PDB-4l5a: Methylthioadenosine phosphorylase from Schistosoma mansoni in com...

ID or keywords:

Entry

Database: PDB / ID: 4l5a

Title

Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with tubercidin

Components

S-methyl-5'-thioadenosine phosphorylase

Keywords

TRANSFERASE/ANTIBIOTIC / Transferase / phosphorylase / Nucleoside phosphorylase / Enzyme / TRANSFERASE-ANTIBIOTIC complex

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 /

molecular replacement / Resolution: 2.2993 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 10, 2013	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jun 11, 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	4l5a.cif.gz	663.1 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	4l5a_validation.pdf.gz	2.2 MB	Display	wwPDB validaton report
Full document	4l5a_full_validation.pdf.gz	2.2 MB	Display
Data in XML	4l5a_validation.xml.gz	64.1 KB	Display
Data in CIF	4l5a_validation.cif.gz	87.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/l5/4l5a ftp://data.pdbj.org/pub/pdb/validation_reports/l5/4l5a	HTTPS FTP

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Related structure data

Related structure data	4l5cC 4l5yC 4l6iC 5f73C 5f76C 5f77C 5f78C 5f7jC 5f7oC 5f7xC 5f7zC 5fakC C: citing same article (ref.)
Similar structure data	4l5y-1 5fak-2 4l6i-1 4l5y-2 3e9z-d 4l6i-2 4l5c-1 5f7x-d 5fak-1 5f7j-2 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

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

214 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
107 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
107 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	81.068, 82.680, 150.558
Angle α, β, γ (deg.)	90.000, 101.340, 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-TBN / '2-(4-AMINO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL / 7-DEAZAADENOSINE Mass: 266.253 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₁₁H₁₄N₄O₄
#3: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO₄
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 561 / 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: 47.4 %
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:

Diamond

/ Beamline: I02 / Wavelength: 0.9686 Å

Detector

Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 7, 2011 / Details: DCM

Radiation

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

Radiation wavelength

Wavelength: 0.9686 Å / Relative weight: 1

Reflection

Resolution: 2.299→30 Å / Num. all: 170562 / Num. obs: 158912 / % possible obs: 93.2 % / Observed criterion σ(F): 3 / Observed criterion σ(I): -3 / B_iso Wilson estimate: 36.749 Å² / R_merge(I) obs: 0.048 / Net I/σ(I): 13.02

Reflection shell

Resolution (Å)	R_merge(I) obs	Mean I/σ(I) obs	Num. measured obs	Num. unique obs	Diffraction-ID	% possible all
2.299-2.44	0.236	3.53	48737	25362	1	92.5
2.44-2.6	0.162	5.05	49646	25324	1	98
2.6-2.81	0.108	7.48	45465	23262	1	96.8
2.81-3.08	0.068	10.89	42452	21681	1	98.1
3.08-3.44	0.045	15.57	37757	19355	1	96.5
3.44-3.96	0.042	19.66	22164	11855	1	67.2
3.96-4.83	0.025	27.2	27949	14409	1	95.9
4.83-6.73	0.025	27.35	21582	11168	1	95.8
6.73-30	0.017	32.35	12861	6496	1	95.6

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
XSCALE		data scaling
PHASER		phasing
PHENIX	1.8.2_1309	refinement
PDB_EXTRACT	3.11	data extraction
GDA		data collection
XDS		data reduction
XDS		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.2993→29.2 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.8484 / SU ML: 0.24 / σ(F): 1.07 / Phase error: 22.58 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2192	7938	5 %	Random
R_work	0.1889	-	-	-
all	0.1904	170562	-	-
obs	0.1904	158778	93.18 %	-

Solvent computation

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

Displacement parameters

B_iso max: 153.31 Å² / B_iso mean: 37.8519 Å² / B_iso min: 15.56 Å²

Refinement step

Cycle: LAST / Resolution: 2.2993→29.2 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12861	0	144	561	13566

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.003	13266
X-RAY DIFFRACTION	f_angle_d	0.791	18007
X-RAY DIFFRACTION	f_chiral_restr	0.048	2086
X-RAY DIFFRACTION	f_plane_restr	0.003	2286
X-RAY DIFFRACTION	f_dihedral_angle_d	12.123	4739

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 (%)
2.2993-2.3254	0.2676	205	0.2553	3883	4088	72
2.3254-2.3528	0.2866	274	0.2303	5292	5566	98
2.3528-2.3815	0.2596	275	0.2072	5247	5522	98
2.3815-2.4116	0.2398	282	0.2125	5319	5601	98
2.4116-2.4433	0.2815	278	0.2171	5291	5569	98
2.4433-2.4768	0.2605	276	0.2097	5237	5513	98
2.4768-2.5121	0.2312	284	0.2008	5346	5630	98
2.5121-2.5496	0.2793	276	0.203	5231	5507	98
2.5496-2.5894	0.2209	281	0.2014	5321	5602	98
2.5894-2.6318	0.2449	281	0.2074	5321	5602	98
2.6318-2.6772	0.2751	265	0.2136	5045	5310	94
2.6772-2.7258	0.246	277	0.2048	5171	5448	97
2.7258-2.7782	0.2673	276	0.1964	5291	5567	98
2.7782-2.8349	0.2603	278	0.1983	5368	5646	98
2.8349-2.8965	0.2419	282	0.2013	5310	5592	98
2.8965-2.9638	0.232	277	0.2045	5280	5557	98
2.9638-3.0378	0.2659	276	0.2029	5258	5534	98
3.0378-3.1199	0.233	281	0.2094	5330	5611	98
3.1199-3.2116	0.2475	282	0.2072	5286	5568	98
3.2116-3.3151	0.2322	278	0.2003	5261	5539	98
3.3151-3.4334	0.2228	263	0.2053	5066	5329	93
3.4334-3.5706	0.2228	253	0.2128	4768	5021	89
3.5706-3.7328	0.2696	134	0.2686	2521	2655	46
3.7328-3.9292	0.21	183	0.2077	3603	3786	67
3.9292-4.1747	0.2037	259	0.1597	4779	5038	89
4.1747-4.496	0.1385	279	0.1365	5258	5537	97
4.496-4.9465	0.1626	271	0.132	5196	5467	97
4.9465-5.6577	0.176	269	0.1617	5105	5374	95
5.6577-7.1111	0.2045	275	0.1692	5258	5533	97
7.1111-29.2026	0.1573	268	0.1497	5198	5466	96

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	1.6677	0.7455	-1.3435	1.4673	-0.4595	2.6588	0.1603	-0.0693	-0.0075	-0.4374	-0.1159	-0.2932	0.1504	0.2609	0.0919	0.3331	0.0723	0.1439	0.2313	0.001	0.5777	40.8645	-24.3125	1.3376
2	1.8525	-0.2282	-0.2764	2.1451	1.1579	0.6389	0.0636	-0.0851	-0.3343	-0.1665	-0.1538	-0.3395	0.0958	0.1363	0.0967	0.2454	-0.002	0.0588	0.1954	0.0323	0.3663	32.6036	-21.1578	6.0619
3	2.7089	-0.1926	-0.3538	1.4503	-0.1037	1.8527	0.053	-0.3055	-0.0843	0.0745	-0.073	-0.1876	-0.2397	0.1776	0.0511	0.2086	-0.0359	-0.0195	0.1958	-0.0235	0.1973	34.7246	-9.1073	14.9958
4	2.6442	0.0296	-0.1118	0.1689	0.2859	1.2375	0.1043	0.0299	0.0134	-0.0144	-0.0409	0.006	-0.2587	0.0152	-0.0308	0.2702	-0.0433	0.0317	0.1851	-0.024	0.2788	25.739	-7.7112	10.7258
5	1.6878	0.613	-0.5434	2.3748	-0.6885	3.001	-0.1723	0.0014	-0.3576	-0.202	0.071	-0.2763	-0.0608	0.2541	0.0714	0.2534	0.0092	0.0369	0.2915	-0.0464	0.4018	41.2126	-15.6194	11.1513
6	1.5218	2.3285	-1.0113	3.7755	-1.0094	2.1879	0.1822	-0.7246	-0.812	0.3717	-0.1526	-0.4336	0.1421	0.0837	-0.0069	0.3426	-0.087	-0.0437	0.3991	0.1321	0.3232	12.0542	-34.8382	42.9224
7	1.1442	0.64	-0.6255	1.5703	-0.18	1.7158	0.0104	-0.2724	-0.4199	0.0235	-0.1381	-0.0679	0.3998	0.1084	0.1034	0.2682	-0.0376	-0.0102	0.2323	0.0759	0.3123	10.0567	-34.3091	34.5385
8	1.966	0.1924	0.2821	1.1578	-0.5326	2.3611	0.1659	-0.3189	0.099	0.2188	-0.1657	-0.1496	-0.3759	0.1096	0.0021	0.2328	-0.0811	-0.0119	0.2012	0.0095	0.1902	10.9445	-16.4882	37.7676
9	3.2339	-2.9839	-2.0172	2.8396	1.4553	3.2431	-0.129	0.0976	0.2358	0.2985	0.086	-0.1802	-0.1671	0.4724	0.0731	0.2621	-0.1338	0.0063	0.2707	0.0281	0.2766	24.7539	-11.7494	26.3166
10	1.8003	0.0005	0.0978	1.2428	-0.1027	2.3057	0.1522	-0.3655	-0.1073	0.1952	-0.1318	-0.1025	-0.0233	0.1908	-0.0306	0.2781	-0.0808	0.009	0.243	0.0338	0.178	10.4554	-22.0845	38.872
11	1.9079	-0.0097	3.0666	1.4274	0.4634	5.1035	0.1679	-0.0815	-0.1596	-0.0682	0.0133	0.4046	-0.0561	-0.8765	-0.1116	0.2071	0.0531	0.0175	0.3373	-0.0005	0.306	-11.9476	-11.7536	0.2607
12	2.3938	1.4453	-1.527	3.3029	0.543	1.8922	-0.266	0.6041	-0.2641	-0.6931	0.2159	0.4469	0.1283	-0.4726	0.0034	0.3267	-0.0467	-0.0481	0.4152	-0.0876	0.3779	-4.5887	-23.9896	-2.2507
13	0.9767	0.469	-0.0419	1.5754	-0.085	2.5156	0.0229	0.1745	-0.0305	-0.2109	0.0254	0.0912	0.0969	-0.1194	-0.0778	0.2055	0.0283	0.0061	0.158	-0.012	0.2056	-4.7414	-14.6128	1.9611
14	2.6761	-0.9184	-0.5637	2.0491	-1.0258	1.4026	0.2704	-0.0424	0.1685	0.0851	-0.1108	-0.1977	-0.525	-0.1146	-0.1976	0.2566	0.0338	0.0123	0.1089	-0.0061	0.194	1.4501	-0.4658	16.1587
15	2.9135	-1.1166	-0.3877	1.5651	0.1688	2.8707	0.0452	0.0561	-0.2472	-0.3992	0.0868	-0.6413	0.2039	0.1276	-0.0931	0.2737	0.021	0.0682	0.1517	-0.0403	0.3463	12.6495	-15.25	1.5454
16	1.6728	-0.7615	-0.1807	1.5861	-0.2992	1.1488	0.0639	-0.0081	0.3676	-0.0078	0.1163	0.0864	-0.7414	-0.1339	-0.1935	0.493	0.0653	0.0446	0.2195	0.0201	0.2781	-3.5983	6.6947	9.8079
17	3.809	2.4975	-0.4531	3.831	-2.1658	1.6509	0.2808	-0.3839	-0.1331	0.3321	-0.3932	-0.0395	-0.2581	-0.0776	0.031	0.2825	0.0043	-0.0041	0.1689	0.0019	0.1813	6.6913	-8.6549	25.4965
18	1.1584	0.3724	-0.3615	0.5743	-0.2911	0.2796	0.0094	-0.0738	-0.1513	0.1126	-0.0884	0.0644	-0.2443	-0.0403	0.0199	0.3558	0.0579	0.015	0.2137	0.0144	0.2568	1.4848	-6.6353	12.3008
19	1.7673	0.5101	-1.6588	1.1679	-0.3446	5.3203	0.1134	-0.0107	0.2361	0.3192	0.0712	0.2494	-0.429	-0.3267	-0.1196	0.4143	0.1651	0.0617	0.282	0.0241	0.3404	-14.4827	-3.299	10.6355
20	2.9843	-1.8385	1.6157	2.0705	-1.1311	0.9056	0.1379	0.4735	-0.2792	-0.5999	0.0009	-0.2802	-0.0162	0.0876	-0.0564	0.5609	-0.0066	0.0958	0.3297	-0.0552	0.2848	9.8077	-5.7703	-10.0865
21	4.3175	1.4488	1.97	1.769	0.7156	1.5033	0.2824	-0.2444	-0.1204	0.24	-0.0993	-0.1801	0.0725	0.0343	0.0076	0.1273	-0.1196	-0.1103	0.7094	0.1696	0.2278	76.0854	30.4358	70.5586
22	1.4775	0.3919	0.565	0.9654	0.227	0.2254	-0.1811	-0.3711	-0.1549	0.3713	0.142	-0.3355	-0.0907	0.0562	0.3551	0.1116	0.0901	-0.1949	0.794	0.3269	0.4183	72.9381	18.6647	74.5584
23	0.481	-0.2511	0.5809	0.6392	-0.3858	0.7511	0.042	-0.5132	-0.3471	0.2391	-0.2634	-0.3256	0.0558	0.6013	-0.1957	0.2076	-0.086	-0.088	0.6454	0.1609	0.3149	70.1637	26.6068	69.8694
24	3.6711	0.6687	-1.9262	2.9378	-0.9231	2.7146	0.094	0.1458	0.2795	-0.2902	-0.0294	-0.0987	-0.2729	0.4336	-0.195	0.2058	-0.0745	-0.0048	0.2723	0.0086	0.1551	63.3765	40.3448	56.0105
25	3.2042	0.3453	-0.7447	1.8901	0.5961	1.8826	0.0696	-0.3353	-0.3324	0.3884	-0.1047	0.4732	0.0033	0.3348	0.0628	0.2168	-0.0396	-0.013	0.2668	0.0743	0.2366	53.3143	25.4738	70.6365
26	0.4971	0.3947	-0.0178	0.5709	-0.0969	0.0416	0.2649	-0.0731	0.1685	0.2426	-0.1811	0.0133	-0.4544	0.3593	0.286	0.2485	-0.469	-0.1141	0.4597	-0.0266	0.2299	68.2559	47.8544	62.104
27	4.521	-5.5005	1.3025	8.5724	-0.2865	1.4346	0.0594	0.2238	0.1309	-0.3618	-0.2798	-0.1409	-0.2912	0.2389	0.1968	0.2019	-0.0677	-0.0168	0.2733	0.0445	0.2287	58.5724	31.5313	46.604
28	0.8293	-0.0501	-0.2898	1.1942	-0.025	0.1382	0.1476	-0.3266	0.0189	-0.0799	-0.2655	-0.3266	-0.2911	0.4219	0.0654	0.2673	-0.122	-0.0201	0.4874	0.0951	0.2425	70.2059	36.1688	60.3094
29	7.0285	3.7944	0.7932	5.6317	1.2783	0.4245	0.0012	-0.4915	0.0858	0.6112	-0.218	-0.0994	-0.3172	0.6018	0.0786	0.3921	-0.1069	-0.0467	0.4993	0.0253	0.1735	55.8889	34.771	82.3304
30	3.6657	0.6575	-0.3912	3.2639	-1.0769	1.3069	0.1306	-0.2171	-0.1733	0.5623	-0.1754	0.5149	0.0389	-0.1944	0.0899	0.2838	-0.033	0.1278	0.2095	-0.0119	0.3511	27.9532	14.5445	72.979
31	1.5345	-0.1556	-0.2665	1.4681	-0.0367	1.7404	0.006	0.0731	-0.1847	-0.0095	-0.0744	0.3134	0.0441	-0.1919	0.0576	0.1167	-0.0097	-0.0021	0.1449	-0.0265	0.2626	30.3061	25.3357	62.0722
32	2.1824	-0.2578	-0.356	0.9665	-0.2599	1.7222	0.0043	0.0223	-0.0782	0.0551	-0.0301	0.2424	-0.0357	-0.1522	0.0411	0.1365	0.0123	-0.0209	0.1487	-0.0161	0.2364	31.9327	27.2097	61.5779
33	0.7919	-1.1416	-1.1202	2.1666	1.2577	2.7184	-0.2391	0.3599	-0.8156	-0.0427	-0.3478	0.2225	0.6425	-0.2285	0.5621	0.4015	0.099	0.0062	0.394	-0.0994	0.3557	53.3206	5.3333	29.2834
34	1.1636	-0.6326	-1.2369	0.791	0.2039	1.6353	-0.2164	0.0791	-0.4586	-0.2149	-0.2015	0.0567	0.5907	0.0991	0.402	0.3596	0.1096	0.049	0.2517	-0.0027	0.3314	55.3443	6.1238	37.6947
35	1.9172	0.1663	-0.4317	1.4285	0.8335	2.4399	0.0304	0.0988	-0.0253	-0.1687	-0.1784	-0.0048	-0.1429	0.008	0.1361	0.216	0.0577	0.0225	0.1477	0.0188	0.1938	53.5913	23.8634	34.7261
36	0.5954	-0.4339	-0.8998	1.6291	0.7252	2.5366	0.0454	0.2758	-0.1059	-0.2305	-0.2122	0.2341	0.0336	-0.2707	0.1179	0.1809	0.0556	-0.0398	0.2345	-0.0447	0.1995	46.0877	20.4796	35.8528
37	2.046	0.3225	2.6257	2.0383	1.4233	3.9482	-0.2195	0.1123	-0.0922	-0.0565	-0.3012	-0.216	0.6207	1.1551	0.1657	0.3214	0.0664	0.09	0.5385	0.1082	0.461	73.0049	18.1806	37.0795

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 3 through 53 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 54 through 91 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 92 through 182 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 183 through 242 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 243 through 291 )
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 3 through 23 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 24 through 91 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 92 through 182 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 183 through 199 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 200 through 290 )
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 3 through 23 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 24 through 38 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 39 through 91 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 92 through 110 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 111 through 139 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 140 through 182 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 183 through 199 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 200 through 242 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 243 through 269 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 270 through 292 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 3 through 20 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 21 through 39 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 40 through 91 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 92 through 110 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 111 through 139 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 140 through 182 )
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 183 through 198 )
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 199 through 270 )
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 271 through 291 )
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 3 through 38 )
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 39 through 182 )
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 183 through 291 )
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 3 through 23 )
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 24 through 91 )
35	X-RAY DIFFRACTION	35	chain 'F' and (resid 92 through 182 )
36	X-RAY DIFFRACTION	36	chain 'F' and (resid 183 through 269 )
37	X-RAY DIFFRACTION	37	chain 'F' and (resid 270 through 292 )

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