PDB-4l6i: Methylthioadenosine phosphorylase from Schistosoma mansoni in com...

ID or keywords:

Entry

Database: PDB / ID: 4l6i

Title

Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with adenine

Components

S-methyl-5'-thioadenosine phosphorylase

Keywords

TRANSFERASE / phosphorylase / Nucleoside phosphorylase

Function / homology

Function and homology information

S-methyl-5'-thioadenosine phosphorylase / S-methyl-5-thioadenosine phosphorylase activity / L-methionine salvage from methylthioadenosine / purine ribonucleoside salvage / nucleus / cytosol
Similarity search - Function

Biological species

Schistosoma mansoni (invertebrata)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.1 Å

Authors

Torini, J.R. / DeMarco, R. / Brandao-Neto, J. / Pereira, H.M.

Citation

Journal: Plos Negl Trop Dis / Year: 2016
Title: Crystal Structure of Schistosoma mansoni Adenosine Phosphorylase/5'-Methylthioadenosine Phosphorylase and Its Importance on Adenosine Salvage Pathway.
Authors: Torini, J.R. / Brandao-Neto, J. / DeMarco, R. / Pereira, H.D.

History

Deposition	Jun 12, 2013	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jun 25, 2014	Provider: repository / Type: Initial release
Revision 1.1	Dec 21, 2016	Group: Database references
Revision 1.2	Feb 28, 2024	Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4l6i.cif.gz	670.1 KB	Display	PDBx/mmCIF format
PDB format	pdb4l6i.ent.gz	556.2 KB	Display	PDB format
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Validation report

Summary document	4l6i_validation.pdf.gz	517.7 KB	Display	wwPDB validaton report
Full document	4l6i_full_validation.pdf.gz	534.7 KB	Display
Data in XML	4l6i_validation.xml.gz	65.2 KB	Display
Data in CIF	4l6i_validation.cif.gz	90.9 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/l6/4l6i ftp://data.pdbj.org/pub/pdb/validation_reports/l6/4l6i	HTTPS FTP

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Related structure data

Related structure data	4l5aC 4l5cC 4l5yC 5f73C 5f76C 5f77C 5f78C 5f7jC 5f7oC 5f7xC 5f7zC 5fakC C: citing same article (ref.)
Similar structure data	5fak-1 5f7j-2 5f7x-d 5fak-2 4l5a-2 4l5y-1 4l5c-1 5f76-d 5f77-d 3d1v-1 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	#210 - Jun 2017 Adenine Riboswitch in Action similarity (1) #130 - Oct 2010 Riboswitches similarity (1) #156 - Dec 2012 ABO Blood Type Glycosyltransferases similarity (1)

Deposited unit

A: S-methyl-5'-thioadenosine phosphorylase

B: S-methyl-5'-thioadenosine phosphorylase

C: S-methyl-5'-thioadenosine phosphorylase

D: S-methyl-5'-thioadenosine phosphorylase

E: S-methyl-5'-thioadenosine phosphorylase

F: S-methyl-5'-thioadenosine phosphorylase

hetero molecules

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

1

A: S-methyl-5'-thioadenosine phosphorylase

B: S-methyl-5'-thioadenosine phosphorylase

C: S-methyl-5'-thioadenosine phosphorylase

hetero molecules

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

2

D: S-methyl-5'-thioadenosine phosphorylase

E: S-methyl-5'-thioadenosine phosphorylase

F: S-methyl-5'-thioadenosine phosphorylase

hetero molecules

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

Unit cell

Length a, b, c (Å)	81.270, 82.550, 150.300
Angle α, β, γ (deg.)	90.000, 100.610, 90.000
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	S-methyl-5'-thioadenosine phosphorylase / 5'-methylthioadenosine phosphorylase Mass: 35259.480 Da / Num. of mol.: 6 / Fragment: SmMTAP Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schistosoma mansoni (invertebrata) / Strain: BH / Gene: SmMTAP / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: I0B503, S-methyl-5'-thioadenosine phosphorylase
#2: Chemical	ChemComp-ADE / ADENINE Mass: 135.127 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₅H₅N₅
#3: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO₄
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 634 / 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: 2.34 Å³/Da / Density % sol: 47.49 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 100mM Bris-tris or Mes, 14-18% PEG3350, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

LNLS

/ Beamline: W01B-MX2 / Wavelength: 1.459 Å

Detector

Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jan 30, 2010 / Details: DCM

Radiation

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

Radiation wavelength

Wavelength: 1.459 Å / Relative weight: 1

Reflection

Resolution: 2.1→147.73 Å / Num. all: 104402 / Num. obs: 104402 / % possible obs: 91.4 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 4.9 % / R_sym value: 0.121 / Net I/σ(I): 8.3

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Mean I/σ(I) obs	Num. measured all	Num. unique all	R_sym value	% possible all
2.1-2.21	5.1	0.511	1.4	84973	16599	0.511	100
2.21-2.35	5.1	0.455	1.4	60693	12009	0.455	76.5
2.35-2.51	5.2	0.254	2.8	76789	14768	0.254	100
2.51-2.71	5.2	0.201	2.9	58412	11290	0.201	81.9
2.71-2.97	5.1	0.134	5.1	65066	12666	0.134	100
2.97-3.32	4.9	0.113	6	56585	11459	0.113	99.9
3.32-3.83	4.6	0.1	5	36069	7769	0.1	76.7
3.83-4.7	4.3	0.062	9.5	32352	7504	0.062	87.3
4.7-6.64	4.1	0.053	11	27733	6693	0.053	100
6.64-30.01	4.4	0.048	11.6	15929	3645	0.048	96.8

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Processing

Software

Name	Version	Classification
SCALA	3.3.20	data scaling
PHENIX	1.8.2_1309	refinement
PDB_EXTRACT	3.11	data extraction
MAR345dtb		data collection
MOSFLM		data reduction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.1→30.01 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.8045 / SU ML: 0.24 / σ(F): 1.33 / Phase error: 26.39 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.241	5227	5.03 %	Random
R_work	0.1923	-	-	-
all	0.1947	104402	-	-
obs	0.1947	103947	91.04 %	-

Solvent computation

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

Displacement parameters

B_iso max: 125.28 Å² / B_iso mean: 30.4438 Å² / B_iso min: 7.52 Å²

Refinement step

Cycle: LAST / Resolution: 2.1→30.01 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13062	0	60	634	13756

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	13382
X-RAY DIFFRACTION	f_angle_d	1.078	18152
X-RAY DIFFRACTION	f_chiral_restr	0.066	2098
X-RAY DIFFRACTION	f_plane_restr	0.005	2324
X-RAY DIFFRACTION	f_dihedral_angle_d	13.262	4825

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.1-2.1239	0.2917	197	0.2255	3605	3802	100
2.1239-2.1489	0.2548	189	0.2187	3601	3790	100
2.1489-2.1751	0.27	176	0.2056	3580	3756	100
2.1751-2.2026	0.2732	196	0.2195	3559	3755	100
2.2026-2.2315	0.347	168	0.2621	3570	3738	98
2.2315-2.2621	0.4815	18	0.3145	388	406	97
2.2621-2.2944	0.3409	145	0.2633	3167	3312	96
2.2944-2.3286	0.2838	207	0.2082	3570	3777	100
2.3286-2.365	0.2848	188	0.1971	3611	3799	100
2.365-2.4038	0.2493	208	0.2045	3545	3753	100
2.4038-2.4452	0.2508	194	0.2014	3586	3780	100
2.4452-2.4897	0.3009	192	0.2118	3604	3796	100
2.4897-2.5375	0.27	189	0.2078	3645	3834	100
2.5375-2.5893	0.2564	216	0.2014	3538	3754	100
2.5893-2.6456	0.2967	195	0.2177	3605	3800	100
2.6456-2.7071	0.3096	70	0.2274	1201	1271	34
2.7071-2.7747	0.2385	179	0.2028	3566	3745	99
2.7747-2.8497	0.279	183	0.1953	3615	3798	100
2.8497-2.9335	0.2585	181	0.213	3594	3775	100
2.9335-3.0281	0.2903	190	0.2165	3639	3829	100
3.0281-3.1362	0.2642	190	0.2105	3614	3804	100
3.1362-3.2616	0.2509	204	0.2101	3577	3781	100
3.2616-3.4098	0.2567	181	0.2033	3626	3807	100
3.4098-3.5893	0.2649	124	0.2012	2529	2653	70
3.5893-3.8138	0.2062	127	0.1831	2448	2575	68
3.8138-4.1076	0.1981	130	0.1625	2603	2733	71
4.1076-4.5197	0.1745	198	0.1401	3611	3809	100
4.5197-5.1708	0.1689	176	0.1425	3659	3835	100
5.1708-6.5038	0.1863	217	0.1655	3639	3856	100
6.5038-30.0132	0.2132	199	0.1791	3625	3824	97

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	2.0184	0.2908	-0.5271	3.2733	1.6835	1.8135	0.3675	0.5762	0.3658	-0.8801	-0.3176	-0.2055	-0.2579	0.2128	-0.0564	0.2605	0.0634	0.0841	0.3008	0.0413	0.4802	15.0572	-22.9714	-74.4023
2	1.3873	-0.4076	-0.3663	0.9209	-0.2344	1.4454	-0.0842	0.1164	-0.0302	-0.1478	0.0201	-0.3005	0.1792	0.2311	-0.0073	0.2118	0.0553	0.0914	0.1245	-0.0525	0.3352	12.13	-29.4813	-71.7923
3	2.2588	-0.9298	0.4112	2.0466	0.0398	0.9534	0.1269	0.1549	-0.3145	-0.1473	-0.1284	-0.1427	0.1251	0.0447	0.006	0.1279	0.0296	0.0118	0.0914	-0.0133	0.1871	5.8466	-23.9129	-67.5968
4	1.3419	0.3063	-0.3187	1.7753	-0.4141	1.719	-0.0029	-0.1171	-0.0954	0.0653	-0.0653	-0.0284	0.0627	0.0278	0.049	0.1058	-0.0416	-0.0165	0.0892	0.0019	0.1599	3.0837	-17.8275	-56.75
5	1.392	0.0752	-0.1061	0.8685	0.0969	0.9315	0.076	-0.0768	0.1388	0.1256	-0.0623	-0.1575	-0.2579	0.1597	-0.013	0.152	-0.0578	-0.0135	0.1106	0.0012	0.1427	8.1483	-7.8747	-60.9789
6	5.0087	0.796	-2.2821	6.0392	3.3273	3.3437	-0.0729	0.4429	0.9297	-0.3445	-0.0482	0.4752	-1.1152	-0.3175	0.155	0.3797	0.0777	-0.0123	0.1832	0.0306	0.2927	-4.5127	1.7573	-69.4431
7	2.5646	0.1186	-0.6013	1.3299	0.0687	1.299	0.0055	-0.0274	-0.168	-0.0217	-0.1227	-0.4384	0.098	0.3973	0.1103	0.126	-0.0069	-0.0288	0.1264	-0.0565	0.2062	14.8043	-18.4806	-62.7399
8	2	-7.25	2	2	-0.7818	2	-0.0883	0.0552	-0.036	-0.0138	0.0065	0.0684	0.0724	-0.0523	0.0639	0.1462	-0.0452	-0.0573	0.1999	-0.1546	0.1887	-1.3212	-8.1826	-68.1467
9	0.8915	-0.0501	0.1019	6.5208	-2.0601	5.8767	-0.1751	-0.4185	-0.6299	0.2236	-0.071	-0.2417	0.354	0.2534	0.243	0.2724	-0.0211	0.0839	0.1865	-0.0038	0.2457	-15.1159	-35.8924	-29.4867
10	0.6557	0.0408	-0.5962	0.5489	-0.3447	0.8609	-0.1419	0.0123	-0.3403	0.039	-0.0452	0.0431	0.3285	-0.1231	0.149	0.3051	-0.1346	0.0421	0.2198	-0.0203	0.2789	-16.0336	-35.2186	-38.0694
11	1.663	-0.5794	-0.7348	1.1048	-0.707	1.4027	-0.0057	-0.0525	0.0909	0.2119	-0.0657	0.0254	-0.2522	-0.0894	0.0474	0.269	-0.0892	0.0214	0.15	-0.0183	0.1619	-14.0403	-17.0692	-34.6123
12	0.391	-0.2265	-0.7668	1.7165	-0.4021	1.9469	0.0927	-0.1944	-0.0514	0.237	-0.1424	-0.1246	-0.0801	0.1408	0.0334	0.2013	-0.0806	-0.0254	0.1673	0.0113	0.1429	-5.2819	-17.5795	-41.0832
13	0.9211	0.3428	-1.2706	1.5436	-0.7542	3.166	-0.0235	-0.4369	-0.2993	0.2722	-0.0916	0.1605	0.0157	-0.1177	0.09	0.3089	-0.1013	0.071	0.1052	-0.057	0.2219	-17.3155	-25.6358	-30.6496
14	8.7125	4.438	5.1486	8.2514	-3.4292	9.156	0.0956	0.3431	0.6697	-0.1773	0.2833	0.5199	0.4294	-0.1085	-0.3697	0.2471	-0.0218	0.0454	0.5138	-0.0136	0.3144	-1.1948	-20.8085	-40.496
15	0.693	-0.3206	-0.0323	0.8955	-0.3444	0.1755	0.1293	0.2717	-0.3028	-0.176	0.0551	0.5958	0.1186	-0.5699	-0.2679	0.101	0.1709	-0.2055	0.923	-0.2269	0.4743	-38.4027	-12.7287	-72.9495
16	0.4198	-0.1809	0.5719	0.6772	0.2499	1.2719	0.0896	0.4136	-0.2609	-0.0878	-0.3269	0.4926	0.1787	-0.8385	-0.1502	0.1869	0.0408	-0.0651	0.5705	-0.1962	0.3057	-30.7153	-17.0061	-71.3483
17	2.2571	-0.6112	-1.1234	1.0052	0.3429	1.9766	0.1376	0.1529	-0.1087	0.0295	-0.1751	0.0406	-0.0482	-0.3808	0	0.1128	0.0323	-0.0515	0.1884	-0.0357	0.1369	-17.9597	-9.9625	-64.7341
18	0.8826	-0.1066	-0.1084	0.4694	0.0176	0.708	0.1587	0.2259	0.1034	-0.0278	-0.1455	0.1296	-0.2956	-0.3209	-0.0338	0.2346	0.1157	0.0024	0.3064	-0.0264	0.1799	-24.797	-1.2785	-60.0874
19	2.0531	-0.3219	-0.9972	1.6626	0.6564	1.8612	0.2581	0.3957	-0.0662	0.0845	-0.26	0.1226	0.2071	0.0455	-0.054	0.1199	0.2531	-0.0365	0.4854	-0.1189	0.2975	-39.7833	-2.8775	-61.8175
20	4.2166	-2.417	1.1925	1.3894	-0.6846	0.3342	0.1863	0.5229	0.1001	-0.3229	-0.1295	0.0844	-0.359	-0.2973	-0.0044	0.3906	0.2858	-0.0541	0.6307	0.0505	0.1709	-19.8083	-3.8841	-83.0085
21	8.3892	-1.5846	4.6968	3.1036	2.0534	5.7113	0.0954	0.9363	-0.0302	-1.0754	0.2906	-0.7034	-0.2898	0.8547	-0.2908	0.3362	0.0454	0.0665	0.2785	-0.0172	0.2282	-4.219	-15.1707	-81.5371
22	2.3706	0.6755	0.6044	2.7729	0.9297	3.1249	0.0895	-0.3201	-0.1855	0.2439	-0.0166	-0.3751	0.0959	0.4616	-0.0871	0.1637	-0.0063	-0.0279	0.2373	0.0446	0.2209	47.4664	-58.158	-0.5023
23	1.0655	-0.3345	-0.0839	0.4193	0.4648	1.0476	0.0741	-0.0061	0.0596	-0.0324	-0.0095	-0.0945	-0.2052	0.0657	-0.0285	0.2447	-0.0509	0.0127	0.1177	0.002	0.192	37.3515	-44.9313	-10.6809
24	2.8527	0.2264	0.3495	2.3051	-0.601	0.2247	0.0379	0.1204	-0.0973	-0.2151	-0.0488	-0.1406	-0.2519	0.2306	0.0186	0.2228	-0.0481	0.0339	0.1172	-0.0118	0.1698	38.8864	-48.9724	-10.3917
25	2.0378	0.0862	-0.55	1.1367	0.1887	1.9419	0.0034	-0.2899	0.0531	0.0742	0.0407	-0.0718	-0.0915	0.1605	-0.0523	0.2968	-0.0627	-0.0168	0.1035	0.025	0.1989	39.119	-46.7672	0.6651
26	2.0716	0.8	-0.1258	2.0566	-0.8856	1.1104	0.0421	-0.1014	-0.2525	0.3715	-0.11	0.3344	0.1177	-0.3062	0.0864	0.2933	-0.0634	0.0971	0.3072	-0.0057	0.3429	2.987	-64.9534	-3.4395
27	1.9376	-0.3073	-0.3317	1.8031	0.8438	1.6244	-0.0636	0.1737	0.0687	-0.1019	-0.0463	0.1338	-0.1751	-0.2852	0.1098	0.2304	0.0632	0.0115	0.2425	0.0148	0.1703	5.644	-50.7833	-14.9454
28	2.2643	0.6985	0.0179	1.3994	0.2558	1.5073	0.0382	-0.04	0.0897	-0.0025	-0.0668	0.2326	-0.1415	-0.3178	0.0392	0.2039	0.0659	0.031	0.2131	0.0094	0.2054	7.9056	-52.7012	-10.678
29	5.6263	2.9171	1.4296	4.8771	3.4865	4.0068	-0.7108	0.5782	-0.3038	0.5511	0.3363	-0.3368	0.7757	-0.8137	0.356	0.3153	0.0551	0.0303	0.3773	0.0606	0.15	15.7753	-48.1277	-4.7646
30	0.7482	-0.275	-1.28	2.1839	0.6462	4.5533	0.0281	0.3449	-0.2033	-0.0741	-0.2568	0.0177	0.6797	-0.2393	0.206	0.2839	0.0245	0.0068	0.235	-0.067	0.2377	30.5199	-78.7486	-40.1439
31	1.6265	-0.1731	-0.0639	1.0262	0.7242	1.4871	0.1111	0.1553	0.0048	-0.1455	-0.1342	0.035	-0.2601	-0.2024	0.0237	0.2193	0.0731	0.013	0.1719	-0.0037	0.1324	29.2145	-62.0169	-36.2902
32	0.428	-0.0083	-0.4438	2.1591	0.2415	1.4796	0.11	0.2762	-0.0279	-0.16	-0.2308	0.3705	-0.2894	-0.4852	0.0893	0.2388	0.1003	-0.01	0.296	-0.0453	0.1798	19.884	-57.5952	-32.024
33	1.9655	0.1466	-0.3884	1.4148	0.7193	2.9811	0.0645	0.5532	-0.2519	-0.1972	-0.076	-0.065	-0.0617	-0.0296	0.0171	0.2284	0.0895	0.0334	0.1284	0.0062	0.1729	32.2509	-66.1698	-41.9683
34	4.1031	1.9575	2.9709	8.7241	3.8518	2.9119	-0.0326	-0.3236	0.3016	0.3666	0.379	-0.8294	0.7012	0.0774	-0.3352	0.3644	0.0658	-0.0369	0.3512	-0.1435	0.1635	15.9387	-60.7209	-32.7366

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 3 through 26 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 27 through 53 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 54 through 90 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 91 through 139 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 140 through 230 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 231 through 242 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 243 through 291 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 301 through 301 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 1 through 23 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 24 through 90 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 91 through 182 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 183 through 242 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 243 through 290 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 301 through 301 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 3 through 26 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 27 through 89 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 90 through 139 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 140 through 229 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 243 through 269 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 270 through 287 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 288 through 292 )
22	X-RAY DIFFRACTION	22	chain 'F' and (resid 3 through 78 )
23	X-RAY DIFFRACTION	23	chain 'F' and (resid 79 through 199 )
24	X-RAY DIFFRACTION	24	chain 'F' and (resid 200 through 242 )
25	X-RAY DIFFRACTION	25	chain 'F' and (resid 243 through 299 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 4 through 90 )
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 91 through 182 )
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 183 through 292 )
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 301 through 301 )
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 3 through 53 )
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 54 through 182 )
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 183 through 242 )
33	X-RAY DIFFRACTION	33	chain 'E' and (resid 243 through 290 )
34	X-RAY DIFFRACTION	34	chain 'E' and (resid 301 through 301 )

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