PDB-4o94: Crystal structure of a trap periplasmic solute binding protein fr...

ID or keywords:

Entry

Database: PDB / ID: 4o94

Title

Crystal structure of a trap periplasmic solute binding protein from Rhodopseudomonas palustris HaA2 (RPB_3329), Target EFI-510223, with bound succinate

Components

TRAP dicarboxylate transporter DctP subunit

Keywords

TRANSPORT PROTEIN / TRAP PERIPLASMIC SOLUTE BINDING FAMILY /

ENZYME FUNCTION INITIATIVE / EFI /

Structural Genomics

Function / homology

Function and homology information

transmembrane transport / outer membrane-bounded periplasmic space
Similarity search - Function

Biological species

Rhodopseudomonas palustris (phototrophic)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

SAD / Resolution: 2 Å

Authors

Vetting, M.W. / Al Obaidi, N.F. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Stead, M. / Attonito, J.D. / Scott Glenn, A. / Chowdhury, S. / Evans, B. ...

Citation

Journal: Biochemistry / Year: 2015
Title: Experimental strategies for functional annotation and metabolism discovery: targeted screening of solute binding proteins and unbiased panning of metabolomes.
Authors: Vetting, M.W. / Al-Obaidi, N. / Zhao, S. / San Francisco, B. / Kim, J. / Wichelecki, D.J. / Bouvier, J.T. / Solbiati, J.O. / Vu, H. / Zhang, X. / Rodionov, D.A. / Love, J.D. / Hillerich, B.S. ...

History

Deposition	Jan 1, 2014	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jan 22, 2014	Provider: repository / Type: Initial release
Revision 1.1	Feb 25, 2015	Group: Database references

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4o94.cif.gz	696.9 KB	Display	PDBx/mmCIF format
PDB format	pdb4o94.ent.gz	611.2 KB	Display	PDB format
PDBx/mmJSON format	4o94.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/o9/4o94 ftp://data.pdbj.org/pub/pdb/validation_reports/o9/4o94	HTTPS FTP

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Related structure data

Related structure data	4ln5C 4mcoC 4mevC 4mhfC 4mijC 4mncC 4mniC 4mx6C 4n15C 4n17C 4n4uC 4n6dC 4n6kC 4n8gC 4n8yC 4n91C 4napC 4nf0C 4ng7C 4nguC 4nhbC 4nn3C 4nq8C 4nx1C 4o7mC 4o8mC 4oa4C 4oanC 4ovpC 4ovqC 4ovrC 4ovsC 4ovtC 4p1eC 4p1lC 4p3lC 4p47C 4p56C 4p8bC 4p9kC 4pafC 4paiC 4pakC 4pbhC 4pbqC 4pc9C 4pcdC 4pddC 4pdhC 4pe3C 4petC 4pf6C 4pf8C 4pfbC 4pfiC 4pfrC 4pgnC 4pgpC 4uabC C: citing same article (ref.)
Similar structure data	1gx2-1 6npn-3 2hpg-2 6x5q-d 2hiw-2 5xdw-d 4jb0-d 7kl4-d 2h6d-d 2hiw-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) 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
Other databases	TargetTrack: EFI-510223

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: TRAP dicarboxylate transporter DctP subunit

B: TRAP dicarboxylate transporter DctP subunit

C: TRAP dicarboxylate transporter DctP subunit

D: TRAP dicarboxylate transporter DctP subunit

hetero molecules

152 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: TRAP dicarboxylate transporter DctP subunit

hetero molecules

defined by author&software
37.9 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: TRAP dicarboxylate transporter DctP subunit

hetero molecules

defined by author&software
38 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: TRAP dicarboxylate transporter DctP subunit

hetero molecules

defined by author&software
38 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: TRAP dicarboxylate transporter DctP subunit

hetero molecules

defined by author&software
37.9 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	46.469, 112.845, 136.294
Angle α, β, γ (deg.)	90.00, 95.91, 90.00
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	TRAP dicarboxylate transporter DctP subunit Mass: 37677.223 Da / Num. of mol.: 4 / Fragment: UNP residues 23-332 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rhodopseudomonas palustris (phototrophic) Strain: HaA2 / Gene: RPB_3329 / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q2IUT5
#2: Chemical	ChemComp-CL / CHLORIDE ION / Chloride Mass: 35.453 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: Cl
#3: Chemical	ChemComp-SIN / SUCCINIC ACID / Succinic acid Mass: 118.088 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₄H₆O₄
#4: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 968 / 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: 2.36 Å³/Da / Density % sol: 47.85 %
Crystal grow	Temperature: 298 K / Method: sitting drop vapor diffusion / pH: 4 Details: Protein (30.3 mg/ml, 10 mM HEPES pH 7.5, 5 mM DTT, 10 mM Succinate); Reservoir (1 M Lithium Chloride 0.1 M tri-Sodium Citrate pH 4, 20 %(w/v) PEG 6000); Cryoprotection (80% of 50% Peg3350, ...Details: Protein (30.3 mg/ml, 10 mM HEPES pH 7.5, 5 mM DTT, 10 mM Succinate); Reservoir (1 M Lithium Chloride 0.1 M tri-Sodium Citrate pH 4, 20 %(w/v) PEG 6000); Cryoprotection (80% of 50% Peg3350, 20% Reservoir), sitting drop vapor diffusion, temperature 298K

Crystal

Density Matthews: 2.36 Å³/Da / Density % sol: 47.85 %

Crystal grow

Temperature: 298 K / Method: sitting drop vapor diffusion / pH: 4
Details: Protein (30.3 mg/ml, 10 mM HEPES pH 7.5, 5 mM DTT, 10 mM Succinate); Reservoir (1 M Lithium Chloride 0.1 M tri-Sodium Citrate pH 4, 20 %(w/v) PEG 6000); Cryoprotection (80% of 50% Peg3350, ...

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 31-ID / Wavelength: 0.9793 Å

Detector

Type: RAYONIX MX225HE / Detector: CCD / Date: Nov 26, 2013 / Details: MIRRORS

Radiation

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

Radiation wavelength

Wavelength: 0.9793 Å / Relative weight: 1

Reflection

Resolution: 2→135.57 Å / Num. all: 90352 / Num. obs: 90352 / % possible obs: 95.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.8 % / B_iso Wilson estimate: 18.23 Å² / R_merge(I) obs: 0.12 / R_sym value: 0.12 / Net I/σ(I): 10.8

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
2-2.11	4.3	0.61	1.1	51688	11890	0.61	86.5
2.11-2.24	4.6	0.454	1.5	55008	11850	0.454	91.6
2.24-2.39	5.1	0.34	2	58496	11581	0.34	94.8
2.39-2.58	5.5	0.265	2.5	61798	11138	0.265	97.8
2.58-2.83	6.2	0.195	3.5	64091	10385	0.195	99.6
2.83-3.16	6.7	0.134	5.2	63480	9485	0.134	99.8
3.16-3.65	7.1	0.092	7.7	59291	8372	0.092	100
3.65-4.47	7.2	0.069	9.9	50936	7076	0.069	100
4.47-6.32	7.4	0.062	10.7	40549	5509	0.062	100
6.32-135.57	7.1	0.052	12.5	21857	3066	0.052	99.6

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Processing

Software

Name	Version	Classification
SCALA	3.3.20	data scaling
PHENIX	1.8.1_1168	refinement
PDB_EXTRACT	3.14	data extraction
MOSFLM		data reduction
PHENIX	AUOTSOLVE	phasing

Refinement

Method to determine structure:

SAD / Resolution: 2→45.19 Å / Occupancy max: 1 / Occupancy min: 0.17 / FOM work R set: 0.8643 / SU ML: 0.22 / σ(F): 0 / σ(I): 0 / Phase error: 21.19 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2144	4544	5.03 %	RANDOM
R_work	0.1631	-	-	-
all	0.1657	90284	-	-
obs	0.1657	90284	95.75 %	-

Solvent computation

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

Displacement parameters

B_iso max: 86.3 Å² / B_iso mean: 22.849 Å² / B_iso min: 0.54 Å²

Refinement step

Cycle: LAST / Resolution: 2→45.19 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9567	0	47	968	10582

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.013	9813
X-RAY DIFFRACTION	f_angle_d	1.316	13249
X-RAY DIFFRACTION	f_chiral_restr	0.076	1442
X-RAY DIFFRACTION	f_plane_restr	0.006	1731
X-RAY DIFFRACTION	f_dihedral_angle_d	14.611	3611

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 (%)
2-2.0227	0.316	127	0.2095	2524	2651	84
2.0227-2.0465	0.2293	144	0.1944	2512	2656	87
2.0465-2.0715	0.2835	151	0.188	2557	2708	87
2.0715-2.0977	0.2688	140	0.1893	2649	2789	88
2.0977-2.1253	0.2464	133	0.1876	2654	2787	88
2.1253-2.1544	0.2868	140	0.1824	2669	2809	91
2.1544-2.1852	0.2714	141	0.1848	2748	2889	92
2.1852-2.2178	0.2218	131	0.1703	2780	2911	91
2.2178-2.2525	0.268	124	0.1638	2768	2892	94
2.2525-2.2894	0.2397	175	0.1651	2752	2927	94
2.2894-2.3289	0.2143	166	0.1539	2842	3008	93
2.3289-2.3712	0.2521	149	0.1486	2821	2970	97
2.3712-2.4168	0.2088	179	0.1538	2860	3039	97
2.4168-2.4661	0.2211	152	0.1571	2879	3031	97
2.4661-2.5198	0.2264	156	0.1563	2939	3095	99
2.5198-2.5784	0.2266	159	0.1573	2945	3104	98
2.5784-2.6429	0.2305	163	0.1575	2917	3080	99
2.6429-2.7143	0.2323	148	0.1609	3012	3160	99
2.7143-2.7942	0.2286	148	0.1718	2942	3090	100
2.7942-2.8843	0.2129	189	0.173	2977	3166	100
2.8843-2.9874	0.2422	149	0.1696	2954	3103	100
2.9874-3.107	0.2359	157	0.1753	3036	3193	100
3.107-3.2484	0.2451	187	0.172	2909	3096	100
3.2484-3.4196	0.2139	153	0.1767	2990	3143	100
3.4196-3.6337	0.2195	153	0.163	2990	3143	100
3.6337-3.9141	0.1714	159	0.1474	3003	3162	100
3.9141-4.3078	0.1514	139	0.1319	3010	3149	100
4.3078-4.9304	0.1427	153	0.1302	2995	3148	100
4.9304-6.2093	0.179	129	0.1563	3055	3184	100
6.2093-45.2015	0.1921	150	0.1857	3051	3201	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	0.0428	0.0417	0.034	0.0288	0.0324	0.0411	0.059	-0.0026	0.0743	0.0222	-0.0439	0.0484	-0.0627	-0.0515	-0.0125	0.0931	0.0146	0.0217	0.0519	0.0052	0.0591	8.9556	10.235	15.0674
2	0.1019	0.0224	-0.0211	0.26	-0.0678	0.1599	-0.0029	0.005	-0.046	-0.0437	-0.034	0.0202	0.0136	0.0093	-0.0393	0.0712	-0.0016	-0.0054	0.073	0.0219	0.0649	16.5639	-2.6868	3.501
3	0.2162	0.0956	0.1489	0.2612	0.1637	0.1479	-0.1046	-0.0924	0.0168	-0.0231	-0.0716	0.0836	-0.0822	-0.0073	-0.1379	0.1358	0.0424	0.0121	0.0716	0.0709	0.1391	8.7549	11.156	4.4565
4	0.0156	-0.0036	0.0103	0.0089	0.0009	-0.0001	-0.047	0.0931	-0.0645	-0.0534	0.0263	0.0118	0.042	0.07	-0.0005	0.1666	-0.0591	0.0117	0.1637	-0.0182	0.1169	21.2367	-6.4535	-13.2519
5	0.005	-0.0024	-0	0.0042	-0.0034	0.0004	0.0185	0.0356	0.0411	0.0007	-0.0631	0.0042	0.028	-0.0533	-0.0001	0.2019	-0.0068	-0.0398	0.2232	0.0107	0.1753	4.8294	-4.9424	-14.977
6	0.0278	-0.0339	0.0336	0.0691	-0.0116	0.0441	0.0694	0.0027	-0.0054	-0.0735	0.0369	0.0363	0.0829	0.0008	0.138	0.1006	0.004	-0.0576	0.0666	-0.0427	-0.0168	9.2261	-6.005	49.6998
7	0.0425	0.0506	0.0555	0.1134	0.0999	0.1836	-0.0534	-0.0713	0.0459	-0.0653	-0.0639	0.0564	-0.0405	-0.0395	-0.1305	0.0096	0.0178	-0.0008	0.0736	-0.0172	0.0359	5.2414	6.6405	63.5112
8	0.0557	0.0078	0.0418	0.0121	0.005	0.0319	0.0044	-0.0878	0.0193	0.0131	-0.0246	0.0358	0.0109	-0.1282	-0.023	0.0007	0.0116	0.0074	0.0821	-0.0425	0.1046	-1.5516	5.7221	60.565
9	0.0006	0.0002	-0.004	0.0265	-0.0012	0.0047	0.0064	0.0337	0.0037	0.0524	0.0073	-0.0131	-0.0153	-0.1091	0.0002	0.0409	-0.0041	-0.0009	0.0922	-0.0188	0.0553	22.8558	4.5211	79.5458
10	0.0197	0.0071	-0.0155	0.0157	-0.0164	0.0253	-0.0336	-0.0182	0.0762	0.0267	0.025	-0.0111	-0.087	0.0574	-0.0177	0.0735	-0.0006	-0.0166	0.0691	-0.0093	0.0675	22.2981	10.8676	68.7632
11	0.0173	0.0369	0.0013	0.0463	-0.0075	0.0089	0.0091	-0.0555	0.0029	0.0402	0	0.0301	0.0193	-0.0406	0.0019	0.04	0.0135	-0.0036	0.0628	-0.0062	0.0395	14.5874	0.7237	64.2758
12	0.0111	-0.0023	0.0093	0.0177	0.0234	0.0576	-0.0722	0.0516	-0.0562	-0.0263	-0.006	0.0437	0.0905	-0.0631	-0.0126	0.1186	-0.0268	-0.0244	0.0825	0.0033	0.0862	5.7514	-9.7106	61.1554
13	0.0055	-0.0084	-0.0006	0.0069	0.0043	0.0013	-0.0326	-0.0474	-0.0644	0.0555	0.0245	0.0057	-0.0303	-0.0354	-0	0.1381	0.0367	0.0032	0.1017	-0.0015	0.062	17.7356	2.7163	84.6334
14	0.0007	-0.0032	-0.0013	0.0106	-0.0008	0.0002	-0.0377	-0.0528	0.0675	-0.0155	-0.0219	-0.0119	0.0032	-0.1168	0.0001	0.0945	0.016	-0	0.2227	-0.0531	0.1584	1.118	13.6596	76.7508
15	0.0159	0.0003	-0.011	0.0235	-0.0053	0.0087	-0.0318	0.0481	0.0383	0.0948	0.004	0.007	-0.0036	0.0385	-0.0005	0.0876	-0.0114	-0.0008	0.0603	-0.0208	0.0784	15.3481	-15.1786	40.1781
16	0.0263	0.0033	0.0169	0.0059	-0.0003	0.0084	-0.0233	0.0421	0.0257	-0.0407	-0.0053	0.0371	-0.0378	-0.0002	-0.0073	0.0599	-0.0117	-0.0029	0.0614	-0.0151	0.0532	17.3658	-19.5658	24.6938
17	0.0026	-0.0025	-0.0031	0.0066	0.0038	0.0038	-0.0544	0.0115	-0.0424	-0.0114	0.0277	-0.0329	-0.0048	-0.0218	-0	0.0748	-0.0023	-0.0032	0.0846	-0.0027	0.1096	21.2862	-38.0164	28.3006
18	0.0067	-0.0111	-0.0043	0.0886	0.0643	0.0473	0.0423	0.0548	-0.0926	-0.0136	0.0529	-0.1608	-0.0428	-0.0037	0.0144	0.0869	0.0131	-0.0037	0.1015	-0.008	0.1002	25.9757	-25.1175	27.556
19	0.0035	0.0009	0.003	0.0147	0.0074	0.0115	-0.0306	-0.0011	0.0165	0.0401	0.0388	-0.0283	0.0563	0.022	-0	0.0519	-0.0051	-0.0087	0.0624	-0.0022	0.1159	1.4752	-44.1456	27.0754
20	0.0154	-0.0046	0.0054	0.0127	-0.0059	0.0232	-0.0192	0.1012	0.0058	-0.0342	0.0386	0.0392	-0.0046	-0.0189	0.0484	-0.1208	-0.1773	-0.0858	-0.1468	-0.1012	0.0053	2.0962	-32.7353	21.7304
21	0.0515	-0.0443	0.0309	0.0481	0.0088	0.0313	0.0221	-0.0548	0.0079	0.0791	-0.0234	0.0383	0.027	0.0236	0.0148	0.0516	-0.0161	0.0109	0.0624	-0.0079	0.0867	9.5038	-29.3629	32.1351
22	0.1063	-0.0491	-0.0339	0.1561	0.0583	0.0482	-0.0501	-0.0854	0.0787	0.1461	0.1159	-0.1206	0.1046	0.0307	0.0622	0.0909	-0.0329	-0.0307	0.0821	0.0267	0.0716	18.5867	-26.9705	42.8186
23	0.013	0.0052	-0.0011	0.0043	-0.0016	0.0036	0.0009	0.0208	-0.0647	-0.0096	0.0799	0.0757	-0.0063	-0.0216	0.0005	0.1226	0.0151	0.0153	0.0902	-0.0243	0.1528	5.9138	-49.0674	28.4056
24	0.0031	-0.0041	0.0015	0.0212	0.0064	0.0047	-0.083	0.0471	-0.0587	-0.0655	0.0017	-0.1625	0.0213	-0.0083	0.0004	0.0938	0.0001	0.0053	0.134	-0.0223	0.1506	23.5217	-40.7046	18.737
25	0.002	0.0033	0.0121	0.0052	-0.0261	0.0678	0.0858	-0.0477	-0.0114	0.1116	-0.0065	0.0335	0.0626	-0.1246	0.0329	0.0968	-0.0802	0.0471	-0.0595	0.1198	-0.0126	17.965	-38.1444	108.2214
26	0.2393	0.0339	-0.0571	0.0396	-0.0097	0.0242	-0.0605	0.1166	-0.0597	0.0073	0.1056	0.1053	-0.0357	-0.0815	0.008	0.0819	0.0245	0.002	0.0682	0.0247	0.0424	17.4904	-25.1603	94.0248
27	0.0377	-0.0103	0.0106	0.0234	-0.0464	0.116	-0.053	0.0406	0.1591	0.063	0.0927	0.0312	-0.0879	-0.0562	0.0196	0.0459	0.0313	-0.0153	0.0779	0.0337	0.1054	20.6551	-20.8916	95.2481
28	0.0044	0.0008	-0.0021	-0.0001	0.0023	0.0038	0.0165	0.0386	0.0044	-0.0362	-0.0185	-0.0593	0.0308	-0.0362	-0	0.0924	0.0199	0.0159	0.1033	0.0198	0.1519	32.9628	-18.9945	88.3174
29	0.0303	0.0105	0.0043	0.0632	-0.0161	0.0816	0.0164	-0.0279	-0.0949	0.1109	-0.0034	-0.1603	-0.0195	-0.0574	0.0006	0.0584	0.0279	-0.0237	0.0429	0.0093	0.0912	29.4676	-25.2297	99.2495
30	0.0766	-0.0081	0.056	0.0815	0.0013	0.0577	-0.0766	-0.0071	-0.0605	0.2006	0.0541	0.0765	-0.0753	-0.1802	-0.0034	0.1929	-0.0087	0.0418	0.1367	-0.0146	0.0849	15.8294	-26.0878	110.2873
31	0.0744	0.0543	-0.0845	0.04	-0.0607	0.0998	0.0736	0.0053	0.0381	0.0662	0.0654	-0.023	-0.0439	0.0184	0.0113	0.254	0.012	-0.0335	0.0597	-0.0178	0.133	33.4628	-4.9672	98.6995
32	0.0019	-0.0024	-0.0105	0.0059	0.0011	0.0149	-0.0765	0.0116	0.0471	0.0375	0.1024	0.1068	-0.1059	0.0484	-0.0004	0.0995	0.0218	0.0022	0.1074	0.0204	0.0805	17.4824	-11.8561	86.523

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 25 through 55 )	A
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 56 through 249 )	A
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 250 through 285 )	A
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 286 through 316 )	A
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 317 through 333 )	A
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 25 through 75 )	B
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 76 through 122 )	B
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 123 through 147 )	B
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 148 through 163 )	B
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 164 through 201 )	B
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 202 through 249 )	B
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 250 through 285 )	B
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 286 through 306 )	B
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 307 through 328 )	B
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 25 through 75 )	C
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 76 through 101 )	C
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 102 through 122 )	C
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 123 through 147 )	C
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 148 through 163 )	C
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 164 through 201 )	C
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 202 through 249 )	C
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 250 through 285 )	C
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 286 through 306 )	C
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 307 through 329 )	C
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 25 through 75 )	D
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 76 through 122 )	D
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 123 through 163 )	D
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 164 through 183 )	D
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 184 through 249 )	D
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 250 through 285 )	D
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 286 through 303 )	D
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 304 through 329 )	D

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