PDB-6eby: Crystal structure of the MbtH-like protein FscK bound to the inte...

ID or keywords:

Entry

Database: PDB / ID: 6eby

Title

Crystal structure of the MbtH-like protein FscK bound to the interface forming region of FscH adenylation domain from Thermobifida fusca

Components

Amino acid adenylation
Conserved protein MbtH

Keywords

PROTEIN BINDING / MbtH-like protein / adenylation domain / domain activation

Function / homology

Function and homology information

amide biosynthetic process / small molecule metabolic process / : / lipid biosynthetic process / phosphopantetheine binding / catalytic activity
Similarity search - Function

Biological species

Thermobifida fusca (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.85 Å

Authors

Bruner, S.D. / Zagulyaeva, A.A.

Citation

Journal: To Be Published
Title: Comprehensive analysis of protein-protein interactions between MbtH-like protein FscK and adenylation domains in nonribosomal biosynthesis of Fuscachelins.
Authors: Bruner, S.D. / Zagulyaeva, A.A.

History

Deposition	Aug 7, 2018	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Aug 21, 2019	Provider: repository / Type: Initial release
Revision 1.1	Jan 29, 2020	Group: Derived calculations Category: pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop Item: _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_assembly_gen.asym_id_list
Revision 1.2	Oct 11, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	6eby.cif.gz	122.8 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	6eby_validation.pdf.gz	434.9 KB	Display	wwPDB validaton report
Full document	6eby_full_validation.pdf.gz	435.2 KB	Display
Data in XML	6eby_validation.xml.gz	13.3 KB	Display
Data in CIF	6eby_validation.cif.gz	18.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/eb/6eby ftp://data.pdbj.org/pub/pdb/validation_reports/eb/6eby	HTTPS FTP

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Related structure data

Related structure data	6ea3SC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	1b2o-d 1zmi-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) 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	#78 - Jun 2006 Luciferase similarity (4) #90 - Jun 2007 Fatty Acid Synthase similarity (6) #153 - Sep 2012 Pyruvate Dehydrogenase Complex similarity (1) #154 - Oct 2012 Citric Acid Cycle similarity (1)

Deposited unit

A: Conserved protein MbtH

B: Amino acid adenylation

C: Conserved protein MbtH

D: Amino acid adenylation

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

1

A: Conserved protein MbtH

B: Amino acid adenylation

defined by author&software
Evidence: isothermal titration calorimetry
17.4 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Conserved protein MbtH

D: Amino acid adenylation

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

Unit cell

Length a, b, c (Å)	43.450, 58.290, 58.700
Angle α, β, γ (deg.)	90.000, 107.210, 90.000
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Conserved protein MbtH Mass: 9094.947 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermobifida fusca (strain YX) (bacteria) Strain: YX / Gene: Tfu_1863 / Plasmid: pET30a / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q47NS3
#2: Protein	Amino acid adenylation Mass: 8291.432 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermobifida fusca (strain YX) (bacteria) Strain: YX / Gene: Tfu_1866 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q47NS0
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 195 / 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: 2.04 Å³/Da / Density % sol: 39.77 %
Crystal grow	Temperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: PEG 3350, sodium chloride, BisTris

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 21-ID-G / Wavelength: 0.9786 Å

Detector

Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 16, 2015

Radiation

Monochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.9786 Å / Relative weight: 1

Reflection

Resolution: 1.85→58.29 Å / Num. obs: 23530 / % possible obs: 98.1 % / Redundancy: 7.7 % / B_iso Wilson estimate: 16.89 Å² / CC_1/2: 0.997 / R_merge(I) obs: 0.072 / R_pim(I) all: 0.028 / R_rim(I) all: 0.077 / Net I/σ(I): 17.9 / Num. measured all: 180172 / Scaling rejects: 249

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	% possible all
1.85-1.89	7.7	0.226	1463	0.98	0.087	0.242	96.9
9.06-58.29	6.4	0.053	223	0.995	0.022	0.057	98.3

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Processing

Software

Name	Version	Classification
PHENIX	1.11.1_2575	refinement
MOSFLM		data reduction
SCALA		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 6EA3

6ea3

Resolution: 1.85→29.452 Å / SU ML: 0.21 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 22.73

	R_factor	Num. reflection	% reflection
R_free	0.2346	3909	8.49 %
R_work	0.2003	-	-
obs	0.2031	46031	97.93 %

Solvent computation

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

Displacement parameters

B_iso max: 78.4 Å² / B_iso mean: 21.0742 Å² / B_iso min: 4.29 Å²

Refinement step

Cycle: final / Resolution: 1.85→29.452 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	2054	0	0	195	2249
B_iso mean	-	-	-	26.5	-
Num. residues	-	-	-	-	262

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.002	2110
X-RAY DIFFRACTION	f_angle_d	0.58	2880
X-RAY DIFFRACTION	f_chiral_restr	0.043	304
X-RAY DIFFRACTION	f_plane_restr	0.004	384
X-RAY DIFFRACTION	f_dihedral_angle_d	17.745	756

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 28

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.85-1.8726	0.2454	151	0.2269	1530	1681	96
1.8726-1.8963	0.2621	152	0.2141	1431	1583	97
1.8963-1.9212	0.2247	158	0.2124	1472	1630	97
1.9212-1.9475	0.281	123	0.2161	1501	1624	97
1.9475-1.9754	0.2592	112	0.2065	1603	1715	97
1.9754-2.0048	0.2426	149	0.1992	1395	1544	97
2.0048-2.0362	0.2136	119	0.2016	1504	1623	98
2.0362-2.0695	0.2339	166	0.2033	1562	1728	97
2.0695-2.1052	0.2397	143	0.1966	1425	1568	98
2.1052-2.1435	0.2707	131	0.1954	1480	1611	97
2.1435-2.1847	0.2247	131	0.1963	1570	1701	98
2.1847-2.2293	0.2931	140	0.2012	1456	1596	97
2.2293-2.2777	0.2091	135	0.1938	1535	1670	98
2.2777-2.3307	0.2211	136	0.2007	1472	1608	98
2.3307-2.3889	0.2707	120	0.2013	1489	1609	98
2.3889-2.4535	0.2787	171	0.2218	1512	1683	98
2.4535-2.5257	0.2237	125	0.2061	1514	1639	98
2.5257-2.6071	0.2319	156	0.2088	1477	1633	98
2.6071-2.7003	0.2758	143	0.2148	1538	1681	98
2.7003-2.8083	0.2391	136	0.2001	1537	1673	98
2.8083-2.936	0.2358	138	0.2145	1486	1624	99
2.936-3.0906	0.2321	135	0.2076	1540	1675	99
3.0906-3.284	0.1992	132	0.2085	1501	1633	99
3.284-3.5372	0.237	147	0.1961	1495	1642	99
3.5372-3.8925	0.2324	139	0.1894	1544	1683	99
3.8925-4.454	0.1792	132	0.1677	1517	1649	99
4.454-5.6053	0.201	147	0.1836	1520	1667	99
5.6053-29.4559	0.2813	142	0.2199	1516	1658	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	0.0161	-0.0322	0.0262	0.0937	-0.1216	0.1316	-0.0367	0.1815	0.1339	-0.1349	0.1042	0.2535	-0.1344	-0.1316	0.0382	0.1023	-0.0448	-0.0122	0.1487	-0.0135	0.1363	-68.2119	44.0497	78.452
2	0.1025	-0.0047	0.0702	0.1116	0.1619	0.2397	0.1096	-0.2204	-0.1671	0.0529	0.0137	-0.0833	0.2754	-0.3012	0.0374	0.1241	-0.0399	-0.0275	0.1381	0.034	0.1156	-67.968	42.6006	87.8148
3	0.0993	0.0401	-0.2033	0.0531	-0.1781	0.6323	0.0225	-0.1505	0.1145	0.4587	0.3003	-0.412	-0.2519	-0.0196	0.0436	0.1378	0.0002	-0.0601	0.1127	-0.0581	0.198	-55.1515	51.5627	95.3633
4	0.0009	-0.0063	0.0357	0.0136	-0.0512	0.2841	-0.0223	-0.3869	-0.302	-0.0861	0.0883	-0.0784	-0.0936	-0.3212	0.0248	0.067	-0.0094	-0.005	0.1165	0.0009	0.082	-62.9802	45.5106	88.0814
5	0.213	0.2938	0.1541	0.7216	0.6576	0.8864	0.1525	-0.2122	-0.5888	0.0416	0.2634	-0.1638	0.2102	0.166	0.1043	0.1678	-0.0049	0.0055	0.0629	0.0776	0.1679	-62.2493	35.8792	86.989
6	0.067	0.158	-0.0091	0.5187	-0.046	0.0127	0.1045	-0.426	-0.001	0.0747	-0.0561	-0.4948	-0.1619	-0.1103	0.0155	-0.1313	0.1907	-0.2701	0.0137	0.1277	0.0088	-55.6536	42.9107	93.3243
7	0.1256	-0.0488	0.0055	0.0259	0.0378	0.0306	0.2969	-0.1112	-0.4301	0.233	-0.1646	0.1426	0.2283	-0.2736	-0.0055	0.1508	-0.0428	-0.0252	0.1388	0.0783	0.1076	-69.6489	42.7989	93.3349
8	0.0164	0.0105	0.0005	0.0223	-0.0031	0.0218	0.0122	-0.0952	0.1491	0.1186	0.0612	0.1314	-0.2965	-0.0807	-0	0.1294	0.0005	0.0108	0.2183	0.0347	0.1711	-72.5407	49.3086	87.3077
9	0.7235	0.0449	0.4245	0.0127	0.034	0.2634	-0.0201	-0.3297	0.2165	0.1113	-0.0689	0.1738	-0.1432	-0.377	-0.0823	0.162	-0.001	0.0348	0.1206	-0.0122	0.0575	-67.1881	54.3541	93.9415
10	0.0452	0.0671	0.1432	0.3108	0.2407	0.6064	-0.0973	-0.424	0.2274	0.1228	0.2077	-0.1611	0.1559	0.2045	0.0539	0.054	0.0413	0.0108	0.2001	-0.0651	0.171	-46.7531	47.1476	76.8453
11	0.0143	-0.0254	-0.0074	0.0289	0.0157	0.0244	0.0553	-0.0313	-0.1708	-0.0105	-0.0326	-0.0305	0.6392	-0.0025	0.0052	0.159	-0.0044	-0.001	0.0836	0.0012	0.0763	-58.1957	38.1079	75.6647
12	0.0681	0.0146	0.0708	0.0085	0.0393	0.172	0.0752	0.0688	0.0649	-0.0287	-0.1382	-0.1064	0.0759	-0.2056	-0.0024	0.1492	0.0109	0.0155	0.0641	-0.0025	0.1252	-54.0076	35.6904	70.1372
13	0.1036	-0.0516	-0.0499	0.0551	-0.0295	0.0366	-0.0679	-0.2121	-0.2205	0.0355	0.0304	-0.0914	-0.2377	0.037	0.0016	0.0807	-0.0157	-0.0063	0.0659	-0.0109	0.0872	-53.8761	47.6909	76.5408
14	0.0713	0.0232	-0.0265	0.1455	0.0588	0.2968	-0.3307	-0.5017	0.0953	0.343	-0.0585	-0.2488	0.1246	0.2141	-0.3571	0.2199	-0.0317	-0.1618	0.1384	-0.0157	0.2637	-53.6605	60.2431	89.1975
15	0.0375	0.0053	-0.0182	0.0132	0.0223	0.0317	0.0376	-0.0672	0.125	-0.2042	0.1183	0.1313	0.0015	-0.1354	0.0047	0.139	0.0214	-0.0055	0.1741	0.0252	0.1177	-65.2183	58.7004	85.8653
16	0.0285	0.0104	0.0544	0.1795	-0.1575	0.3484	0.0329	-0.0897	-0.0782	0.1905	0.0246	-0.0086	-0.085	0.0375	0.0249	0.0634	-0.0049	-0.0114	0.0722	-0.0019	0.1277	-57.6364	47.8402	83.0783
17	0.1024	0.053	-0.1004	0.0743	0.0019	0.1834	0.3242	0.0519	-0.0034	0.0373	0.0463	0.086	-0.0045	0.3326	0.0794	0.0596	0.0256	-0.0126	0.1422	-0.0015	0.1008	-52.3419	47.9867	85.0728
18	0.0543	0.012	-0.0091	0.0181	0.0363	0.0243	0.0368	-0.0937	0.0568	-0.0894	0.14	0.0179	0.2295	-0.0981	0.0111	0.1214	-0.0005	-0.0136	0.0838	0.0052	0.0935	-58.8134	47.5591	71.0643
19	-0.0034	-0.0048	-0.0094	0.202	-0.2737	0.3259	-0.1451	0.0905	-0.0225	-0.0612	-0.1526	-0.0378	0.2833	0.3596	-0.0784	0.1807	0.0921	-0.0156	0.1668	-0.0113	0.1259	-47.3101	40.0067	64.5108
20	0.0774	0.047	-0.0236	0.0738	-0.0746	0.0703	0.0422	-0.0078	-0.2021	0.1089	-0.0385	0.0763	-0.1739	0.1294	0.0183	0.1602	0.0018	-0.0024	0.1214	-0.0326	0.1184	-55.9512	47.1768	64.7522
21	0.0335	0.0617	0.1042	0.4218	0.2359	0.3423	0.2321	-0.2124	-0.0035	0.0157	-0.0907	0.3001	-0.0684	-0.3293	-0.0149	0.1628	0.0126	0.0155	0.1361	0.0548	0.119	-61.8847	63.7224	62.4295
22	0.0844	-0.033	-0.0126	0.3448	0.0993	0.017	0.015	0.0516	-0.0085	0.0306	0.0482	-0.0464	0.005	-0.2353	0.0385	0.152	-0.0207	0.0053	0.1606	0.0581	0.0912	-59.968	65.2463	54.4688
23	0.0152	-0.0098	-0.0048	-0.0004	0.0077	0.0229	-0.0576	0.2212	-0.3444	-0.1177	-0.3292	-0.2056	0.3531	-0.0082	-0.005	0.1485	0.0455	0.0527	0.2811	0.0126	0.222	-42.7191	56.7895	54.1995
24	0.1941	0.1572	0.095	0.1139	0.0877	0.045	-0.0886	0.3771	0.0873	0.0835	0.1085	-0.0504	-0.1476	0.3497	0.0062	0.124	0.0228	0.0151	0.1866	0.0194	0.0887	-52.513	62.4113	56.2377
25	0.5434	-0.1293	-0.0661	0.0689	0.1585	0.3819	-0.0928	0.1011	0.2004	0.1143	-0.0568	-0.2676	-0.4496	0.3721	-0.0354	0.2013	-0.0588	0.0176	0.1386	0.0743	0.2299	-49.0065	70.3019	59.2461
26	0.0131	0.1079	0.0455	0.9737	0.3588	0.1134	0.1832	-0.1433	0.1768	0.0458	0.5107	-0.457	-0.2215	0.3643	0.2872	0.0277	-0.0119	0.2661	0.3373	0.1407	0.0159	-46.1776	63.3865	52.6621
27	0.1881	0.0313	0.456	0.0011	0.0741	1.0698	-0.11	-0.0137	0.2347	-0.1722	-0.4218	-0.1489	-0.0171	-0.1727	-0.2417	0.2098	-0.0161	0.0114	0.1893	0.1222	0.0999	-59.2541	63.9449	50.0163
28	0.0254	-0.007	-0.0023	0.0047	0.0065	0.0341	-0.0648	0.0955	-0.2315	-0.2606	0.2143	0.0443	0.1584	0.0006	0.0024	0.2095	-0.0418	-0.0132	0.2444	0.0381	0.1047	-58.8888	57.5079	49.3335
29	0.0389	0.0636	0.0168	0.131	0.0814	0.0324	-0.1564	0.3006	-0.1394	-0.2712	0.0042	0.0989	0.3349	0.4318	-0.0821	0.3522	0.0579	0.137	0.2174	-0.009	-0.565	-53.0291	52.2069	49.7922
30	0.012	0.0015	-0.0114	0.0163	0.0063	0.0117	-0.0518	-0.0402	-0.2083	0.1228	0.1323	-0.2529	0.1053	0.4092	0	0.1479	0.0203	-0.0263	0.2326	-0.013	0.1831	-47.1948	61.2256	75.1203
31	0.6115	-0.2664	-0.7068	0.1255	0.307	0.8443	0.2218	-0.1752	0.5183	-0.4514	0.2762	0.1982	-0.6232	0.1536	0.0802	0.1965	0.0117	0.0247	0.0504	0.0364	0.1506	-56.0529	70.8949	68.5049
32	0.049	-0.0319	0.1425	0.1835	-0.1065	0.5691	-0.0161	-0.0135	0.0718	-0.1173	0.1291	0.13	-0.0424	0.3609	0.0599	0.0541	-0.0343	0.0138	0.0486	0.0086	0.1058	-55.9627	68.0414	75.7327
33	0.1944	-0.076	-0.2569	0.4271	-0.191	0.4524	0.1629	0.0609	-0.0862	0.157	0.1218	-0.1341	0.0098	0.1649	0.137	0.0559	0.0343	-0.0009	0.1318	-0.0786	0.1563	-46.4479	54.1115	68.263
34	0.3178	0.2144	-0.0149	0.1651	-0.0496	0.0294	-0.0722	-0.015	-0.4135	-0.1749	0.1398	-0.3166	0.4377	0.3763	-0.0019	0.2717	0.0054	-0.0056	0.2573	-0.0535	0.1774	-49.8639	46.3729	57.6569
35	0.1632	-0.1548	-0.176	0.1914	0.1997	0.1964	0.1681	0.144	0.2685	-0.3534	0.2968	0.2041	-0.0433	-0.1297	0.0172	0.15	0.0127	-0.0073	0.1785	0.0344	0.1479	-56.8382	54.2305	60.7046
36	0.0117	-0.0435	0.0025	0.1464	-0.1308	0.18	0.0515	0.1763	0.062	0.0101	-0.0087	0.1298	0.0841	0.1575	0.0042	0.0707	-0.0292	0.0133	0.0807	0.016	0.1204	-48.6992	62.4684	64.9599
37	0.1787	0.0089	-0.15	0.113	-0.0935	0.1415	0.2703	-0.1917	0.1489	0.019	-0.1104	0.0416	-0.0503	0.2164	0.0273	0.0741	-0.0331	-0.0144	0.1502	0.0025	0.0958	-49.3537	59.2196	66.1607
38	0.0034	0.0021	-0.0263	0.0383	-0.0733	0.2863	0.0832	0.027	-0.0543	-0.0292	0.2092	-0.2694	0.0062	0.3101	0.015	0.0553	-0.0083	0.013	0.0637	-0.0242	0.098	-58.133	64.1902	79.2501
39	0.0525	0.035	-0.0366	0.0435	-0.0799	0.2208	0.197	-0.1263	0.0447	0.1998	-0.2374	0.0686	-0.3548	0.273	-0.0096	0.1197	-0.0303	-0.0186	0.0913	-0.0374	0.1671	-53.4013	65.6215	85.7933
40	0.0139	-0.0124	0.0148	0.0003	0.0103	-0.0088	-0.0546	-0.013	-0.0008	-0.1641	-0.0603	0.1295	-0.062	-0.0631	-0.0048	0.111	-0.0081	-0.0345	0.0775	-0.031	0.124	-63.2519	58.9185	77.4115

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 3:8)	A	3 - 8
2	X-RAY DIFFRACTION	2	(chain A and resid 9:16)	A	9 - 16
3	X-RAY DIFFRACTION	3	(chain A and resid 17:21)	A	17 - 21
4	X-RAY DIFFRACTION	4	(chain A and resid 22:26)	A	22 - 26
5	X-RAY DIFFRACTION	5	(chain A and resid 27:31)	A	27 - 31
6	X-RAY DIFFRACTION	6	(chain A and resid 32:36)	A	32 - 36
7	X-RAY DIFFRACTION	7	(chain A and resid 37:43)	A	37 - 43
8	X-RAY DIFFRACTION	8	(chain A and resid 44:49)	A	44 - 49
9	X-RAY DIFFRACTION	9	(chain A and resid 50:56)	A	50 - 56
10	X-RAY DIFFRACTION	10	(chain B and resid 378:382)	B	378 - 382
11	X-RAY DIFFRACTION	11	(chain B and resid 383:388)	B	383 - 388
12	X-RAY DIFFRACTION	12	(chain B and resid 389:397)	B	389 - 397
13	X-RAY DIFFRACTION	13	(chain B and resid 398:404)	B	398 - 404
14	X-RAY DIFFRACTION	14	(chain B and resid 405:410)	B	405 - 410
15	X-RAY DIFFRACTION	15	(chain B and resid 411:416)	B	411 - 416
16	X-RAY DIFFRACTION	16	(chain B and resid 417:426)	B	417 - 426
17	X-RAY DIFFRACTION	17	(chain B and resid 427:434)	B	427 - 434
18	X-RAY DIFFRACTION	18	(chain B and resid 435:440)	B	435 - 440
19	X-RAY DIFFRACTION	19	(chain B and resid 441:446)	B	441 - 446
20	X-RAY DIFFRACTION	20	(chain B and resid 447:454)	B	447 - 454
21	X-RAY DIFFRACTION	21	(chain C and resid 3:7)	C	3 - 7
22	X-RAY DIFFRACTION	22	(chain C and resid 8:15)	C	8 - 15
23	X-RAY DIFFRACTION	23	(chain C and resid 16:20)	C	16 - 20
24	X-RAY DIFFRACTION	24	(chain C and resid 21:27)	C	21 - 27
25	X-RAY DIFFRACTION	25	(chain C and resid 28:33)	C	28 - 33
26	X-RAY DIFFRACTION	26	(chain C and resid 34:38)	C	34 - 38
27	X-RAY DIFFRACTION	27	(chain C and resid 39:44)	C	39 - 44
28	X-RAY DIFFRACTION	28	(chain C and resid 45:50)	C	45 - 50
29	X-RAY DIFFRACTION	29	(chain C and resid 51:56)	C	51 - 56
30	X-RAY DIFFRACTION	30	(chain D and resid 378:383)	D	378 - 383
31	X-RAY DIFFRACTION	31	(chain D and resid 384:389)	D	384 - 389
32	X-RAY DIFFRACTION	32	(chain D and resid 390:400)	D	390 - 400
33	X-RAY DIFFRACTION	33	(chain D and resid 401:406)	D	401 - 406
34	X-RAY DIFFRACTION	34	(chain D and resid 407:414)	D	407 - 414
35	X-RAY DIFFRACTION	35	(chain D and resid 415:420)	D	415 - 420
36	X-RAY DIFFRACTION	36	(chain D and resid 421:426)	D	421 - 426
37	X-RAY DIFFRACTION	37	(chain D and resid 427:437)	D	427 - 437
38	X-RAY DIFFRACTION	38	(chain D and resid 438:442)	D	438 - 442
39	X-RAY DIFFRACTION	39	(chain D and resid 443:449)	D	443 - 449
40	X-RAY DIFFRACTION	40	(chain D and resid 450:454)	D	450 - 454

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