PDB-8sws: Structure of K. lactis PNP S42E-H98R variant bound to transition ...

ID or keywords:

Entry

Database: PDB / ID: 8sws

Title

Structure of K. lactis PNP S42E-H98R variant bound to transition state analog DADMe-IMMUCILLIN G and sulfate

Components

Purine nucleoside phosphorylase

Keywords

TRANSFERASE / PENTOSYLTRANSFERASE / PURINE NUCLEOSIDE PHOSPHORYLASE

Function / homology

Function and homology information

nucleoside metabolic process / purine-nucleoside phosphorylase / purine-nucleoside phosphorylase activity / cytoplasm
Similarity search - Function

Biological species

Kluyveromyces lactis NRRL Y-1140 (yeast)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.99 Å

Authors

Fedorov, E. / Ghosh, A.

Funding support

United States, 2items

Organization	Grant number	Country
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	GM041916	United States
National Institutes of Health/National Cancer Institute (NIH/NCI)	CA013330	United States

Citation

Journal: Biochemistry / Year: 2023
Title: Phosphate Binding in PNP Alters Transition-State Analogue Affinity and Subunit Cooperativity.
Authors: Minnow, Y.V.T. / Schramm, V.L. / Almo, S.C. / Ghosh, A.

History

Deposition	May 19, 2023	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Oct 18, 2023	Provider: repository / Type: Initial release
Revision 1.1	Oct 25, 2023	Group: Database references / Category: citation / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2	Nov 22, 2023	Group: Database references / Category: citation Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3	Feb 14, 2024	Group: Refinement description / Category: pdbx_initial_refinement_model Item: _pdbx_initial_refinement_model.source_name / _pdbx_initial_refinement_model.type

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	8sws_validation.pdf.gz	5.3 MB	Display	wwPDB validaton report
Full document	8sws_full_validation.pdf.gz	5.3 MB	Display
Data in XML	8sws_validation.xml.gz	62.6 KB	Display
Data in CIF	8sws_validation.cif.gz	86.7 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/sw/8sws ftp://data.pdbj.org/pub/pdb/validation_reports/sw/8sws	HTTPS FTP

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Related structure data

Related structure data	8swpC 8swqC 8swrC 8swtC 8swuC C: citing same article (ref.)
Similar structure data	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: Purine nucleoside phosphorylase

B: Purine nucleoside phosphorylase

C: Purine nucleoside phosphorylase

D: Purine nucleoside phosphorylase

E: Purine nucleoside phosphorylase

F: Purine nucleoside phosphorylase

hetero molecules

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

1

A: Purine nucleoside phosphorylase

B: Purine nucleoside phosphorylase

C: Purine nucleoside phosphorylase

hetero molecules

defined by author&software
Evidence: gel filtration, Superdex S200
102 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: Purine nucleoside phosphorylase

E: Purine nucleoside phosphorylase

F: Purine nucleoside phosphorylase

hetero molecules

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

Unit cell

Length a, b, c (Å)	89.883, 111.120, 97.963
Angle α, β, γ (deg.)	90.00, 108.79, 90.00
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Purine nucleoside phosphorylase Mass: 33556.227 Da / Num. of mol.: 6 / Mutation: S42E, H98R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Kluyveromyces lactis NRRL Y-1140 (yeast) Gene: KLLA0_C16621g / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): pRIL / References: UniProt: Q6CSZ6
#2: Chemical	ChemComp-IM5 / 2-amino-7-{[(3R,4R)-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-yl]methyl}-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one / DADMe-ImmG Mass: 279.295 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₂H₁₇N₅O₃ / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: SO₄ / Feature type: SUBJECT OF INVESTIGATION
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 313 / 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: 1

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Sample preparation

Crystal	Density Matthews: 2.3 Å³/Da / Density % sol: 46.53 %
Crystal grow	Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 25% (w/v) PEG 3,350, 0.2 M Lithium sulphate and 0.1 M BIS-TRIS

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

NSLS

/ Beamline: X29A / Wavelength: 1.075 Å

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 31, 2013 / Details: M

Radiation

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

Radiation wavelength

Wavelength: 1.075 Å / Relative weight: 1

Reflection

Resolution: 1.99→50 Å / Num. obs: 124549 / % possible obs: 100 % / Redundancy: 3.8 % / R_merge(I) obs: 0.128 / Χ²: 1.179 / Net I/σ(I): 10.1 / Num. measured all: 467792

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique obs	Χ²	Diffraction-ID	% possible all
1.99-2.02	3.7	0.984	6179	1.303	1	99.9
2.02-2.06	3.7	0.801	6173	1.322	1	99.9
2.06-2.1	3.7	0.725	6253	1.369	1	100
2.1-2.14	3.7	0.619	6200	1.321	1	100
2.14-2.19	3.7	0.515	6188	1.278	1	100
2.19-2.24	3.7	0.454	6228	1.277	1	100
2.24-2.3	3.8	0.387	6189	1.301	1	100
2.3-2.36	3.8	0.356	6236	1.264	1	100
2.36-2.43	3.8	0.296	6233	1.199	1	100
2.43-2.51	3.8	0.252	6213	1.186	1	100
2.51-2.6	3.8	0.224	6210	1.185	1	100
2.6-2.7	3.8	0.183	6186	1.129	1	100
2.7-2.82	3.8	0.156	6243	1.143	1	100
2.82-2.97	3.8	0.136	6225	1.096	1	100
2.97-3.16	3.8	0.117	6242	1.083	1	100
3.16-3.4	3.8	0.108	6222	1.058	1	100
3.4-3.74	3.8	0.101	6258	1.048	1	100
3.74-4.29	3.7	0.092	6268	1	1	100
4.29-5.4	3.7	0.087	6255	0.967	1	100
5.4-50	3.8	0.089	6348	1.057	1	99.4

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Processing

Software

Name	Version	Classification
PHENIX	(1.20.1_4487: ???)	refinement
HKL-3000		data scaling
CBASS		data collection
HKL-3000		data reduction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.99→47.68 Å / SU ML: 0.26 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.97 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2271	6248	5.02 %
R_work	0.1943	-	-
obs	0.196	124374	99.74 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 1.99→47.68 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12974	0	130	313	13417

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.018
X-RAY DIFFRACTION	f_angle_d	1.501
X-RAY DIFFRACTION	f_dihedral_angle_d	7.291	1895
X-RAY DIFFRACTION	f_chiral_restr	0.08	2073
X-RAY DIFFRACTION	f_plane_restr	0.013	2336

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 (%)
1.99-2.01	0.3856	209	0.3328	3797	X-RAY DIFFRACTION	97
2.01-2.04	0.3682	237	0.3057	3902	X-RAY DIFFRACTION	100
2.04-2.06	0.2772	186	0.2772	3901	X-RAY DIFFRACTION	100
2.06-2.09	0.333	226	0.2846	3922	X-RAY DIFFRACTION	100
2.09-2.11	0.3192	227	0.2767	3891	X-RAY DIFFRACTION	100
2.11-2.14	0.3252	223	0.2553	3935	X-RAY DIFFRACTION	100
2.14-2.17	0.279	209	0.253	3916	X-RAY DIFFRACTION	100
2.17-2.21	0.2898	191	0.2417	3911	X-RAY DIFFRACTION	100
2.21-2.24	0.319	208	0.2377	3978	X-RAY DIFFRACTION	100
2.24-2.28	0.2518	203	0.2296	3942	X-RAY DIFFRACTION	100
2.28-2.32	0.261	207	0.2212	3905	X-RAY DIFFRACTION	100
2.32-2.36	0.2719	214	0.2214	3938	X-RAY DIFFRACTION	100
2.36-2.4	0.2766	172	0.2252	3937	X-RAY DIFFRACTION	100
2.41-2.45	0.2421	202	0.2168	3951	X-RAY DIFFRACTION	100
2.45-2.51	0.2266	200	0.2048	3958	X-RAY DIFFRACTION	100
2.51-2.57	0.243	200	0.2134	3919	X-RAY DIFFRACTION	100
2.57-2.63	0.2387	235	0.2091	3892	X-RAY DIFFRACTION	100
2.63-2.7	0.2551	222	0.2015	3952	X-RAY DIFFRACTION	100
2.7-2.78	0.2637	211	0.2035	3965	X-RAY DIFFRACTION	100
2.78-2.87	0.2379	197	0.2002	3917	X-RAY DIFFRACTION	100
2.87-2.97	0.2583	227	0.2033	3943	X-RAY DIFFRACTION	100
2.97-3.09	0.2405	204	0.2069	3944	X-RAY DIFFRACTION	100
3.09-3.23	0.2258	202	0.202	3966	X-RAY DIFFRACTION	100
3.23-3.4	0.2294	196	0.1883	3953	X-RAY DIFFRACTION	100
3.4-3.62	0.2131	227	0.1879	3948	X-RAY DIFFRACTION	100
3.62-3.9	0.2131	191	0.1692	3994	X-RAY DIFFRACTION	100
3.9-4.29	0.1775	205	0.1485	3978	X-RAY DIFFRACTION	100
4.29-4.91	0.168	210	0.1429	3954	X-RAY DIFFRACTION	100
4.91-6.18	0.1898	211	0.1759	3988	X-RAY DIFFRACTION	100
6.18-47.68	0.1726	196	0.1675	4029	X-RAY DIFFRACTION	99

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	4.3307	-0.023	-0.8161	2.5132	0.6754	2.3041	0.1754	0.6272	-0.6959	-0.4615	-0.2918	0.1156	0.243	0.0519	0.0255	0.4396	0.1424	-0.0873	0.4926	-0.1272	0.407	120.4687	-14.4126	34.1701
2	6.2011	0.5004	-0.4142	2.9065	0.9412	3.3684	0.4683	1.2974	-0.0478	-0.8167	-0.2462	-0.0885	-0.278	0.3372	0.0052	0.5401	0.1594	0.0387	0.5685	-0.0117	0.3269	122.2817	-8.5058	31.8911
3	1.5866	0.2257	0.288	1.5279	-0.1	0.9934	0.0781	0.3236	-0.229	-0.216	-0.0346	0.0895	0.1651	0.3998	-0.0397	0.297	0.0399	-0.0112	0.3565	-0.0185	0.3198	115.1243	-3.5764	37.4645
4	1.3773	-0.1642	0.2722	0.708	-0.0876	1.4439	0.0172	0.0911	0.0811	-0.0035	-0.0406	-0.1303	-0.1464	0.5314	0.0195	0.1782	-0.0482	0.0081	0.3753	0.0092	0.2356	120.3375	9.0683	43.2104
5	3.915	-0.0621	-0.2628	2.7663	0.7123	3.8807	0.1099	-0.1021	-0.6415	-0.1298	-0.0966	0.2871	0.4176	-0.4629	-0.0007	0.2897	-0.0276	-0.0704	0.3651	0.0354	0.5012	72.8693	-0.2475	50.5911
6	3.8326	-1.388	-0.1075	1.0915	0.0017	0.2953	0.2295	0.3814	-0.2676	-0.1823	-0.183	0.2034	-0.2074	-0.2876	-0.0065	0.2075	0.0327	-0.0141	0.2956	0.0361	0.3651	83.6084	5.6529	47.2564
7	3.9219	-0.4367	-0.7574	1.3312	-0.1864	2.3795	0.0642	0.0884	0.3891	-0.0202	0.0087	0.0364	-0.3377	-0.409	0.0117	0.2517	-0.0064	0.0235	0.1705	-0.0171	0.3316	89.671	16.54	57.5183
8	2.496	-0.0464	0.0939	0.605	-0.0843	1.7869	0.0901	-0.1983	0.0451	0.058	-0.0155	0.0023	-0.0508	0.0691	-0.0702	0.2004	-0.0287	0.02	0.1608	-0.0025	0.224	96.6443	8.6528	59.2199
9	4.3318	-1.5291	0.3103	4.0731	0.8004	3.7623	0.0782	0.5246	-0.1097	-0.4937	-0.0819	0.2787	-0.2262	0.231	-0.0318	0.3962	0.0751	-0.0738	0.5568	-0.0091	0.3407	101.649	17.0249	6.858
10	2.7852	0.0311	-0.1166	1.7375	1.2058	2.8866	0.2347	0.6021	0.1732	-0.7157	-0.0596	0.2289	-1.0521	-0.1285	-0.0466	0.7593	0.0907	-0.0419	0.4813	0.1395	0.4987	96.6288	31.5344	11.2749
11	2.087	-1.6959	-0.1287	3.2805	0.4049	2.8188	0.1227	0.2328	-0.0082	-0.3899	-0.2426	-0.0008	-0.4733	-0.0109	0.0016	0.4853	-0.0006	-0.0263	0.4831	0.1477	0.3097	103.613	25.4826	14.9376
12	1.2003	-0.3562	-0.1619	0.3222	0.6513	1.9167	0.0624	0.1279	0.3506	-0.3491	0.0025	-0.0518	-0.7494	0.3332	0.0164	0.5157	-0.1286	0.0002	0.3452	0.1059	0.3737	106.9227	29.9957	30.5016
13	2.6941	-2.0713	-3.2068	3.6102	2.1578	3.9151	-0.0088	-0.2218	0.2087	-0.2759	-0.158	0.4309	-0.4202	-0.5688	0.2099	0.3456	-0.0179	-0.0234	0.1929	0.0707	0.4187	96.9306	23.9999	45.2396
14	1.1136	-0.6161	-0.1233	1.1828	1.044	3.6579	-0.0204	0.0766	0.2906	-0.3509	0.0413	0.1368	-0.7162	0.5773	-0.0077	0.3803	-0.1057	-0.0323	0.3581	0.1347	0.3946	105.9374	24.6414	28.6331
15	0.7571	0.3829	-1.3387	0.8243	-0.9125	4.0499	-0.1745	-0.0209	0.0517	0.0899	-0.2162	0.1825	-0.8729	0.0304	0.196	0.5715	-0.0048	-0.0106	0.3076	0.0784	0.5889	95.7272	31.9519	43.7136
16	1.5645	1.4665	-0.5511	3.6981	-0.9931	5.4633	-0.4803	0.2585	0.5543	-0.3153	-0.3925	0.1009	-0.6295	-0.0138	0.3099	1.4364	-0.1251	-0.1972	0.416	0.182	0.5216	100.0035	42.8698	22.0765
17	1.3899	0.3522	-0.9674	2.0341	-0.6795	2.6193	-0.135	0.1558	-0.5871	-0.0885	-0.0356	-0.5362	0.6232	0.5008	0.1479	0.5416	0.1839	-0.0226	0.5206	-0.0445	0.5305	92.7953	2.0909	-1.6846
18	2.5365	0.3498	0.3828	0.5297	-0.2061	0.9079	0.0599	-0.0834	-0.4021	-0.0228	-0.0637	-0.2093	0.176	0.159	-0.0544	0.3844	0.0663	-0.0315	0.3972	-0.0264	0.3522	82.5974	6.9013	1.016
19	4.651	1.2571	-1.4743	2.6056	-0.3123	2.6679	0.0145	0.1503	0.3148	-0.1003	0.0068	-0.0441	-0.1509	0.3928	0.0563	0.3047	0.064	0.0059	0.2976	-0.0086	0.2638	75.2344	17.5585	-8.5887
20	2.0207	0.328	0.3109	0.9923	-0.0678	1.5987	0.0392	0.3449	-0.1362	-0.1317	0.0153	-0.0513	0.2454	0.1394	-0.0491	0.3469	0.0554	-0.0033	0.3044	-0.0425	0.2223	69.3246	8.9391	-10.811
21	6.1189	1.0238	-1.6852	2.0852	-1.91	3.361	0.0524	-0.7931	-1.6099	-0.05	-0.3397	-0.8302	0.545	0.5841	0.2285	0.9502	0.0623	-0.0145	0.6134	0.2711	0.8541	59.8287	-20.4208	12.5323
22	3.4299	0.5681	-0.9008	1.8539	-0.7816	1.4674	0.1129	-0.6243	-1.2218	0.0702	0.0052	0.2104	1.1469	-0.7927	-0.0383	1.0733	-0.3662	-0.0348	0.6304	0.1902	0.8383	40.5022	-18.0497	10.5933
23	5.5879	-0.5375	-0.6704	1.6117	-1.9177	2.5853	0.0053	-1.3783	-0.6903	0.5041	-0.1389	-0.1475	0.2178	-0.2276	0.0222	0.959	-0.266	0.0798	0.6177	0.2246	0.5073	48.4669	-16.3615	17.0931
24	1.2724	-0.3069	-0.0461	1.2473	0.3052	1.0465	-0.0306	-0.2125	-0.4547	0.1109	0.0628	0.0301	0.7846	-0.3027	-0.0004	0.6601	-0.0861	-0.0086	0.3094	0.0445	0.422	50.1182	-8.6862	9.5935
25	1.5232	-0.0527	-0.1816	1.0514	0.2138	1.7856	-0.0497	0.1097	-0.1389	-0.1471	0.0051	0.108	0.3724	-0.3552	0.0352	0.3529	-0.0674	-0.0228	0.289	-0.0055	0.2315	49.1976	3.2425	2.1108
26	1.6792	0.7264	0.0706	1.1284	0.2168	2.0773	-0.1075	-0.0602	0.3039	-0.1112	-0.0415	0.3935	-0.2576	-0.5328	0.1216	0.2428	0.0417	-0.0703	0.4706	-0.0279	0.293	41.9917	19.3125	11.9517
27	2.0219	0.5945	0.9862	2.2914	1.0035	2.4263	0.0557	-0.2604	-0.3864	-0.0527	-0.131	0.1021	0.6818	-0.8517	0.1044	0.5024	-0.2469	-0.0137	0.7008	0.0434	0.4505	34.6565	-2.4857	9.1776
28	2.4405	0.5107	1.2283	4.5387	-0.8597	1.9376	0.0186	-0.4812	-0.1431	0.4253	0.0681	-0.4189	-0.0168	-0.18	-0.0342	0.2748	0.0418	-0.055	0.4375	-0.0261	0.3199	62.7486	19.3736	40.2889
29	2.9293	0.2716	1.2356	3.9917	-0.91	1.8176	-0.0584	-0.076	0.0898	0.4148	-0.0731	-0.623	-0.1943	0.1483	0.0398	0.2603	0.0201	-0.0497	0.3667	-0.0169	0.2978	65.7981	25.1499	36.4441
30	0.4985	0.1013	0.3287	1.5498	0.3228	1.2728	0.0015	-0.1624	0.0961	-0.1295	0.0374	0.0425	-0.1674	-0.2421	-0.042	0.2024	0.0382	0.0089	0.2644	-0.031	0.2547	56.1289	26.7082	19.9157
31	2.0597	0.9788	-2.2828	4.3579	-1.6397	2.6086	-0.0077	-0.1064	0.125	-0.2455	0.015	-0.5938	0.1663	0.5233	0.0662	0.3527	0.0591	0.0152	0.2673	-0.0745	0.3316	66.9263	23.2983	4.1897
32	0.3943	-0.7022	0.1768	0.2469	0.3045	1.9849	-0.009	-0.0377	0.237	-0.135	0.0782	-0.0793	-0.3131	0.0002	-0.075	0.2948	0.0045	0.006	0.2532	-0.0359	0.3217	62.5766	30.5178	17.2597

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 5 through 64 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 65 through 94 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 95 through 132 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 133 through 306 )
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 8 through 94 )
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 95 through 132 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 133 through 193 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 194 through 306 )
9	X-RAY DIFFRACTION	9	chain 'C' and (resid 5 through 27 )
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 28 through 85 )
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 86 through 122 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 123 through 207 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 208 through 224 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 225 through 246 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 247 through 288 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 289 through 306 )
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 4 through 94 )
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 95 through 132 )
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 133 through 193 )
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 194 through 306 )
21	X-RAY DIFFRACTION	21	chain 'E' and (resid 5 through 25 )
22	X-RAY DIFFRACTION	22	chain 'E' and (resid 26 through 57 )
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 58 through 84 )
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 85 through 132 )
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 133 through 246 )
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 247 through 280 )
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 281 through 306 )
28	X-RAY DIFFRACTION	28	chain 'F' and (resid 5 through 44 )
29	X-RAY DIFFRACTION	29	chain 'F' and (resid 45 through 118 )
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 119 through 207 )
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 208 through 224 )
32	X-RAY DIFFRACTION	32	chain 'F' and (resid 225 through 306 )

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