PDB-6ok0: Crystal structure of Sel1 repeat protein from Oxalobacter formigenes

ID or keywords:

Entry

Database: PDB / ID: 6ok0

Title

Crystal structure of Sel1 repeat protein from Oxalobacter formigenes

Components

(Sel1 repeat protein) x 4

Keywords

HYDROLASE / Sel1 repeat / Structural Genomics / PSI-Biology / Midwest Center for Structural Genomics / MCSG

Function / homology

Function and homology information

beta-lactamase activity / beta-lactamase
Similarity search - Function

Biological species

Oxalobacter formigenes OXCC13 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

SAD / Resolution: 2.174 Å

Authors

Chang, C. / Tesar, C. / Endres, M. / Babnigg, G. / Hassan, H. / Joachimiak, A. / Midwest Center for Structural Genomics (MCSG)

Citation

Journal: To Be Published
Title: Crystal structure of Sel1 repeat protein from Oxalobacter formigenes
Authors: Chang, C. / Tesar, C. / Endres, M. / Babnigg, G. / Hassan, H. / Joachimiak, A. / Midwest Center for Structural Genomics (MCSG)

History

Deposition	Apr 12, 2019	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 15, 2020	Provider: repository / Type: Initial release
Revision 1.1	Apr 2, 2025	Group: Data collection / Database references / Structure summary Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	6ok0.cif.gz	221.6 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	6ok0_validation.pdf.gz	482.5 KB	Display	wwPDB validaton report
Full document	6ok0_full_validation.pdf.gz	485.2 KB	Display
Data in XML	6ok0_validation.xml.gz	23.2 KB	Display
Data in CIF	6ok0_validation.cif.gz	32 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ok/6ok0 ftp://data.pdbj.org/pub/pdb/validation_reports/ok/6ok0	HTTPS FTP

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Related structure data

Related structure data	6ok3C 6onwC 6orcC 6orkC 6ur7C C: citing same article (ref.)
Similar structure data	1c89-d 3uv4-1 5fej-1 5fej-3 5ffd-d 6mj9-d 5fej-4 6q5r-3 4qey-6 2xlm-d 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

Related structure data

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#134 - Feb 2011 Integrin similarity (1) #172 - Apr 2014 RecA and Rad51 similarity (1) #194 - Feb 2016 Designer Insulins similarity (1) #234 - Jun 2019 MDM2 and Cancer similarity (1) #259 - Jul 2021 Designed Proteins and Citizen Science similarity (1)

Deposited unit

A: Sel1 repeat protein

B: Sel1 repeat protein

C: Sel1 repeat protein

D: Sel1 repeat protein

hetero molecules

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

1

A: Sel1 repeat protein

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

2

B: Sel1 repeat protein

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

3

C: Sel1 repeat protein

hetero molecules

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

4

D: Sel1 repeat protein

hetero molecules

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

Unit cell

Length a, b, c (Å)	42.768, 68.587, 74.365
Angle α, β, γ (deg.)	68.540, 79.250, 89.970
Int Tables number	1
Space group name H-M	P1

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Protein , 4 types, 4 molecules ABCD

#1: Protein	Sel1 repeat protein Mass: 16021.429 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oxalobacter formigenes OXCC13 (bacteria) Gene: OFBG_00636 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: C3X8T2, beta-lactamase
#2: Protein	Sel1 repeat protein Mass: 15981.360 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oxalobacter formigenes OXCC13 (bacteria) Gene: OFBG_00636 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: C3X8T2, beta-lactamase
#3: Protein	Sel1 repeat protein Mass: 16020.419 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oxalobacter formigenes OXCC13 (bacteria) Gene: OFBG_00636 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: C3X8T2, beta-lactamase
#4: Protein	Sel1 repeat protein Mass: 15994.380 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oxalobacter formigenes OXCC13 (bacteria) Gene: OFBG_00636 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: C3X8T2, beta-lactamase

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Non-polymers , 4 types, 242 molecules

#5: Chemical	ChemComp-PGE / TRIETHYLENE GLYCOL Mass: 150.173 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C₆H₁₄O₄
#6: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#7: Chemical	ChemComp-IMD / IMIDAZOLE Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₃H₅N₂
#8: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 239 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has protein modification	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: 3.16 Å³/Da / Density % sol: 61.07 %
Crystal grow	Temperature: 289 K / Method: vapor diffusion, sitting drop Details: 0.2M magnesium chloride, 0.1M This-HCl, 20% PEG8000

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 19-ID / Wavelength: 0.97924 Å

Detector

Type: DECTRIS PILATUS3 X 6M / Detector: PIXEL / Date: Mar 28, 2017

Radiation

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

Radiation wavelength

Wavelength: 0.97924 Å / Relative weight: 1

Reflection

Resolution: 2.17→50 Å / Num. obs: 37770 / % possible obs: 93.3 % / Redundancy: 5.3 % / R_merge(I) obs: 0.138 / R_pim(I) all: 0.061 / R_rim(I) all: 0.151 / Χ²: 0.825 / Net I/σ(I): 7.2 / Num. measured all: 200503

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Χ²	% possible all
2.17-2.21	3.1	0.553	1575	0.792	0.303	0.636	0.856	78.6
2.21-2.25	3.6	0.505	1742	0.885	0.254	0.568	0.93	84.3
2.25-2.29	3.9	0.446	1722	0.893	0.217	0.499	0.917	87.6
2.29-2.34	4	0.433	1857	0.914	0.207	0.482	0.929	91.3
2.34-2.39	4.3	0.418	1900	0.924	0.195	0.463	0.895	92
2.39-2.44	4.5	0.42	1883	0.932	0.194	0.465	0.87	93.4
2.44-2.51	4.6	0.375	1883	0.932	0.174	0.415	0.87	92.9
2.51-2.57	4.5	0.362	1854	0.926	0.17	0.402	0.891	93.7
2.57-2.65	5.4	0.336	1996	0.945	0.149	0.369	0.868	96.7
2.65-2.73	5.7	0.297	1946	0.958	0.13	0.325	0.873	96.8
2.73-2.83	5.9	0.24	1949	0.971	0.104	0.262	0.928	96.1
2.83-2.95	6	0.215	1945	0.97	0.093	0.235	0.893	96.2
2.95-3.08	5.9	0.184	1937	0.98	0.08	0.201	0.866	95
3.08-3.24	6.1	0.16	1945	0.974	0.069	0.175	0.887	95.6
3.24-3.44	6.4	0.129	1925	0.985	0.055	0.14	0.844	96.7
3.44-3.71	6.3	0.107	1962	0.988	0.045	0.117	0.827	96.7
3.71-4.08	6.1	0.091	1919	0.989	0.038	0.099	0.731	94.3
4.08-4.67	6.4	0.084	1962	0.988	0.036	0.092	0.673	96.6
4.67-5.89	6.3	0.081	1917	0.986	0.034	0.088	0.602	95.6
5.89-50	6.2	0.084	1951	0.984	0.036	0.092	0.626	95.8

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Processing

Software

Name	Version	Classification
PHENIX	1.14_3260	refinement
HKL-3000		data reduction
HKL-3000		data scaling
PDB_EXTRACT	3.25	data extraction
HKL-3000		phasing

Refinement

Method to determine structure:

SAD / Resolution: 2.174→39.629 Å / SU ML: 0.25 / Cross valid method: THROUGHOUT / σ(F): 1.98 / Phase error: 24.39 / Stereochemistry target values: MLHL

	R_factor	Num. reflection	% reflection
R_free	0.2153	1690	4.84 %
R_work	0.1886	56503	-
obs	0.1899	35290	73.22 %

Solvent computation

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

Displacement parameters

B_iso max: 107.11 Å² / B_iso mean: 36.3395 Å² / B_iso min: 7.81 Å²

Refinement step

Cycle: final / Resolution: 2.174→39.629 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	3927	0	16	239	4182
B_iso mean	-	-	72.41	37.98	-
Num. residues	-	-	-	-	525

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 21

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.174-2.2096	0.2776	57	0.2313	1254	1311	34
2.2096-2.2477	0.2369	55	0.2181	1608	1663	42
2.2477-2.2886	0.2483	89	0.2099	1615	1704	45
2.2886-2.3326	0.24	79	0.2203	1815	1894	50
2.3326-2.3802	0.2336	98	0.2146	2045	2143	54
2.3802-2.432	0.2898	103	0.2282	2087	2190	57
2.432-2.4885	0.26	130	0.2253	2228	2358	61
2.4885-2.5508	0.2106	113	0.2231	2337	2450	63
2.5508-2.6197	0.2605	128	0.2265	2665	2793	73
2.6197-2.6968	0.2335	147	0.2131	2834	2981	77
2.6968-2.7838	0.2382	159	0.2168	2884	3043	80
2.7838-2.8833	0.2619	144	0.2062	3172	3316	84
2.8833-2.9987	0.2354	179	0.2171	3007	3186	84
2.9987-3.1351	0.2206	153	0.2081	3092	3245	84
3.1351-3.3003	0.2298	182	0.2131	3364	3546	92
3.3003-3.507	0.1994	140	0.185	3477	3617	94
3.507-3.7775	0.2381	163	0.1674	3459	3622	94
3.7775-4.1573	0.2062	185	0.1564	3296	3481	91
4.1573-4.758	0.151	207	0.1491	3488	3695	95
4.758-5.9913	0.2027	183	0.1755	3367	3550	92
5.9913-39.6358	0.2098	177	0.1845	3409	3586	93

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	0.0247	-0.0035	-0.0268	0.0278	0.0146	0.0314	0.0041	0.1252	-0.1366	0.2012	-0.0135	-0.0993	0.0677	-0.158	0	0.169	0.0527	0.0291	0.2259	-0.0394	0.441	37.2378	40.0473	2.6885
2	0.4039	-0.0481	0.0542	0.2054	-0.004	0.0393	-0.0167	0.2016	-0.7429	-0.0955	0.292	-0.0363	0.0459	-0.0434	0.0327	0.2795	-0.0204	-0.0127	0.146	-0.0216	0.3563	28.3689	37.7969	4.9756
3	0.1692	0.0944	-0.0116	0.1396	-0.1174	0.105	0.1528	0.0984	-0.4031	0.2683	-0.1297	0.0321	0.1424	0.1928	-0.0027	0.1683	0.0139	-0.013	0.1375	-0.0029	0.2621	27.9439	48.0098	9.6446
4	0.0387	-0.0028	0.0705	0.2306	-0.0839	0.1211	-0.1031	0.0066	-0.372	0.0135	0.1393	0.099	0.0406	0.011	-0.0016	0.1033	0.0218	-0.0089	0.159	0.0261	0.2092	27.8041	57.9936	7.8179
5	0.0378	-0.0146	-0.0749	0.1366	-0.0508	0.1531	-0.0132	0.2828	-0.0381	-0.0702	0.014	-0.1621	0.0274	0.0999	-0.0005	0.0802	-0.0177	-0.0174	0.1529	0.0247	0.1303	34.6185	65.26	3.9741
6	0.6084	0.0371	-0.1529	0.0369	-0.0827	0.2901	0.1088	-0.2989	0.018	0.1243	-0.0893	-0.3277	-0.0921	0.0163	-0.0398	0.0482	-0.0019	0.0067	0.1416	-0.0137	0.2554	38.6191	68.7356	6.7718
7	0.0722	0.0321	0.0565	0.0115	0.0219	0.0457	0.1438	0.3513	-0.0645	0.0102	0.2414	-0.0898	-0.1267	0.0589	0.0011	0.4287	-0.0022	0.0967	0.3934	-0.0281	0.2548	13.1516	65.0606	-22.1011
8	0.1873	-0.1187	0.087	0.3884	0.0645	0.0874	-0.3367	-0.1489	0.0018	0.0758	0.2345	-0.2983	0.1076	0.1787	-0.1264	0.7076	0.4004	-0.0231	0.4681	-0.3247	0.3328	18.5261	55.3699	-16.2284
9	0.3882	-0.1501	0.1927	0.6554	-0.2936	0.1934	-0.1256	0.1728	-0.0459	0.2391	-0.0478	-0.0329	0.0931	-0.4507	-0.0919	0.4014	0.0213	0.0371	0.3262	-0.1249	0.2087	9.672	60.7818	-16.6136
10	0.0588	0.0885	0.0571	0.195	0.1295	0.0679	0.0724	0.0336	-0.3553	0.0477	-0.0927	-0.0371	0.2738	-0.1193	-0.0211	0.4033	0.0025	0.0191	0.2359	-0.1362	0.2158	5.5616	57.6169	-13.5578
11	0.4455	-0.1039	0.0058	0.0531	-0.0244	0.0299	0.1478	0.347	0.0864	-0.0062	-0.0321	-0.1305	0.1481	-0.004	0.0002	0.2532	-0.0258	0.0102	0.2268	-0.031	0.1201	8.9663	69.3793	-9.3639
12	0.1499	-0.0897	-0.0862	0.0561	0.0345	0.1091	-0.106	0.5782	-0.4023	-0.247	0.1645	0.6055	0.2452	-0.2635	-0.0044	0.2438	-0.0503	-0.023	0.3684	-0.019	0.1956	-3.9321	66.7753	-9.4544
13	0.0103	0.0908	0.0594	0.9019	0.4298	0.2233	-0.2366	0.0136	0.0236	-0.1995	0.3362	-0.1044	0.0995	-0.0418	0.4237	0.1989	0.0066	-0.0062	0.261	0.011	0.0858	4.779	75.0767	-5.2879
14	0.0364	-0.0851	-0.0517	0.4334	0.1277	0.0835	-0.2037	0.4007	0.1177	-0.0602	-0.0167	0.6701	-0.0153	-0.2725	-0.0229	0.3278	-0.0519	-0.0529	0.287	0.049	0.3425	-1.905	82.3819	-7.8375
15	0.9587	-0.3839	-0.6213	0.2502	0.4497	0.8785	0.009	0.0007	0.4859	-0.4657	0.0365	-0.4097	-0.6186	0.4438	0.0221	0.39	0.0128	0.0062	0.2266	0.0915	0.2047	4.5515	88.6337	-9.9033
16	0.0398	0.0308	0.0113	0.016	-0.0082	0.011	-0.0143	-0.4217	0.0458	-0.0514	-0.0619	-0.0473	-0.1013	-0.0507	0.0001	0.182	-0.048	-0.0088	0.216	-0.0173	0.3864	15.534	101.458	12.1495
17	0.9329	0.2022	0.0979	0.1903	0.1469	0.1311	-0.0878	0.2209	0.6881	-0.3467	0.1881	0.07	0.0551	0.0314	0.0052	0.2627	-0.0008	-0.025	0.053	-0.0251	0.6561	9.0327	109.1833	4.7231
18	0.1656	-0.0609	-0.0586	0.0774	0.0006	0.0665	-0.1459	-0.2029	0.3388	0.086	0.2621	0.0229	-0.2008	0.08	-0.0006	0.2569	0.0204	0.0063	0.1602	-0.0439	0.334	6.2623	101.1813	12.8101
19	0.1954	-0.1988	0.0478	0.1949	-0.097	0.9324	0.1927	0.0368	0.4485	-0.1358	-0.0548	0.0927	-0.0942	0.3218	0.0542	0.1226	-0.002	-0.0076	0.0891	0.0201	0.2781	6.5886	93.857	5.6112
20	0.1985	0.1304	0.0337	0.3568	0.0678	0.0156	0.0046	-0.085	0.3998	0.439	-0.0584	0.7442	0.1782	0.0608	-0.0079	0.2035	0.0097	0.0344	0.1924	0.0418	0.2179	1.3282	85.5935	13.3644
21	0.2044	-0.1105	0.2714	0.1281	-0.1317	0.3835	0.034	0.0513	-0.0413	-0.1257	-0.0779	-0.1075	-0.0082	0.0303	-0.0008	0.0697	0.0089	0.0001	0.141	0.0273	0.1875	13.8695	77.3576	7.5827
22	0.0186	0.0157	0.0082	0.2739	0.1568	0.085	-0.0234	-0.7067	0.1701	0.1624	0.4172	-0.353	0.3593	0.3235	0.0023	0.5946	0.059	-0.0803	0.6135	-0.1032	0.3083	33.4199	76.4122	37.4736
23	0.0501	-0.0542	-0.0727	0.0927	0.0699	0.1181	-0.1307	-0.0653	0.126	-0.0513	0.2102	-0.2639	-0.1273	0.4921	-0.0154	0.3189	-0.291	0.0424	0.5887	-0.3618	0.5476	39.8386	86.3572	32.0095
24	0.5254	-0.1012	-0.3043	0.3365	0.2236	0.2577	0.0481	-0.1614	0.1109	-0.2959	0.197	-0.264	-0.2084	0.3093	0.512	0.3774	-0.0636	0.0488	0.3539	-0.1669	0.1287	31.0451	80.9977	31.9156
25	0.1306	0.0823	0.0941	0.0495	0.0737	0.054	0.1253	0.0402	0.4936	-0.0178	0.0919	-0.35	-0.4142	0.0304	-0.0004	0.4505	-0.0053	0.0545	0.2895	-0.0853	0.2664	27.9654	83.4201	27.8268
26	0.0382	0.0067	-0.0049	0.0322	0.0016	0.0123	0.0822	-0.2486	0.1382	0.1386	0.019	-0.3	0.0611	0.0196	-0	0.3124	0.0097	-0.0074	0.2811	-0.0063	0.1743	29.289	71.632	25.6651
27	0.03	-0.0384	0.0154	0.0306	-0.011	0.0065	-0.254	-0.4928	0.0458	-0.0961	0.3347	0.5321	-0.3544	-0.1251	0.0001	0.2778	0.0477	-0.024	0.3014	0.0318	0.2528	17.4391	75.0695	24.6776
28	0.4634	-0.1427	-0.3073	1.7285	0.6772	0.4116	-0.3218	-0.1059	-0.1041	0.2769	0.3994	-0.268	-0.2636	-0.0037	0.3962	0.226	-0.0583	0.0104	0.2492	0.0281	0.0529	26.1353	66.762	20.5122
29	0.2138	-0.3078	0.0042	1.7108	0.4537	0.2021	-0.1976	-0.0533	-0.2313	0.1469	-0.1192	0.7592	0.2635	-0.3029	-0.0634	0.3134	0.0113	0.0314	0.3001	0.0082	0.2317	18.9828	59.4332	23.1927
30	0.8214	-0.0653	0.0625	0.0415	0.101	0.4148	0.0206	0.0702	-0.3882	0.4707	0.1028	0.0483	0.5056	-0.0576	-0.0151	0.4186	-0.0173	0.0068	0.2013	0.0528	0.1759	26.1814	53.4916	25.2263

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 9 through 20 )	A	9 - 20
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 21 through 52 )	A	21 - 52
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 53 through 77 )	A	53 - 77
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 78 through 104 )	A	78 - 104
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 105 through 117 )	A	105 - 117
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 118 through 139 )	A	118 - 139
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 9 through 20 )	B	9 - 20
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 21 through 32 )	B	21 - 32
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 33 through 45 )	B	33 - 45
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 46 through 64 )	B	46 - 64
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 65 through 77 )	B	65 - 77
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 78 through 88 )	B	78 - 88
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 89 through 104 )	B	89 - 104
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 105 through 124 )	B	105 - 124
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 125 through 139 )	B	125 - 139
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 9 through 20 )	C	9 - 20
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 21 through 32 )	C	21 - 32
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 33 through 52 )	C	33 - 52
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 53 through 77 )	C	53 - 77
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 78 through 88 )	C	78 - 88
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 89 through 139 )	C	89 - 139
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 8 through 20 )	D	8 - 20
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 21 through 32 )	D	21 - 32
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 33 through 45 )	D	33 - 45
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 46 through 66 )	D	46 - 66
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 67 through 77 )	D	67 - 77
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 78 through 88 )	D	78 - 88
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 89 through 104 )	D	89 - 104
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 105 through 124 )	D	105 - 124
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 125 through 139 )	D	125 - 139

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