PDB-6clu: Staphylococcus aureus Dihydropteroate Synthase (saDHPS) F17L E208...

ID or keywords:

Entry

Database: PDB / ID: 6clu

Title

Staphylococcus aureus Dihydropteroate Synthase (saDHPS) F17L E208K double mutant structure

Components

Dihydropteroate synthase

Keywords

ANTIMICROBIAL PROTEIN / antibiotic resistance mutations / sulfonamide resistance

Function / homology

Function and homology information

dihydropteroate synthase /

dihydropteroate synthase activity / folic acid biosynthetic process / tetrahydrofolate biosynthetic process / response to antibiotic /

metal ion binding
Similarity search - Function

Biological species

Staphylococcus aureus (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.95 Å

Authors

Gajewski, S. / Griffith, E.C. / Wu, Y. / White, S.W.

Funding support

United States, 3items

Organization	Grant number	Country
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)	R01 AI070721-08	United States
St. Jude Children's Research Hospital (ALSAC)		United States
Department of Energy (DOE, United States)	W-31-109-Eng-38	United States

Citation

Journal: Front Microbiol / Year: 2018
Title: The Structural and Functional Basis for Recurring Sulfa Drug Resistance Mutations inStaphylococcus aureusDihydropteroate Synthase.
Authors: Griffith, E.C. / Wallace, M.J. / Wu, Y. / Kumar, G. / Gajewski, S. / Jackson, P. / Phelps, G.A. / Zheng, Z. / Rock, C.O. / Lee, R.E. / White, S.W.

History

Deposition	Mar 2, 2018	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Aug 22, 2018	Provider: repository / Type: Initial release
Revision 1.1	Feb 20, 2019	Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2	Dec 18, 2019	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3	Mar 13, 2024	Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	6clu.cif.gz	364 KB	Display	PDBx/mmCIF format
PDB format	pdb6clu.ent.gz	297.1 KB	Display	PDB format
PDBx/mmJSON format	6clu.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/cl/6clu ftp://data.pdbj.org/pub/pdb/validation_reports/cl/6clu	HTTPS FTP

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Related structure data

Related structure data	6clvC C: citing same article (ref.)
Similar structure data	2zgx-d 2yck-d 6zuu-d 6zug-d 4dlm-d 2p51-d 3oqe-d 3rq8-d 6t56-d 3rqq-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) 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

6clvC

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Dihydropteroate synthase

B: Dihydropteroate synthase

C: Dihydropteroate synthase

D: Dihydropteroate synthase

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

1

A: Dihydropteroate synthase

defined by author
Evidence: homology
32.4 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Dihydropteroate synthase

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

3

C: Dihydropteroate synthase

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

4

D: Dihydropteroate synthase

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

5

A: Dihydropteroate synthase

B: Dihydropteroate synthase

defined by software
64.8 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

6

C: Dihydropteroate synthase

D: Dihydropteroate synthase

defined by software
64.8 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	76.636, 76.636, 176.226
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	78
Space group name H-M	P4₃

#1: Protein	Dihydropteroate synthase / / DHPS / Dihydropteroate pyrophosphorylase Mass: 32406.936 Da / Num. of mol.: 4 / Mutation: F17L, E208K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: folP, dpsA / Production host: Escherichia coli (E. coli) / References: UniProt: O05701, dihydropteroate synthase
#2: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 197 / Source method: isolated from a natural source / Formula: H₂O

#1: Protein

Dihydropteroate synthase /

/ DHPS / Dihydropteroate pyrophosphorylase

Mass: 32406.936 Da / Num. of mol.: 4 / Mutation: F17L, E208K
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Staphylococcus aureus (bacteria) / Gene: folP, dpsA / Production host:

Escherichia coli (E. coli) / References: UniProt: O05701,

dihydropteroate synthase

#2: Water

ChemComp-HOH / water /

Water

Mass: 18.015 Da / Num. of mol.: 197 / 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: 2.19 Å³/Da / Density % sol: 43.81 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: 0.2M Sodium Nitrate, and 20% PEG 3350

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 0.97943 Å
Detector	Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 4, 2013
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97943 Å / Relative weight: 1
Reflection twin	Operator: h,-k,-l / Fraction: 0.32
Reflection	Resolution: 1.95→46.622 Å / Num. obs: 684630 / % possible obs: 99.9 % / Redundancy: 9.2 % / Net I/σ(I): 9.7
Reflection shell	Resolution: 1.95→1.99 Å

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
PHENIX	1.11.1_2575	refinement
XDS		data reduction
Aimless		data scaling
PHASER		phasing
PDB_EXTRACT	3.24	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.95→46.622 Å / Cross valid method: THROUGHOUT / σ(F): 48.42 / Phase error: 30.43

	R_factor	Num. reflection	% reflection
R_free	0.2036	2005	2.72 %
R_work	0.1819	-	-
obs	0.1893	73613	99.9 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å

Displacement parameters

B_iso max: 72.61 Å² / B_iso mean: 32.2363 Å² / B_iso min: 18.27 Å²

Refinement step

Cycle: final / Resolution: 1.95→46.622 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7039	0	0	197	7236
B_iso mean	-	-	-	32.33	-
Num. residues	-	-	-	-	946

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.001	7142
X-RAY DIFFRACTION	f_angle_d	0.371	9690
X-RAY DIFFRACTION	f_chiral_restr	0.04	1182
X-RAY DIFFRACTION	f_plane_restr	0.003	1245
X-RAY DIFFRACTION	f_dihedral_angle_d	13.883	4330

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 14

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.9505-1.9993	0.437	143	0.3928	5041	5184	96
1.9993-2.0533	0.3615	141	0.3257	5069	5210	97
2.0533-2.1137	0.3119	147	0.2904	5114	5261	97
2.1137-2.1818	0.2719	145	0.2689	5091	5236	97
2.1818-2.2597	0.2857	144	0.2406	5130	5274	97
2.2597-2.35	0.2537	142	0.2224	5085	5227	97
2.35-2.4568	0.2319	144	0.2162	5106	5250	97
2.4568-2.5861	0.2309	141	0.2077	5096	5237	97
2.5861-2.7478	0.2129	143	0.1959	5099	5242	97
2.7478-2.9594	0.2109	148	0.1812	5135	5283	97
2.9594-3.2561	0.1776	140	0.1642	5080	5220	97
3.2561-3.7248	0.1713	133	0.1566	5160	5293	97
3.7248-4.6834	0.1678	144	0.1408	5120	5264	97
4.6834-20.4078	0.188	150	0.1643	5156	5306	97

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	1.7233	0.8234	0.2435	1.763	0.1231	1.319	0.1634	0.3846	0.3066	0.1077	-0.1396	-0.4359	0.3176	0.4127	-0.0885	0.2632	0.053	0.0122	0.3291	0.0009	0.379	90.2239	119.4001	7.9285
2	1.1751	0.2776	0.087	0.0714	-0.1086	1.6611	-0.0608	0.0769	0.2779	-0.0605	0.0625	-0.1626	0.0799	0.0925	0.065	0.2296	0.0338	0.0484	0.3064	0.0204	0.3705	90.2005	123.4208	3.9821
3	0.2952	0.2626	-0.2652	1.0846	1.3502	4.3997	-0.4454	-0.0863	0.1356	-0.05	-0.0557	-0.4769	-0.1958	0.2932	0.0542	0.263	0.0354	0.0229	0.3824	0.0344	0.6185	92.2094	134.4413	9.396
4	1.1863	-0.1484	-0.5746	1.1557	-0.2115	1.3369	0.0671	0.0443	0.3566	-0.0462	-0.0599	-0.2095	-0.068	-0.0711	-0.0174	0.2001	0.047	0.0319	0.2486	0.0232	0.3561	80.2767	133.6721	10.448
5	1.3745	0.111	-0.3374	1.6274	-0.3796	1.5404	0.0994	0.0829	-0.086	0.0756	-0.0282	-0.0476	0.1235	-0.0139	-0.0662	0.2328	0.0288	0.0131	0.2196	-0.0062	0.2944	73.2735	123.2826	20.6815
6	1.0088	-0.6767	-0.1662	4.3755	-1.5443	1.1257	-0.098	-0.0126	0.1287	0.0302	0.2239	-0.0509	-0.1395	-0.2731	-0.0382	0.1691	0.0406	0.0113	0.3179	0.009	0.2547	66.2669	125.4631	18.5231
7	1.2551	0.3106	-0.9636	1.2559	0.3623	1.0686	-0.087	-0.0006	-0.1634	0.0659	0.0706	-0.0156	0.0852	-0.0016	0.0013	0.179	0.0156	0.0107	0.2068	-0.0134	0.2702	75.4965	113.8669	15.3862
8	1.6809	0.0071	0.0898	1.51	0.0286	0.8958	0.0354	-0.0497	-0.1325	-0.1387	-0.0065	-0.1406	0.0702	-0.0825	-0.0228	0.1984	0.0365	0.0228	0.2547	-0.0232	0.2916	79.7892	109.372	8.0123
9	3.9926	0.9064	1.5022	1.8314	0.3235	1.6108	0.1278	0.0684	-0.0722	-0.2632	-0.0158	0.1822	0.0792	-0.0709	-0.0317	0.3023	0.029	-0.0109	0.2575	0.0019	0.3045	75.6388	107.8843	-2.3288
10	1.1073	0.5001	-0.2165	0.4164	0.0781	0.1805	-0.1351	-0.0139	-0.1229	-0.0555	0.0919	-0.0201	0.1406	0.1723	0.055	0.2011	0.0258	-0.0002	0.2841	0.0052	0.3602	86.1601	83.5375	-0.5719
11	1.464	0.2997	0.3576	0.9842	-0.1608	1.1127	0.0629	0.1298	-0.0442	-0.2285	-0.0705	-0.3778	0.2212	0.0868	0.0719	0.2969	0.051	0.0629	0.2917	-0.0041	0.4231	83.1882	73.8502	-4.894
12	1.9124	-0.5808	-0.0812	1.6296	0.0132	1.1978	-0.0013	0.1562	-0.107	-0.3635	-0.1037	-0.0686	0.0931	-0.0343	0.0769	0.3105	-0.0009	0.0331	0.2983	-0.0209	0.3441	73.6314	73.038	-6.2938
13	1.7056	0.566	-0.3169	2.3814	-0.0043	1.0649	-0.159	-0.1435	0.0319	-0.0785	0.1062	-0.0474	0.0729	-0.0199	0.0819	0.1641	0.0129	-0.0108	0.224	0.0015	0.2717	64.4409	83.1234	-3.8602
14	1.4555	0.7698	0.8996	1.4791	0.7909	0.8034	0.176	0.1217	0.0196	-0.061	-0.1304	0.1407	-0.1485	-0.1604	-0.0212	0.1994	0.0162	-0.0152	0.2477	-0.0132	0.2689	72.8556	93.2488	0.943
15	1.4642	-1.2738	-1.7206	1.2842	1.6727	2.6576	0.0054	0.0038	-0.3977	0.085	-0.1538	0.1444	-0.06	0.0042	0.0788	0.215	0.0004	-0.0242	0.2491	0.0097	0.3122	76.1884	98.8334	11.8471
16	1.3329	-0.3828	0.2396	2.215	-0.9458	1.3365	0.0766	-0.1135	-0.2026	0.3635	0.0016	0.1223	-0.0074	0.0363	0.0172	0.3201	-0.0622	0.0193	0.1876	0.0195	0.3809	99.0521	111.4116	-25.9188
17	0.6436	0.1193	0.2263	1.2512	0.0869	0.9718	-0.0888	-0.1269	-0.4095	-0.0652	-0.1498	-0.0511	0.0102	0.0426	0.0494	0.3524	-0.0104	0.0233	0.2124	0.0592	0.4956	101.8841	105.1905	-24.4436
18	1.354	0.9404	1.37	1.3943	1.5323	2.8722	0.1621	-0.2833	-0.2112	0.3604	-0.1436	-0.0197	0.301	-0.0215	-0.0058	0.4154	0.0354	-0.0188	0.2756	0.0853	0.5142	113.6606	107.3938	-16.8527
19	1.8681	0.1067	-0.0226	2.497	0.7343	1.5521	-0.2429	-0.0189	-0.244	0.0926	0.1659	0.1427	-0.0236	0.3518	0.1324	0.2911	-0.0119	0.0091	0.2065	0.0817	0.354	112.2672	113.1693	-23.0211
20	0.6857	0.0112	-0.4273	1.6734	0.4231	1.4438	-0.0213	-0.0479	-0.2556	0.1049	0.0532	-0.2871	0.0511	0.0476	-0.0194	0.2949	-0.0443	-0.0183	0.1789	0.036	0.3544	112.8786	122.5908	-21.3512
21	1.4861	-0.6547	0.144	1.8771	0.1629	0.497	0.1655	-0.0412	0.0312	-0.1273	0.0119	0.0373	-0.0423	-0.0866	-0.0639	0.2644	-0.044	-0.0601	0.1942	0.0544	0.289	104.2176	126.4927	-21.7599
22	4.1534	-0.7035	-0.9626	1.2793	0.0252	0.7745	0.0933	-0.329	0.0442	0.1335	-0.0417	-0.1561	-0.1008	0.1996	-0.0455	0.3311	-0.0539	-0.0386	0.1587	0.022	0.2416	104.7312	134.5206	-23.1009
23	1.3685	0.0777	-0.1429	1.3988	0.1071	0.7986	-0.1777	-0.214	-0.3892	-0.001	-0.1932	-0.0409	-0.0501	0.1875	0.0654	0.3243	-0.0334	-0.043	0.1877	0.0252	0.2646	101.605	125.9535	-23.9409
24	1.3424	0.4492	-0.7386	1.1213	-0.0672	2.1067	0.1248	0.0423	0.0028	0.0946	-0.0676	0.2443	-0.1814	-0.3865	0.0175	0.3014	-0.0585	0.0114	0.2508	-0.0073	0.3346	90.438	131.8482	-22.496
25	1.4993	0.1973	-0.0954	0.6495	0.0129	0.7748	0.2585	-0.2394	-0.008	0.4335	-0.2164	0.2517	-0.0922	0.0026	-0.0041	0.3547	-0.0665	0.036	0.2608	0.0122	0.3583	91.0858	121.4011	-21.3572
26	1.4889	0.0911	0.1021	2.219	-0.1677	0.7535	-0.0679	-0.0561	-0.1867	0.3052	0.0428	0.0067	-0.0649	-0.0654	0.0654	0.3058	-0.0414	0.0175	0.2159	0.0031	0.2994	88.352	117.2691	-24.9778
27	1.8542	-0.7221	0.8511	1.9569	-1.0777	3.2708	-0.1163	0.2836	-0.0534	-0.0833	-0.0274	-0.4867	-0.0382	-0.3021	0.0607	0.2192	-0.027	0.0086	0.253	-0.026	0.3671	87.1117	116.337	-37.2421
28	0.8577	0.3283	0.2668	1.2526	-0.1502	0.5797	-0.0337	0.0782	-0.4252	0.2383	0.0333	0.2712	0.3387	-0.0661	-0.0314	0.3427	-0.0291	0.0613	0.2015	-0.0023	0.5306	65.2755	104.7935	-32.8086
29	2.7251	1.9486	0.2411	2.6994	0.3959	0.9955	-0.15	-0.2871	-0.2651	0.4679	-0.1386	-0.0251	0.4305	0.0308	0.0816	0.5264	-0.025	0.1455	0.2653	0.0723	0.5033	62.9129	103.0712	-23.2674
30	1.3639	0.7052	-0.13	0.6382	0.3821	0.7496	-0.1075	-0.0904	-0.7813	0.2312	-0.0135	0.5165	0.3194	-0.0629	0.1297	0.3476	-0.0598	0.166	0.2793	0.0379	0.7257	54.8989	105.406	-32.7593
31	1.5987	-0.1557	0.5753	1.1693	-0.2605	2.2716	-0.0856	-0.2214	0.0173	0.238	-0.0613	0.556	0.0287	-0.3029	-0.0056	0.3142	-0.0501	0.155	0.2017	-0.0062	0.7282	52.1815	111.1271	-32.8624
32	1.5667	-0.5219	-0.6396	1.5508	0.1026	1.1341	0.0623	0.1279	-0.1879	0.0739	-0.0262	0.591	0.0621	-0.1098	0.0062	0.2373	-0.0139	0.0276	0.2737	-0.0388	0.501	56.0092	117.7555	-43.9315
33	1.1936	-0.4305	-0.2711	1.1209	-0.2202	0.5112	0.1688	0.0093	-0.1239	0.0636	-0.115	0.3702	-0.0995	-0.0963	-0.063	0.2557	-0.0196	0.0298	0.2324	-0.0371	0.3699	61.6836	123.6526	-44.8076
34	1.0675	-1.1535	-0.814	2.6824	1.3463	1.7098	-0.0073	-0.0658	-0.0532	-0.0419	-0.0533	0.06	-0.1247	0.1594	0.0397	0.2354	-0.0041	0.0131	0.2542	0.0007	0.2872	74.6589	122.9604	-45.7013
35	1.5912	-1.3332	0.1688	2.3635	-0.0914	0.7716	0.0252	-0.1693	0.0714	-0.0184	0.1334	-0.1284	0.078	-0.0775	-0.1813	0.2173	-0.0282	0.024	0.1828	-0.0029	0.3828	68.9686	118.1404	-37.9509
36	0.9121	-0.4664	-0.587	3.0925	-0.8787	0.8918	0.0579	0.1574	-0.2787	-0.5151	-0.0838	-0.7861	0.3391	0.0717	-0.054	0.3825	0.0134	0.0529	0.2824	-0.0457	0.4466	82.0505	106.8204	-42.6287
37	1.4803	0.2858	-0.0204	1.8355	0.0555	1.323	-0.0757	-0.126	-0.0886	-0.0889	0.0735	0.0532	0.022	0.0357	-0.0211	0.2434	-0.024	0.0168	0.216	-0.0067	0.2988	75.9232	114.5755	-34.0822
38	1.5157	1.4753	0.4522	4.5867	0.9984	0.7086	0.0767	-0.1542	0.2147	0.3849	0.0179	0.2032	-0.0661	0.0736	-0.1121	0.294	-0.0454	0.0519	0.2149	-0.0085	0.3029	77.7453	122.6389	-23.9845

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 2 through 25 )	A	2 - 25
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 26 through 59 )	A	26 - 59
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 60 through 74 )	A	60 - 74
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 75 through 121 )	A	75 - 121
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 122 through 138 )	A	122 - 138
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 139 through 157 )	A	139 - 157
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 158 through 216 )	A	158 - 216
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 217 through 242 )	A	217 - 242
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 243 through 260 )	A	243 - 260
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 2 through 59 )	B	2 - 59
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 60 through 87 )	B	60 - 87
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 88 through 111 )	B	88 - 111
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 112 through 190 )	B	112 - 190
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 191 through 242 )	B	191 - 242
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 243 through 264 )	B	243 - 264
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 2 through 25 )	C	2 - 25
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 26 through 59 )	C	26 - 59
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 60 through 74 )	C	60 - 74
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 75 through 97 )	C	75 - 97
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 98 through 121 )	C	98 - 121
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 122 through 138 )	C	122 - 138
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 139 through 157 )	C	139 - 157
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 158 through 175 )	C	158 - 175
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 176 through 192 )	C	176 - 192
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 193 through 215 )	C	193 - 215
26	X-RAY DIFFRACTION	26	chain 'C' and (resid 216 through 242 )	C	216 - 242
27	X-RAY DIFFRACTION	27	chain 'C' and (resid 243 through 262 )	C	243 - 262
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 2 through 25 )	D	2 - 25
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 26 through 39 )	D	26 - 39
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 40 through 74 )	D	40 - 74
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 75 through 97 )	D	75 - 97
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 98 through 138 )	D	98 - 138
33	X-RAY DIFFRACTION	33	chain 'D' and (resid 139 through 175 )	D	139 - 175
34	X-RAY DIFFRACTION	34	chain 'D' and (resid 176 through 192 )	D	176 - 192
35	X-RAY DIFFRACTION	35	chain 'D' and (resid 193 through 203 )	D	193 - 203
36	X-RAY DIFFRACTION	36	chain 'D' and (resid 204 through 215 )	D	204 - 215
37	X-RAY DIFFRACTION	37	chain 'D' and (resid 216 through 242 )	D	216 - 242
38	X-RAY DIFFRACTION	38	chain 'D' and (resid 243 through 263 )	D	243 - 263

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