0.4528	0.5345	-0.2123	0.1719	-0.1969	-0.1455	0.2545	-0.0004	0.5604	0.0482	-0.008	0.4228	-0.0225	0.551	48.8669	16.0282	55.8334
6	1.5339	-0.069	0.2589	0.0574	-0.0154	0.0486	-0.2386	0.6095	0.169	-0.2302	0.0076	0.2329	-0.3118	0.0257	0.0144	0.6291	0.0465	-0.0487	0.3629	0.0996	0.8456	37.6377	24.7134	49.7443
7	0.5986	-0.441	-0.3014	0.6974	0.2254	0.0942	-0.1917	-0.1392	1.8195	-0.5153	0.5129	0.4304	-0.1118	0.5414	0.0663	0.6164	0.0134	0.1277	0.6458	0.1341	0.8866	47.6983	25.7613	50.9445
8	0.472	0.0505	0.4935	0.4215	0.0178	0.7257	0.0449	-0.1591	0.1848	-1.0141	0.2698	0.3918	-0.1563	-0.8714	0.0093	1.223	-0.0242	-0.2428	1.2467	-0.1263	1.1935	52.723	35.697	59.976
9	0.5173	0.3579	-0.0651	0.3198	0.1586	0.1436	-0.5553	0.0122	-0.745	0.3487	0.152	-0.2256	0.4257	0.4698	-0.0095	0.4936	0.1096	-0.0482	0.5723	0.0065	0.4482	50.7807	-4.796	92.1104
10	0.8731	-1.3183	-0.5358	2.005	0.6165	1.0794	-0.7376	0.6039	-0.8391	0.9293	0.491	1.3709	0.637	-0.5409	-0.1101	0.3805	0.0662	-0.0358	0.4582	0.1119	0.4153	38.6124	3.3268	90.0752
11	0.1607	0.1823	-0.1031	0.3306	-0.191	0.0443	0.1461	0.9561	-0.9272	-0.2473	0.1323	-0.4876	-0.2338	0.1204	0.0028	0.5862	0.072	0.0355	0.5154	-0.0627	0.4766	50.0433	-2.4238	79.0291
12	0.1285	0.1485	-0.306	0.2992	-0.2603	1.0671	0.1762	-0.0995	0.2654	-0.2949	-0.7972	-0.8063	0.1998	1.5469	-0.0439	0.4789	0.0603	0.0213	0.711	0.0134	0.4541	58.4398	6.5604	81.9679
13	0.4191	0.0712	-0.3963	0.0478	-0.0864	0.4542	0.0067	-0.2646	0.2107	-0.0852	-0.1981	0.09	0.0172	-0.594	-0	0.4241	0.0253	-0.0803	0.5632	0.024	0.3598	49.1497	8.9826	82.0969
14	0.0203	-0.0407	0.0637	0.3807	-0.3342	0.2831	0.0738	-0.6469	-0.7696	0.3007	0.72	0.7226	-0.7397	-0.4797	-0.0099	0.852	0.1052	-0.0677	0.6598	-0.0332	0.5217	47.831	8.4781	96.9669
15	0.2407	-0.0499	0.1414	0.0856	0.1063	0.2424	-0.3473	-0.6858	0.661	0.4142	-0.0656	0.0181	-0.7601	-0.103	0.0067	0.8045	0.0687	-0.0645	0.5402	-0.0888	0.6467	48.0914	15.6503	90.4301
16	8.3028	2.0005	5.6406	1.9997	8.1002	3.8326	-0.2682	0.3425	-0.1888	-0.7781	0.384	-0.6227	-1.1705	0.2623	-0.3524	1.53	-0.0019	0.2113	1.2304	0.3714	1.2289	54.6961	19.2204	85.8689
17	0.1642	-0.0695	-0.1827	0.2669	0.1687	0.2735	-0.3439	0.2908	-0.0197	0.3277	0.3447	0.1332	0.0903	0.1017	0.0007	0.4509	0.0711	0.2098	0.5391	-0.0071	0.5165	74.8904	-4.3835	51.93
18	0.211	0.0445	-0.0628	0.0112	0.0233	0.0383	-0.0101	-0.046	-0.2193	0.4021	0.2485	-0.5006	0.2068	0.4971	-0.0122	0.5231	0.1249	-0.005	0.6123	0.0008	0.5757	78.4023	-8.4083	65.2425
19	0.0252	-0.1017	-0.0697	0.1665	0.0936	0.1178	-0.0963	-0.6721	-0.6721	-0.6	0.5386	0.8881	-0.0609	-0.1973	-0.0015	0.4813	0.1149	-0.0302	0.5228	0.0385	0.5847	63.88	-2.995	59.6265
20	0.1367	-0.1457	0.2353	0.5896	-0.0218	0.2718	0.5453	0.5309	0.2129	-0.471	-0.053	-0.2439	-0.7363	-0.6236	0.0012	0.519	0.092	0.1335	0.5097	0.0615	0.5495	67.3215	9.1438	59.3042
21	0.4261	-0.3217	-0.0861	0.2428	0.2422	0.234	0.0014	-0.6891	-0.3122	0.1646	0.2114	-0.262	-0.3252	0.2651	-0.002	0.4608	0.0235	0.0716	0.5973	0.0335	0.5139	70.5671	3.9426	66.6815
22	0.8353	-0.6758	0.3864	0.8267	0.4101	2.637	-0.1752	-0.7754	1.0421	-0.1855	1.4909	-0.302	1.2998	0.8975	0.0864	0.4819	-0.1621	0.0249	0.7918	-0.1304	0.67	84.4251	1.4315	60.9062
23	0.4044	-0.4248	0.1726	0.5084	-0.0794	0.1973	-0.3016	-1.043	0.1778	1.4225	0.4151	-0.9551	-0.7482	0.5296	0.0268	0.6732	-0.073	-0.0222	0.6817	-0.1121	0.5602	81.3768	7.0024	68.2456
24	0.0274	-0.2109	0.4037	0.4966	-0.8066	1.3518	-0.8667	1.0113	-0.5237	0.2887	0.2295	-0.471	-0.8437	0.156	-0.0559	1.0684	-0.4385	0.1744	1.6506	-0.4369	1.7094	81.505	16.798	68.488
25	-0.0131	0.0191	0.0925	0.3045	0.1925	0.0138	-0.0881	-0.5479	-0.5087	0.3912	-0.1348	-0.0818	0.3927	-0.0071	-0.0014	0.4986	0.0493	-0.0493	0.5204	0.0532	0.3998	27.7022	4.379	50.6192
26	0.6592	0.005	-0.045	0.1672	0.5007	1.4911	-0.776	0.4571	-0.1576	-0.9487	0.9698	-0.6603	-0.6623	1.917	0.0237	0.4736	-0.0691	0.1103	0.4294	-0.0169	0.4493	33.025	4.4137	37.2594
27	1.36	0.2399	0.5345	0.0127	0.0826	0.2077	-0.2999	-0.5828	1.2315	-0.0915	0.1693	0.0112	-0.3814	-0.0833	-0.0118	0.3874	0.0743	-0.0387	0.2261	0.0135	0.4547	18.4102	10.6739	42.8883
28	0.4781	0.377	-0.4179	0.4568	-0.0539	0.4716	-0.2475	-0.1344	-0.1632	0.153	-0.0962	0.3353	0.233	-0.7404	-0.0001	0.4436	0.0226	0.0174	0.4899	0.0494	0.5112	12.6885	-0.7319	43.3018
29	0.6111	-0.4053	0.2919	0.3761	-0.0072	0.1549	0.0961	0.1508	0.0469	-0.4482	-0.0818	-0.2647	0.4157	-0.1172	-0	0.4689	0.0703	0.0055	0.4573	0.0884	0.4203	18.674	0.7897	35.4495
30	0.1542	0.0708	0.0997	0.1581	0.0038	0.0586	0.601	0.0856	-0.2715	0.8312	-0.4536	-0.924	-0.6376	0.4457	-0.0409	0.5549	0.0719	-0.1637	0.3813	0.1148	0.6378	30.6752	-6.7354	41.9817
31	0.0428	0.0217	-0.0846	0.2674	0.0532	0.2168	0.1688	-0.1515	-0.6257	-0.1773	-0.0831	-0.8557	0.0292	0.4743	0.0039	0.3882	-0.0185	-0.0308	0.4643	0.0361	0.5878	24.0434	-8.4193	34.7791
32	0.325	-0.3779	-0.1253	0.4454	0.1307	0.0934	-0.1237	0.2581	0.1111	-0.0781	0.0359	0.3078	-0.1572	-0.455	-0.0031	1.0308	-0.0639	-0.4142	0.9962	0.004	1.2742	15.6079	-12.4155	33.946
33	0.1705	-0.2098	-0.1586	0.4064	-0.0588	0.9617	-0.1234	-0.3464	-0.232	0.1676	0.5216	0.6517	-0.693	-0.1327	0.0236	0.3556	0.0356	0.0317	0.4899	0.0248	0.7042	-16.7193	18.6274	49.3243
34	0.0548	0.1513	0.1286	0.1633	0.1322	0.1004	-0.6077	-0.8379	-0.0446	1.5715	0.5766	0.2393	-0.2876	-0.3035	0.0006	0.7568	0.1351	0.0977	0.6073	0.0958	0.6766	-8.8719	13.5684	59.0367
35	0.0338	-0.1362	-0.0321	0.2661	0.088	-0.0011	-0.4517	-0.2851	-0.0725	0.1017	-0.1612	0.101	-0.2362	-0.4447	-0.001	0.4268	0.0274	0.0008	0.4258	0.0572	0.501	-3.1908	17.9847	43.9458
36	0.0808	-0.0738	0.1096	0.2875	-0.2401	0.3147	0.3474	0.6828	-0.4592	-0.6983	-0.3221	0.8352	0.2585	-0.362	-0.0001	0.3101	-0.0126	-0.0249	0.4474	-0.0621	0.6361	-9.2022	9.0942	37.7807
37	0.339	0.0847	-0.186	0.4433	0.312	0.3456	-0.0528	-0.5238	-0.4591	0.3504	0.023	0.3873	0.4026	-0.0339	0.0011	0.397	-0.018	0.0543	0.356	0.0115	0.5801	-5.5774	6.692	46.4089
38	1.4515	-1.0343	1.0041	1.6415	0.7373	3.3094	-0.9712	0.2089	-0.2367	0.4256	-0.4383	0.3219	0.046	-0.205	-0.5307	0.5947	-0.1967	0.2081	0.7907	0.2809	0.9737	-18.8341	7.1024	53.9787
39	0.5212	0.5768	-0.1134	0.5746	-0.1576	0.024	-0.3082	-0.9331	-0.7838	-0.3883	0.35	0.6067	0.7455	-0.1833	-0.0373	0.678	0.0631	0.2026	0.5243	-0.0321	0.8794	-13.1111	0.1734	51.5307
40	0.0584	-0.0872	0.2013	0.124	-0.3338	1.1572	-0.0444	0.3669	0.1764	-0.308	0.0796	-0.0649	0.3012	0.0664	0.0044	1.3806	0.0044	0.3093	1.1556	0.0785	1.7359	-15.4949	-7.1162	44.8852
41	0.1318	0.1507	-0.1339	0.1596	0.0327	0.3289	-0.3328	0.8752	0.2813	-0.1056	0.053	0.4017	0.4465	0.5053	-0.0023	0.6388	0.1114	0.052	0.5028	0.0981	0.3636	10.6371	19.5376	9.1656
42	0.5401	-0.0637	0.034	0.6744	-0.0196	0.0505	0.5137	1.3229	0.4815	-0.3911	0.0503	-0.0658	0.2808	-0.3913	0.0419	0.4012	0.015	-0.0253	0.574	0.0662	0.3294	-1.5821	24.5709	11.9938
43	0.1023	-0.1712	-0.1219	0.4022	0.1058	0.0462	-0.414	-0.3127	0.2754	0.3862	0.213	-0.4071	-0.7997	-0.2343	0.0015	0.4875	0.1501	-0.0742	0.4669	0.0076	0.3391	8.8778	18.8916	24.3291
44	0.5126	0.2058	-0.5115	0.773	-0.1154	1.0249	-0.0669	-0.2312	-0.9874	-0.434	-0.2497	-0.7149	0.8665	0.8132	-0.0689	0.6169	0.1118	-0.0034	0.4357	-0.0321	0.3396	8.0373	7.0354	20.3745
45	0.191	0.2727	-0.0093	0.586	-0.4653	0.7004	-0.2953	0.1278	-0.0648	-0.199	-0.2972	0.5296	0.539	-1.1725	-0.0006	0.4339	-0.0481	-0.0306	0.4789	-0.1339	0.4023	-0.0586	12.0312	20.1718
46	1.1107	-0.4982	-0.4822	0.7656	0.6631	0.5426	0.2068	-0.1287	0.3177	-0.8133	-0.2258	0.3046	0.5725	-0.3831	0.2725	0.9743	-0.4215	-0.8242	0.2036	-1.2075	-2.0236	-0.1651	13.9444	4.9719
47	0.3333	0.1348	-0.5642	0.046	-0.22	0.9909	0.0311	0.8475	-0.2897	-0.6427	0.2844	0.3092	-0.2232	-0.3087	0.2315	0.6429	-0.0869	-0.1704	0.4759	-0.2212	0.4708	-5.4986	9.2464	10.6261
48	0.1277	-0.0682	0.0606	0.2799	-0.0983	0.0032	-0.1918	-1.2018	0.4723	-0.0621	-0.2047	-0.0345	-0.2308	-0.0403	-0.0095	1.0755	0.1312	-0.1395	1.3223	-0.18	1.471	-4.995	-4.444	8.803

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 0 through 17 )	A	0 - 17
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 18 through 30 )	A	18 - 30
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 31 through 42 )	A	31 - 42
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 43 through 64 )	A	43 - 64
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 65 through 89 )	A	65 - 89
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 90 through 95 )	A	90 - 95
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 96 through 106 )	A	96 - 106
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 107 through 115 )	A	107 - 122
9	X-RAY DIFFRACTION	9	chain 'B' and (resid -1 through 17 )	B	-1 - 17
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 18 through 30 )	B	18 - 30
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 31 through 42 )	B	31 - 42
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 43 through 64 )	B	43 - 64
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 65 through 89 )	B	65 - 89
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 90 through 95 )	B	90 - 95
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 96 through 106 )	B	96 - 106
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 107 through 107 )	B	107 - 122
17	X-RAY DIFFRACTION	17	chain 'C' and (resid -1 through 17 )	C	-1 - 17
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 18 through 30 )	C	18 - 30
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 31 through 42 )	C	31 - 42
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 43 through 64 )	C	43 - 64
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 65 through 89 )	C	65 - 89
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 90 through 95 )	C	90 - 95
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 96 through 106 )	C	96 - 106
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 107 through 109 )	C	107 - 122
25	X-RAY DIFFRACTION	25	chain 'D' and (resid -1 through 17 )	D	-1 - 17
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 18 through 30 )	D	18 - 30
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 31 through 42 )	D	31 - 42
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 43 through 64 )	D	43 - 64
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 65 through 89 )	D	65 - 89
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 90 through 95 )	D	90 - 95
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 96 through 106 )	D	96 - 106
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 107 through 108 )	D	107 - 122
33	X-RAY DIFFRACTION	33	chain 'E' and (resid 3 through 17 )	E	3 - 17
34	X-RAY DIFFRACTION	34	chain 'E' and (resid 18 through 30 )	E	18 - 30
35	X-RAY DIFFRACTION	35	chain 'E' and (resid 31 through 42 )	E	31 - 42
36	X-RAY DIFFRACTION	36	chain 'E' and (resid 43 through 64 )	E	43 - 64
37	X-RAY DIFFRACTION	37	chain 'E' and (resid 65 through 89 )	E	65 - 89
38	X-RAY DIFFRACTION	38	chain 'E' and (resid 90 through 95 )	E	90 - 95
39	X-RAY DIFFRACTION	39	chain 'E' and (resid 96 through 106 )	E	96 - 106
40	X-RAY DIFFRACTION	40	chain 'E' and (resid 107 through 110 )	E	107 - 122
41	X-RAY DIFFRACTION	41	chain 'F' and (resid 2 through 17 )	F	2 - 17
42	X-RAY DIFFRACTION	42	chain 'F' and (resid 18 through 30 )	F	18 - 30
43	X-RAY DIFFRACTION	43	chain 'F' and (resid 31 through 42 )	F	31 - 42
44	X-RAY DIFFRACTION	44	chain 'F' and (resid 43 through 64 )	F	43 - 64
45	X-RAY DIFFRACTION	45	chain 'F' and (resid 65 through 89 )	F	65 - 89
46	X-RAY DIFFRACTION	46	chain 'F' and (resid 90 through 95 )	F	90 - 95
47	X-RAY DIFFRACTION	47	chain 'F' and (resid 96 through 106 )	F	96 - 106
48	X-RAY DIFFRACTION	48	chain 'F' and (resid 107 through 112 )	F	107 - 122

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