PDB-8swq: Structure of K. lactis PNP bound to transition state analog DADMe...

ID or keywords:

Entry

Database: PDB / ID: 8swq

Title

Structure of K. lactis PNP bound to transition state analog DADMe-IMMUCILLIN H 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: 1.979 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 15, 2023	Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.3	Nov 22, 2023	Group: Database references / Category: citation Item: _citation.journal_volume / _citation.page_first / _citation.page_last

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	8swq_validation.pdf.gz	3.6 MB	Display	wwPDB validaton report
Full document	8swq_full_validation.pdf.gz	3.6 MB	Display
Data in XML	8swq_validation.xml.gz	66.4 KB	Display
Data in CIF	8swq_validation.cif.gz	93.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/sw/8swq ftp://data.pdbj.org/pub/pdb/validation_reports/sw/8swq	HTTPS FTP

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Related structure data

Related structure data	8swpC 8swrC 8swsC 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

204 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)	89.963, 110.788, 98.043
Angle α, β, γ (deg.)	90.00, 108.95, 90.00
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Purine nucleoside phosphorylase Mass: 33729.617 Da / Num. of mol.: 6 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-DIH / 7-[[(3R,4R)-3-(hydroxymethyl)-4-oxidanyl-pyrrolidin-1-ium-1-yl]methyl]-3,5-dihydropyrrolo[3,2-d]pyrimidin-4-one Mass: 265.288 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₂H₁₇N₄O₃ / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO₄ / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₃H₈O₃
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 695 / 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: 46.51 %
Crystal grow	Temperature: 292 K / Method: vapor diffusion, sitting drop Details: 25% (w/v) PEG 3,350, 0.2 M Ammonium sulphate and 0.11 M BIS-TRIS PH range: 5.5

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 31-ID / Wavelength: 0.98 Å

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 2, 2013

Radiation

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

Radiation wavelength

Wavelength: 0.98 Å / Relative weight: 1

Reflection

Resolution: 1.979→30 Å / Num. obs: 126431 / % possible obs: 99.8 % / Redundancy: 3.9 % / R_merge(I) obs: 0.119 / Χ²: 1.04 / Net I/σ(I): 10

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique obs	Χ²	Diffraction-ID	% possible all
1.98-2.01	3.9	0.785	12497	1.064	1	100
2.01-2.05	3.9	0.646	12472	1.068	1	100
2.05-2.09	3.9	0.569	12461	1.083	1	100
2.09-2.13	3.9	0.477	12511	1.055	1	100
2.13-2.18	3.9	0.405	12333	1.049	1	100
2.18-2.23	3.9	0.34	12499	1.047	1	100
2.23-2.29	3.9	0.296	12409	1.091	1	100
2.29-2.35	3.9	0.263	12408	1.05	1	100
2.35-2.42	3.9	0.23	12465	1.034	1	100
2.42-2.49	3.9	0.197	12521	1.036	1	100
2.49-2.58	3.9	0.176	12392	1.055	1	100
2.58-2.69	3.9	0.15	12524	1.053	1	100
2.69-2.81	3.9	0.128	12398	1.041	1	100
2.81-2.96	3.9	0.117	12463	1.047	1	100
2.96-3.14	3.9	0.109	12415	1.027	1	100
3.14-3.38	3.9	0.108	12457	1.025	1	100
3.38-3.72	3.9	0.103	12453	0.977	1	100
3.72-4.26	3.9	0.081	12483	0.999	1	100
4.26-5.36	3.9	0.067	12416	1.012	1	100
5.36-30	3.8	0.06	12062	0.997	1	96.7

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Processing

Software

Name	Version	Classification
PHENIX	1.8.2_1309	refinement
HKL-3000		data scaling
HKL-3000		data reduction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.979→26.367 Å / SU ML: 0.16 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 19.81 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.197	6316	5.01 %
R_work	0.1632	-	-
obs	0.1649	125961	99.63 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 1.979→26.367 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12734	0	130	695	13559

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	13191
X-RAY DIFFRACTION	f_angle_d	1.255	17892
X-RAY DIFFRACTION	f_dihedral_angle_d	14.612	4782
X-RAY DIFFRACTION	f_chiral_restr	0.083	2057
X-RAY DIFFRACTION	f_plane_restr	0.005	2289

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 (%)
1.9793-2.0018	0.2437	187	0.2099	3736	X-RAY DIFFRACTION	93
2.0018-2.0254	0.2591	212	0.2007	3993	X-RAY DIFFRACTION	100
2.0254-2.0501	0.2628	210	0.2002	4000	X-RAY DIFFRACTION	100
2.0501-2.076	0.2358	201	0.1971	3976	X-RAY DIFFRACTION	100
2.076-2.1033	0.2351	229	0.1922	3971	X-RAY DIFFRACTION	100
2.1033-2.1321	0.2233	201	0.1793	4045	X-RAY DIFFRACTION	100
2.1321-2.1626	0.2237	194	0.1718	3940	X-RAY DIFFRACTION	100
2.1626-2.1948	0.2164	208	0.1766	4014	X-RAY DIFFRACTION	100
2.1948-2.2291	0.2057	203	0.1661	4007	X-RAY DIFFRACTION	100
2.2291-2.2656	0.2336	187	0.1668	3981	X-RAY DIFFRACTION	100
2.2656-2.3047	0.1709	217	0.1666	4004	X-RAY DIFFRACTION	100
2.3047-2.3466	0.1949	227	0.1615	3957	X-RAY DIFFRACTION	100
2.3466-2.3917	0.2156	209	0.1639	4027	X-RAY DIFFRACTION	100
2.3917-2.4404	0.1907	197	0.1694	3971	X-RAY DIFFRACTION	100
2.4404-2.4935	0.2381	212	0.1672	4001	X-RAY DIFFRACTION	100
2.4935-2.5514	0.2193	218	0.1728	4011	X-RAY DIFFRACTION	100
2.5514-2.6152	0.2009	192	0.1647	3969	X-RAY DIFFRACTION	100
2.6152-2.6858	0.1939	211	0.1608	4033	X-RAY DIFFRACTION	100
2.6858-2.7648	0.2018	209	0.1662	3946	X-RAY DIFFRACTION	100
2.7648-2.8539	0.214	227	0.1727	4017	X-RAY DIFFRACTION	100
2.8539-2.9558	0.2275	229	0.1733	3989	X-RAY DIFFRACTION	100
2.9558-3.074	0.2193	209	0.1711	3999	X-RAY DIFFRACTION	100
3.074-3.2136	0.1925	213	0.1746	4012	X-RAY DIFFRACTION	100
3.2136-3.3827	0.1865	218	0.1715	4005	X-RAY DIFFRACTION	100
3.3827-3.5942	0.2044	208	0.1634	3994	X-RAY DIFFRACTION	100
3.5942-3.8709	0.1753	216	0.1475	4017	X-RAY DIFFRACTION	100
3.8709-4.259	0.1511	198	0.1319	4056	X-RAY DIFFRACTION	100
4.259-4.8719	0.1621	240	0.1252	3983	X-RAY DIFFRACTION	100
4.8719-6.1253	0.184	223	0.1606	4049	X-RAY DIFFRACTION	100
6.1253-26.367	0.1932	211	0.1741	3942	X-RAY DIFFRACTION	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	3.165	-0.0085	-0.0934	0.6689	0.6035	0.9137	0.2207	0.7851	-0.5364	-0.4243	-0.2001	-0.0273	0.0077	0.0947	-0.1528	0.3353	0.0681	-0.0472	0.2834	-0.1137	0.3696	89.0818	-13.019	126.0195
2	1.9805	-0.2287	0.2138	0.9858	-0.1135	0.7533	-0.0152	0.0826	0.0292	-0.0552	-0.0116	-0.0286	-0.0131	0.1404	0.0262	0.1102	-0.0135	0.0072	0.1337	0	0.136	87.9752	5.9389	135.0252
3	5.2097	2.6078	-6.39	1.5122	-3.5428	8.4971	-0.0211	0.7172	-0.6686	-0.3685	0.0008	0.2945	0.5402	-1.1693	0.1604	0.2969	-0.0429	-0.0911	0.4009	-0.0721	0.3862	38.7566	-0.2953	132.5425
4	2.6294	0.295	-0.1532	2.8465	1.0172	3.9072	0.0723	-0.3302	-0.4734	0.1423	-0.0521	0.2257	0.4716	-0.3986	0.0093	0.1934	-0.0443	-0.0433	0.262	0.0697	0.3519	41.7421	-0.6431	147.6222
5	2.6748	-0.1384	0.6235	0.3023	-0.006	0.9473	0.131	0.0038	-0.1203	-0.0807	-0.0225	0.0577	-0.0388	-0.1407	-0.1087	0.1321	-0	0.0054	0.127	0.0283	0.211	54.2611	6.6057	144.6963
6	3.6154	-0.3265	-1.6041	1.3257	0.324	3.2896	0.156	0.5767	0.4267	-0.1798	-0.0751	0.1045	-0.3027	-0.3805	-0.0684	0.1569	0.0087	-0.0034	0.1451	0.0494	0.2206	60.0331	16.1768	139.6026
7	3.2771	0.1868	-0.2284	2.6435	-1.1026	4.95	0.2632	-0.478	0.3469	0.4282	0.2345	0.2993	-0.4372	-0.5546	-0.0843	0.2078	0.0532	0.1069	0.2592	-0.0748	0.2808	49.042	18.4598	159.4135
8	2.3678	-0.1684	-0.0502	0.5174	0.0352	1.1191	0.0156	-0.092	0.0948	0.0441	0.0071	0.0362	-0.0579	0.0382	-0.018	0.1213	-0.0179	0.0251	0.0891	-0.001	0.142	65.2384	11.0955	149.1155
9	2.6425	1.1796	2.2119	0.6139	0.9335	1.9256	0.1853	-0.3159	-0.4726	0.4017	0.0591	-0.1847	-0.0496	0.3602	-0.1666	0.2155	0.0397	-0.0119	0.3369	0.0306	0.2269	85.3749	1.2604	156.3067
10	6.4632	-3.196	-1.1787	3.8054	0.6611	3.2165	-0.0585	-0.3308	-0.1771	0.2312	0.0577	0.1938	-0.0197	-0.1768	-0.0184	0.1567	-0.067	0.0164	0.1566	0.0343	0.151	53.9496	3.6609	158.098
11	0.8033	-0.0765	0.4638	2.2642	-0.356	1.1991	0.1763	0.5056	0.0992	-0.5952	-0.2127	0.4034	-0.5253	-0.0594	0.0945	0.4774	0.1275	-0.0777	0.4632	0.0548	0.3185	67.3821	25.1607	102.2544
12	2.2079	-2.6679	1.469	6.5723	-1.6044	1.0333	0.1312	0.1583	-0.0051	0.3472	-0.0868	0.4513	-0.7342	-0.4326	-0.1374	0.5152	0.0898	-0.0277	0.4436	0.1144	0.2558	69.4784	26.3239	107.5092
13	1.164	-0.5743	-0.072	1.4169	0.3082	1.386	0.0474	0.1739	0.3093	-0.2124	-0.1056	0.0364	-0.3793	0.0315	0.0225	0.2441	-0.0308	-0.0347	0.1625	0.0735	0.2857	74.0098	28.6937	124.2379
14	0.603	0.2308	-0.3018	2.0692	-1.6909	3.0872	-0.0302	0.0533	0.1517	-0.1799	-0.3874	0.0628	-0.6659	0.1637	0.2359	0.5753	0.0766	-0.1056	0.2223	0.0219	0.4936	65.0765	36.9633	128.6678
15	3.9988	1.9195	-0.5037	1.8905	0.3274	1.306	-0.0472	-0.4096	-1.1006	0.3771	0.0402	0.0367	0.9079	-0.0441	-0.1902	1.088	0.1527	-0.2702	0.1548	0.4514	0.6147	118.1594	-20.6255	105.7013
16	3.0446	-0.0125	0.6046	2.1093	-0.0743	1.4437	0.0603	-0.8365	-0.8696	0.1894	-0.1956	0.1836	0.7595	-0.4564	0.1318	0.8077	-0.1742	0.0803	0.4681	0.1177	0.5418	101.6099	-17.6654	105.0995
17	1.1263	0.0531	-0.0734	0.9795	0.3888	1.5162	-0.0163	0.0414	-0.2165	-0.0186	-0.0131	0.0417	0.396	-0.1495	0.0297	0.3224	-0.0427	-0.0274	0.1892	0.0006	0.1778	107.5035	1.3676	97.4541
18	1.6767	0.4445	0.2295	2.5631	0.7971	2.1628	-0.0481	-0.0986	0.0413	0.0768	-0.1511	0.4274	0.3433	-0.5477	0.1203	0.2083	-0.0592	-0.0181	0.3648	0.0136	0.2304	94.8348	6.2527	104.7768
19	4.2597	0.4823	-4.5684	1.3337	0.0963	7.8937	0.2899	0.0782	-0.6407	-0.0288	-0.2552	-0.6751	0.4576	1.1414	0.0785	0.3622	0.1708	-0.2115	0.4203	0.0173	0.4023	154.5097	2.2901	101.5373
20	3.0489	0.2856	-1.1151	2.9976	-0.4076	1.9343	-0.153	0.2596	-0.4028	-0.3323	0.0304	-0.5575	0.5699	0.7204	0.0777	0.4134	0.1737	0.0269	0.6328	-0.1357	0.4144	153.7122	3.7585	83.9747
21	1.7963	0.5807	-1.059	2.4237	-1.7664	4.1665	-0.1203	0.2961	-0.4934	-0.1965	-0.0559	-0.3834	0.6028	0.326	0.1049	0.3893	0.1663	0.0268	0.4662	-0.082	0.4307	150.9936	0.6068	89.0663
22	2.6021	0.6085	0.337	0.8752	0.2258	0.9985	0.0449	0.1328	-0.249	0.0567	0.012	-0.1663	0.0913	0.2296	-0.0713	0.303	0.0722	-0.0015	0.3106	-0.0505	0.1793	138.5676	7.8929	89.1945
23	3.9659	1.5933	-2.606	1.7669	-0.8313	2.7272	0.2212	-0.6963	0.1338	0.4547	-0.2124	-0.0188	-0.2759	0.7673	0.0246	0.3121	-0.0029	-0.0178	0.3296	-0.0783	0.1797	131.5759	16.2334	94.8142
24	2.0138	0.2928	-0.1956	0.6638	0.0188	1.1972	0.0316	0.3489	0.0263	-0.0751	0.0466	-0.0101	0.1207	0.1634	-0.0594	0.2625	0.0486	0.0036	0.2716	-0.0284	0.1187	129.4512	12.6816	83.4629
25	4.2463	0.2734	-0.7653	0.8005	0.081	1.4443	0.1214	0.2034	-0.0984	-0.0922	-0.0288	-0.0172	0.2707	0.2446	-0.0787	0.4139	0.0763	-0.0292	0.3265	-0.0895	0.1918	129.061	3.3606	76.3146
26	0.2491	0.0647	-0.504	8.2866	2.8457	2.5109	0.0444	-0.2902	-0.1075	0.7764	0.023	-0.0937	0.0849	0.2645	0.1697	0.1995	0.0266	-0.1106	0.3102	0.0396	0.2534	121.5523	12.8763	134.9693
27	2.5523	0.7374	1.0466	3.9504	-1.1219	2.7004	-0.048	-0.1656	0.1281	0.3605	0.0052	-0.504	-0.2135	0.1504	0.0418	0.1928	0.0188	-0.0493	0.2617	-0.0428	0.1993	124.4757	27.8243	131.1373
28	1.9905	0.831	0.97	5.7303	0.2054	2.2774	0.0114	0.05	0.0801	-0.0696	0.0302	-0.4229	-0.1616	0.1278	-0.0919	0.1694	0.0243	-0.0202	0.2463	-0.0092	0.1764	121.1352	23.5274	127.5643
29	0.6604	0.3335	-0.0358	1.7765	0.1687	1.329	-0.0082	-0.0841	0.0752	-0.1858	0.0291	0.0334	-0.0961	-0.1071	-0.0247	0.1353	0.0274	0.0048	0.1718	-0.0141	0.1406	113.6644	24.4786	113.414
30	0.7443	0.2746	-0.1728	1.1932	0.3365	1.9639	-0.0654	0.069	0.0508	-0.2754	0.1107	-0.1162	-0.1195	0.0218	-0.0245	0.1593	0.0163	0.0133	0.1506	-0.0238	0.1474	118.8888	26.3043	107.1908
31	0.9176	-0.8438	-0.4687	0.8067	1.1336	2.8634	0.3106	0.0902	0.1937	-0.3656	-0.0658	-0.1563	-0.8146	0.3905	-0.092	0.2947	-0.0284	0.0716	0.2063	-0.014	0.2421	125.5705	30.6171	99.1403
32	3.8344	2.6863	-5.1893	5.5924	-1.4385	9.1864	-0.0043	-0.238	0.642	-0.0285	0.0083	-0.3515	-0.613	0.3571	-0.2003	0.3258	0.0417	-0.0544	0.2119	-0.0184	0.3062	120.4002	39.7664	120.8696

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 5 through 89 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 90 through 306 )
3	X-RAY DIFFRACTION	3	chain 'B' and (resid 5 through 27 )
4	X-RAY DIFFRACTION	4	chain 'B' and (resid 28 through 89 )
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 90 through 144 )
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 145 through 180 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 181 through 193 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 194 through 267 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 268 through 280 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 281 through 306 )
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 5 through 78 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 79 through 118 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 119 through 257 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 258 through 306 )
15	X-RAY DIFFRACTION	15	chain 'D' and (resid 5 through 25 )
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 26 through 89 )
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 90 through 267 )
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 268 through 306 )
19	X-RAY DIFFRACTION	19	chain 'E' and (resid 8 through 24 )
20	X-RAY DIFFRACTION	20	chain 'E' and (resid 25 through 57 )
21	X-RAY DIFFRACTION	21	chain 'E' and (resid 58 through 89 )
22	X-RAY DIFFRACTION	22	chain 'E' and (resid 90 through 144 )
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 145 through 180 )
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 181 through 267 )
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 268 through 306 )
26	X-RAY DIFFRACTION	26	chain 'F' and (resid 5 through 27 )
27	X-RAY DIFFRACTION	27	chain 'F' and (resid 28 through 78 )
28	X-RAY DIFFRACTION	28	chain 'F' and (resid 79 through 118 )
29	X-RAY DIFFRACTION	29	chain 'F' and (resid 119 through 193 )
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 194 through 246 )
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 247 through 286 )
32	X-RAY DIFFRACTION	32	chain 'F' and (resid 287 through 306 )

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