PDB-9e2b: Structure of a solute binding protein from Desulfonauticus sp. bo...

ID or keywords:

Entry

Database: PDB / ID: 9e2b

Title

Structure of a solute binding protein from Desulfonauticus sp. bound to L-tryptophan

Components

ABC-type transporter, periplasmic subunit family 3

Keywords

PEPTIDE BINDING PROTEIN / Solute binding protein / tryptophan / amino acid binding protein

Function / homology

Function and homology information

ligand-gated monoatomic ion channel activity / membrane
Similarity search - Function

Biological species

Desulfonauticus sp. 38_4375 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.8 Å

Authors

Rahman, M. / Frkic, R.L. / Smith, O.B. / Jackson, C.J.

Funding support

Australia, 2items

Citation

Journal: To Be Published
Title: Structure of a solute binding protein from Desulfonauticus sp. bound to L-tryptophan
Authors: Rahman, M. / Frkic, R.L. / Smith, O.B. / Jackson, C.J.

History

Deposition	Oct 22, 2024	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Nov 6, 2024	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	9e2b.cif.gz	629.8 KB	Display	PDBx/mmCIF format
PDB format	pdb9e2b.ent.gz	519.7 KB	Display	PDB format
PDBx/mmJSON format	9e2b.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	9e2b_validation.pdf.gz	2.1 MB	Display	wwPDB validaton report
Full document	9e2b_full_validation.pdf.gz	2.1 MB	Display
Data in XML	9e2b_validation.xml.gz	74.8 KB	Display
Data in CIF	9e2b_validation.cif.gz	98.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/e2/9e2b ftp://data.pdbj.org/pub/pdb/validation_reports/e2/9e2b	HTTPS FTP

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Related structure data

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
Related items in Molecule of the Month	#235 - Jul 2019 AMPA Receptor similarity (2) #228 - Dec 2018 Directed Evolution of Enzymes similarity (1)

Deposited unit

A: ABC-type transporter, periplasmic subunit family 3

B: ABC-type transporter, periplasmic subunit family 3

C: ABC-type transporter, periplasmic subunit family 3

D: ABC-type transporter, periplasmic subunit family 3

E: ABC-type transporter, periplasmic subunit family 3

F: ABC-type transporter, periplasmic subunit family 3

hetero molecules

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

1

A: ABC-type transporter, periplasmic subunit family 3

B: ABC-type transporter, periplasmic subunit family 3

D: ABC-type transporter, periplasmic subunit family 3

hetero molecules

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

2

C: ABC-type transporter, periplasmic subunit family 3

E: ABC-type transporter, periplasmic subunit family 3

F: ABC-type transporter, periplasmic subunit family 3

hetero molecules

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

Unit cell

Length a, b, c (Å)	74.507, 74.593, 92.348
Angle α, β, γ (deg.)	98.21, 91.24, 119.84
Int Tables number	1
Space group name H-M	P1

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Protein , 1 types, 6 molecules ABCDEF

#1: Protein	ABC-type transporter, periplasmic subunit family 3 Mass: 30652.303 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Desulfonauticus sp. 38_4375 (bacteria) / Gene: XD41_0486 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A101DJ27

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Non-polymers , 6 types, 924 molecules

#2: Chemical	ChemComp-TRP / TRYPTOPHAN Type: L-peptide linking / Mass: 204.225 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₁₁H₁₂N₂O₂ / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical	... ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 23 / Source method: obtained synthetically / Formula: C₂H₆O₂
#4: Chemical	ChemComp-PEG / DI(HYDROXYETHYL)ETHER Mass: 106.120 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₄H₁₀O₃
#5: Chemical	ChemComp-ACT / ACETATE ION Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂H₃O₂
#6: Chemical	ChemComp-PG4 / TETRAETHYLENE GLYCOL Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₈H₁₈O₅ / Comment: precipitant*YM
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 889 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y
Has protein modification	N

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 2.38 Å³/Da / Density % sol: 48.36 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: 27% PEG 3350, 0.1M sodium acetate pH 4.5

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
Detector	Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 3, 2024
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9537 Å / Relative weight: 1
Reflection	Resolution: 1.8→39.14 Å / Num. obs: 153832 / % possible obs: 97.8 % / Redundancy: 3.7 % / CC_1/2: 0.993 / R_merge(I) obs: 0.089 / R_pim(I) all: 0.054 / R_rim(I) all: 0.104 / Χ²: 0.99 / Net I/σ(I): 7.6 / Num. measured all: 568516
Reflection shell	Resolution: 1.8→1.83 Å / % possible obs: 96.4 % / Redundancy: 3.8 % / R_merge(I) obs: 1.254 / Num. measured all: 28491 / Num. unique obs: 7559 / CC_1/2: 0.484 / R_pim(I) all: 0.746 / R_rim(I) all: 1.461 / Χ²: 0.99 / Net I/σ(I) obs: 0.8

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Processing

Software

Name	Version	Classification
PHENIX	(1.20.1_4487: ???)	refinement
Aimless		data scaling
XDS		data reduction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.8→39.14 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 24.24 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2161	7969	5.18 %
R_work	0.185	-	-
obs	0.1866	153748	97.72 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 1.8→39.14 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12138	0	224	889	13251

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007
X-RAY DIFFRACTION	f_angle_d	0.886
X-RAY DIFFRACTION	f_dihedral_angle_d	16.042	4723
X-RAY DIFFRACTION	f_chiral_restr	0.057	1843
X-RAY DIFFRACTION	f_plane_restr	0.009	2158

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 (%)
1.8-1.82	0.4608	219	0.4365	4914	X-RAY DIFFRACTION	96
1.82-1.84	0.444	262	0.3979	4748	X-RAY DIFFRACTION	96
1.84-1.86	0.4113	229	0.3526	4888	X-RAY DIFFRACTION	97
1.86-1.89	0.3808	281	0.3181	4661	X-RAY DIFFRACTION	96
1.89-1.91	0.3183	321	0.2904	4824	X-RAY DIFFRACTION	97
1.91-1.94	0.3119	263	0.2689	4742	X-RAY DIFFRACTION	97
1.94-1.97	0.3099	259	0.2426	4895	X-RAY DIFFRACTION	97
1.97-2	0.2638	250	0.2288	4764	X-RAY DIFFRACTION	97
2-2.03	0.2683	247	0.2225	4836	X-RAY DIFFRACTION	97
2.03-2.06	0.2552	260	0.215	4848	X-RAY DIFFRACTION	97
2.06-2.1	0.255	293	0.212	4808	X-RAY DIFFRACTION	97
2.1-2.13	0.2507	284	0.214	4879	X-RAY DIFFRACTION	97
2.13-2.18	0.2516	276	0.214	4736	X-RAY DIFFRACTION	97
2.18-2.22	0.2347	302	0.2064	4837	X-RAY DIFFRACTION	98
2.22-2.27	0.2438	263	0.2046	4908	X-RAY DIFFRACTION	98
2.27-2.32	0.2154	250	0.1805	4841	X-RAY DIFFRACTION	98
2.32-2.38	0.2408	251	0.1787	4845	X-RAY DIFFRACTION	98
2.38-2.44	0.2206	236	0.1805	4925	X-RAY DIFFRACTION	98
2.44-2.51	0.2278	221	0.1936	4881	X-RAY DIFFRACTION	98
2.51-2.6	0.242	276	0.1898	4893	X-RAY DIFFRACTION	98
2.6-2.69	0.2434	260	0.1848	4887	X-RAY DIFFRACTION	98
2.69-2.8	0.2184	280	0.1817	4877	X-RAY DIFFRACTION	98
2.8-2.92	0.2253	262	0.1883	4874	X-RAY DIFFRACTION	98
2.92-3.08	0.2368	254	0.1926	4962	X-RAY DIFFRACTION	99
3.08-3.27	0.2185	248	0.1915	4905	X-RAY DIFFRACTION	99
3.27-3.52	0.22	288	0.183	4917	X-RAY DIFFRACTION	99
3.52-3.88	0.1824	300	0.1622	4889	X-RAY DIFFRACTION	99
3.88-4.44	0.1582	350	0.1387	4847	X-RAY DIFFRACTION	99
4.44-5.59	0.1541	269	0.1384	4921	X-RAY DIFFRACTION	99
5.59-39.14	0.1609	215	0.1457	5027	X-RAY DIFFRACTION	100

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	2.4729	1.8329	1.0783	6.8264	-0.1348	1.7597	0.0079	0.5258	-0.0782	-0.8825	0.0046	-0.3529	-0.026	0.258	-0.0204	0.2533	0.0532	0.0601	0.4121	0.076	0.1816	16.9211	-13.9518	-20.1353
2	0.8431	0.0932	0.0564	1.5234	0.2079	0.5611	0.0524	0.1093	0.2862	-0.0484	-0.0759	-0.0214	-0.0862	0.0132	0.027	0.1771	0.0309	-0.0094	0.2204	0.0792	0.2336	7.7071	2.0077	-5.2043
3	2.2171	-1.6376	-1.204	2.7326	1.5172	1.656	-0.0153	0.0259	0.1373	0.0906	-0.0187	0.218	0.0026	-0.2002	0.052	0.1763	0.0399	-0.0007	0.2029	0.0477	0.2531	-8.2919	-2.2546	3.7903
4	2.7625	-0.8215	0.4694	2.6225	0.5633	2.1403	-0.0163	-0.0191	-0.0495	0.0171	-0.0443	0.6147	-0.0513	-0.2749	0.0506	0.2176	0.0521	-0.0327	0.2574	0.031	0.3794	-16.0749	4.8818	2.588
5	0.9469	-0.4081	0.011	1.0973	0.2376	0.3681	-0.0514	-0.0325	0.1504	0.0809	0.0203	0.0975	-0.0562	-0.017	0.0234	0.192	0.0263	0.011	0.1801	0.0388	0.2366	1.8794	-0.2597	6.1805
6	3.418	-0.5104	1.4959	2.1435	1.4746	2.5254	-0.0976	0.7801	0.3544	-0.5163	0.0462	0.0203	-0.0589	0.1072	0.0367	0.2917	0.0594	-0.0325	0.3086	0.0537	0.1424	-0.0038	-17.3826	-22.8791
7	1.0123	-0.1384	0.1661	1.6442	-0.3618	0.965	0.0398	0.1742	-0.1772	-0.0826	0.0206	0.2352	0.0579	-0.1199	-0.0573	0.2015	0.0176	-0.0475	0.2779	-0.0316	0.2542	-10.564	-31.3098	-8.3808
8	3.2388	1.8737	0.2119	6.0166	-0.9676	1.9097	0.144	-0.4513	-0.4899	0.463	-0.0835	-0.1446	0.0814	0.008	-0.0411	0.2489	0.0143	0.0006	0.2595	0.0116	0.2631	-8.2181	-48.215	13.3455
9	2.3092	0.1015	-0.367	2.5685	-0.7581	2.3868	0.0041	0.0449	-0.3976	0.0096	-0.0205	-0.1169	0.2062	0.1085	0.0124	0.2126	0.0247	-0.0137	0.2146	-0.0364	0.3226	-5.8581	-51.8212	4.4367
10	0.7654	0.5515	-0.1213	1.5877	-0.4297	0.1098	0.0645	0.006	-0.0796	0.1616	-0.0595	0.0924	-0.0275	-0.0269	0.0008	0.1969	0.0081	-0.0188	0.2158	-0.0167	0.2231	-7.7733	-35.6902	3.0986
11	4.7606	0.4175	-2.016	2.8428	-1.1169	3.3244	0.0448	-0.0674	-0.3624	0.2988	-0.0378	0.3476	0.083	-0.2067	0.0299	0.1932	0.0278	0.0169	0.2276	0.0175	0.2754	-18.212	-28.2929	6.6584
12	1.5725	0.3209	-0.0996	1.9146	0.4969	1.2203	-0.067	0.0705	0.1135	-0.3277	0.0436	-0.1463	-0.0305	0.065	-0.0155	0.3043	-0.0438	0.0416	0.1767	0.0476	0.2198	12.0465	4.6538	-54.3949
13	1.2357	-0.3033	0.0134	1.6318	0.6967	1.3283	-0.0656	-0.1132	0.0873	-0.0148	-0.063	0.1003	-0.0227	-0.1706	0.1276	0.251	-0.0376	-0.014	0.2279	-0.0116	0.1887	0.1094	4.3331	-42.0989
14	4.151	-1.1393	-2.3352	3.5737	0.4098	5.0853	-0.0747	0.0605	0.2263	-0.3263	-0.138	0.3525	-0.1054	-0.7157	0.2151	0.3011	-0.0138	-0.0803	0.3634	-0.0699	0.2632	-11.4783	5.0795	-38.0914
15	5.2379	1.4066	-0.3001	4.8039	-0.0737	2.8948	0.0479	0.0552	0.6328	-0.2306	-0.3001	0.2592	-0.4717	-0.5497	0.2275	0.4026	0.0706	-0.052	0.4248	-0.1014	0.3466	-12.2478	13.9379	-35.303
16	1.8392	-0.4942	-0.803	1.5791	0.5375	3.2874	-0.1161	-0.3596	0.276	0.2148	0.073	0.1058	-0.0825	-0.1656	0.054	0.2386	-0.0124	-0.0151	0.2836	-0.0685	0.2717	-3.1408	7.4025	-32.8455
17	2.4669	-0.0351	2.279	1.473	0.6148	4.2917	0.0634	0.1088	-0.0698	-0.1524	-0.0069	-0.1389	0.1062	-0.0898	-0.053	0.3115	-0.0391	0.0653	0.1864	-0.0077	0.1877	14.025	-7.4683	-49.1457
18	3.3975	-0.1493	0.1411	1.7385	-0.2221	3.4784	-0.022	-0.4527	0.214	0.5406	0.035	-0.0895	-0.1037	-0.0144	-0.037	0.2696	-0.063	-0.0026	0.2802	-0.0502	0.2333	13.6164	6.7225	-32.0703
19	2.9556	-2.2903	-0.7465	5.3462	-0.6663	1.0583	0.4013	0.7337	-0.2351	-0.7397	-0.2884	0.1188	0.3376	0.355	-0.1455	0.2744	0.037	0.0131	0.3281	-0.0921	0.1835	11.4872	-30.6812	-20.8176
20	1.2485	-0.6373	0.1785	2.2377	-0.221	0.5125	0.0276	0.1091	-0.1204	0.0296	-0.0381	-0.3119	0.0506	0.1089	0.0219	0.1609	0.0307	0.0058	0.1998	-0.0079	0.2201	24.7804	-30.3769	-2.5721
21	2.5339	-0.3153	0.1885	0.721	-0.7211	2.4929	0.0658	0.0385	0.2901	0.6309	-0.0947	-0.488	-0.5279	0.5633	0.0602	0.4254	-0.0604	-0.1665	0.3348	0.0209	0.4007	33.9496	-13.9589	14.9196
22	2.2064	-1.5446	-0.1909	8.7201	1.2937	2.5259	-0.2052	0.0029	0.0512	0.0416	0.185	-1.1784	-0.2596	0.7177	-0.0161	0.4284	-0.0625	-0.0659	0.551	0.0815	0.544	41.1913	-17.43	10.2356
23	3.9833	-1.6284	1.7275	0.6844	-0.5129	2.8377	0.3152	0.0008	-0.3271	0.6677	-0.0912	-1.0003	0.4047	0.8778	-0.0836	0.493	0.0491	-0.2441	0.4474	-0.0166	0.5603	36.7068	-23.0552	16.3135
24	0.8361	0.2122	0.1622	1.7445	0.0071	1.3237	0.0775	-0.0232	-0.0733	0.3364	-0.0688	-0.1542	0.1624	0.0907	-0.007	0.209	0.0487	-0.0322	0.1996	0.0115	0.1816	19.9785	-24.9423	4.5315
25	1.3142	0.2504	0.4369	2.5714	-0.0748	3.086	-0.0782	-0.3818	-0.2561	0.4095	0.0868	-0.2944	0.1036	0.0695	0.0127	0.262	0.0176	-0.0658	0.2196	0.031	0.236	22.1682	-36.2571	13.3446
26	8.9197	1.3021	-1.2155	2.0078	0.4919	2.5587	-0.2095	0.8906	0.3057	-0.6291	0.2257	0.0572	-0.1715	-0.3189	0.01	0.4823	-0.0574	-0.0501	0.2922	-0.0155	0.21	-3.7147	-9.1724	-65.3507
27	1.2227	-0.2666	-0.229	1.8671	-0.3266	0.9859	-0.026	-0.0113	-0.1332	-0.1871	0.0318	0.3357	0.0874	-0.105	-0.0044	0.2813	-0.0891	-0.0284	0.2719	-0.0601	0.2732	-13.6977	-24.4885	-50.8076
28	1.0536	0.8422	-1.0433	1.8718	-1.3291	1.2377	0.0096	0.0106	-0.11	-0.0589	-0.08	-0.077	0.2227	-0.0731	0.0367	0.3043	-0.0926	0.0117	0.2668	-0.0545	0.2154	0.8774	-29.4171	-47.5717
29	3.6747	-0.7255	-5.2669	2.8242	-0.1651	8.2931	-0.0691	-0.9947	-0.6609	0.1119	-0.0883	-0.7076	0.4288	0.7952	0.168	0.4112	-0.0738	-0.1018	0.4311	0.071	0.5178	-0.1101	-52.762	-33.2176
30	1.9727	0.7091	-0.4089	1.64	-0.6772	1.2139	0.0012	0.0473	-0.2623	-0.1551	-0.0211	-0.1417	0.0889	-0.0347	0.0261	0.3459	-0.0824	0.0071	0.2952	-0.0793	0.3616	-6.3428	-44.8521	-41.7787
31	0.7635	0.5653	-0.3369	1.5926	-0.2073	0.1492	0.0571	-0.0932	-0.0445	0.0885	-0.0979	-0.062	0.0047	-0.0201	0.0478	0.3224	-0.0869	0.0005	0.2676	-0.0345	0.2104	-3.1649	-26.2745	-43.2604
32	2.5729	-1.3085	-0.0936	2.0898	-0.3464	5.4139	0.0971	-0.4446	-0.2371	0.2769	-0.0845	0.1506	0.1805	-0.2193	0.0076	0.2849	-0.0986	0.0315	0.3316	-0.016	0.222	-13.742	-24.5577	-34.2834
33	1.4458	-0.4454	0.1811	1.8607	-0.1302	0.7272	-0.0125	0.111	-0.0812	-0.0621	-0.0656	-0.1411	0.0624	0.045	0.0644	0.3339	-0.0462	0.0859	0.2208	-0.0267	0.2064	22.1166	-23.7353	-57.1367
34	1.9391	-0.2481	0.6422	0.755	0.0023	0.6404	-0.1261	-0.1819	0.2265	0.0736	0.0042	-0.5435	-0.0265	0.2569	0.1713	0.4166	-0.0513	0.0187	0.4097	-0.0364	0.5494	33.9566	-15.2105	-40.576
35	2.0301	-0.2435	0.9054	1.6097	0.0671	1.5095	-0.2699	-0.4505	-0.0272	0.3051	0.2329	-0.1952	0.0836	-0.0084	-0.0726	0.4059	0.0314	0.0202	0.2939	0.0147	0.2896	26.1531	-31.9448	-38.7025

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 22 through 41 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 42 through 111 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 112 through 143 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 144 through 189 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 190 through 301 )
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 22 through 41 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 42 through 124 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 125 through 143 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 144 through 189 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 190 through 251 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 252 through 301 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 22 through 65 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 66 through 152 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 153 through 169 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 170 through 189 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 190 through 235 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 236 through 251 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 252 through 301 )
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 22 through 41 )
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 42 through 124 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 125 through 169 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 170 through 189 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 190 through 209 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 210 through 251 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 252 through 301 )
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 23 through 41 )
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 42 through 107 )
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 108 through 133 )
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 134 through 152 )
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 153 through 209 )
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 210 through 251 )
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 252 through 301 )
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 22 through 122 )
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 123 through 251 )
35	X-RAY DIFFRACTION	35	chain 'F' and (resid 252 through 301 )

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