PDB-6p61: Structure of a Glycosyltransferase from Leptospira borgpetersenii...

ID or keywords:

Entry

Database: PDB / ID: 6p61

Title

Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197)

Components

Glycosyltransferase

Keywords

TRANSFERASE / SSGCID / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease

Function / homology

: / Glycosyltransferase 2-like / Glycosyl transferase family 2 / Nucleotide-diphospho-sugar transferases / transferase activity / CITRIC ACID / Glycosyltransferase

Function and homology information

Biological species

Leptospira borgpetersenii serovar Hardjo-bovis

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.95 Å

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Citation

Journal: to be published
Title: Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197)
Authors: Abendroth, J. / Conrady, D.G. / Lorimer, D.D. / Horanyi, P.S. / Edwards, T.E.

History

Deposition	May 31, 2019	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jul 10, 2019	Provider: repository / Type: Initial release
Revision 1.1	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
Revision 1.2	Apr 3, 2024	Group: Refinement description / Category: pdbx_initial_refinement_model

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	6p61.cif.gz	350.2 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	6p61_validation.pdf.gz	493.1 KB	Display	wwPDB validaton report
Full document	6p61_full_validation.pdf.gz	502.7 KB	Display
Data in XML	6p61_validation.xml.gz	38.9 KB	Display
Data in CIF	6p61_validation.cif.gz	55.9 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/p6/6p61 ftp://data.pdbj.org/pub/pdb/validation_reports/p6/6p61	HTTPS FTP

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Related structure data

Similar structure data	2xd7-3 5cit-2 2y87-d 4kdc-d 4ge1-4 2xd7-2 2p6w-d 5w8c-d 4ixl-2 6tmc-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
Other databases	TargetTrack: SSGCID-LpboA.19148.a

Similar structure data

Other databases

TargetTrack: SSGCID-LpboA.19148.a

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#254 - Feb 2021 Cellulose Synthase similarity (3) #156 - Dec 2012 ABO Blood Type Glycosyltransferases similarity (1)

Deposited unit

A: Glycosyltransferase

B: Glycosyltransferase

C: Glycosyltransferase

D: Glycosyltransferase

hetero molecules

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

1

A: Glycosyltransferase

hetero molecules

defined by author&software
Evidence: gel filtration
27.4 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Glycosyltransferase

hetero molecules

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

3

C: Glycosyltransferase

hetero molecules

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

4

D: Glycosyltransferase

hetero molecules

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

Unit cell

Length a, b, c (Å)	56.250, 123.170, 76.770
Angle α, β, γ (deg.)	90.000, 92.440, 90.000
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Glycosyltransferase Mass: 26704.361 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) (bacteria) Strain: JB197 / Gene: LBJ_1113 / Plasmid: LpboA.19148.a.B1 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) Variant (production host): BL21(DE3) / References: UniProt: Q04TP4
#2: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C₂H₆O₂
#3: Chemical	ChemComp-CIT / CITRIC ACID Mass: 192.124 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₆H₈O₇
#4: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₃H₈O₃
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 714 / 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: 2.49 Å³/Da / Density % sol: 50.7 %
Crystal grow	Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: Optimization screen based on MCSG-1, condition F3: 200mM Ammonium citrate dibasic pH 5.5, 18% (w/V) PEG 3350: LpboA.19148.a.B1.PS38508 at 26.29mg/ml, seeded: cryo: 20% EG: tray 309474 e3: ...Details: Optimization screen based on MCSG-1, condition F3: 200mM Ammonium citrate dibasic pH 5.5, 18% (w/V) PEG 3350: LpboA.19148.a.B1.PS38508 at 26.29mg/ml, seeded: cryo: 20% EG: tray 309474 e3: puck irc8-7. Protein purified in 20mM HEPES pH7, 300mM NaCl, 5% Glycerol, 1mM TCEP

Crystal

Density Matthews: 2.49 Å³/Da / Density % sol: 50.7 %

Crystal grow

Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: Optimization screen based on MCSG-1, condition F3: 200mM Ammonium citrate dibasic pH 5.5, 18% (w/V) PEG 3350: LpboA.19148.a.B1.PS38508 at 26.29mg/ml, seeded: cryo: 20% EG: tray 309474 e3: ...

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

ALS

/ Beamline: 5.0.2 / Wavelength: 1.00003 Å

Detector

Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: May 14, 2019

Radiation

Monochromator: Double-crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1.00003 Å / Relative weight: 1

Reflection

Resolution: 1.95→33.152 Å / Num. obs: 75239 / % possible obs: 99 % / Redundancy: 3.281 % / B_iso Wilson estimate: 33.519 Å² / CC_1/2: 0.999 / R_merge(I) obs: 0.051 / R_rim(I) all: 0.061 / Χ²: 1.012 / Net I/σ(I): 14.82 / Num. measured all: 246869 / Scaling rejects: 30

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Mean I/σ(I) obs	Num. measured obs	Num. possible	Num. unique obs	CC_1/2	R_rim(I) all	% possible all
1.95-2	2.29	0.373	2.16	11769	5572	5140	0.797	0.477	92.2
2-2.06	2.784	0.325	2.94	15032	5473	5399	0.866	0.401	98.6
2.06-2.12	3.333	0.26	4.41	17701	5327	5311	0.932	0.31	99.7
2.12-2.18	3.461	0.215	5.39	17867	5173	5163	0.955	0.254	99.8
2.18-2.25	3.435	0.204	6.01	17142	5010	4991	0.955	0.242	99.6
2.25-2.33	3.321	0.17	6.82	16022	4842	4824	0.969	0.203	99.6
2.33-2.42	3.328	0.135	8.39	15456	4654	4644	0.98	0.161	99.8
2.42-2.52	3.506	0.109	10.55	15672	4472	4470	0.987	0.129	100
2.52-2.63	3.519	0.1	11.68	15129	4306	4299	0.988	0.118	99.8
2.63-2.76	3.421	0.079	14.27	14065	4120	4111	0.993	0.093	99.8
2.76-2.91	3.292	0.065	16.64	12906	3931	3921	0.994	0.078	99.7
2.91-3.08	3.392	0.053	20.36	12645	3741	3728	0.996	0.063	99.7
3.08-3.3	3.482	0.043	24.63	12067	3484	3466	0.997	0.051	99.5
3.3-3.56	3.421	0.035	29.33	11118	3262	3250	0.998	0.042	99.6
3.56-3.9	3.243	0.03	32	9576	2971	2953	0.998	0.036	99.4
3.9-4.36	3.517	0.027	37.2	9550	2728	2715	0.999	0.032	99.5
4.36-5.03	3.476	0.025	39.62	8269	2391	2379	0.999	0.03	99.5
5.03-6.17	3.233	0.027	34.84	6585	2045	2037	0.999	0.032	99.6
6.17-8.72	3.5	0.025	37.17	5464	1573	1561	0.999	0.03	99.2
8.72-33.152	3.231	0.02	43.45	2834	894	877	0.999	0.024	98.1

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Processing

Software

Name	Version	Classification
XDS		data reduction
XSCALE		data scaling
PHENIX	(dev_3500)	refinement
PDB_EXTRACT	3.25	data extraction
MR-Rosetta		phasing
Coot		model building

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB entry 3BCV_B as per RosettaMR

Resolution: 1.95→33.152 Å / SU ML: 0.19 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 18.88

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.1835	2075	2.76 %	0
R_work	0.151	-	-	-
obs	0.1519	75188	99.03 %	-

Solvent computation

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

Displacement parameters

B_iso max: 112.2 Å² / B_iso mean: 34.6296 Å² / B_iso min: 14.03 Å²

Refinement step

Cycle: final / Resolution: 1.95→33.152 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	6165	0	146	723	7034
B_iso mean	-	-	60.43	42.93	-
Num. residues	-	-	-	-	767

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	6627
X-RAY DIFFRACTION	f_angle_d	0.743	8989
X-RAY DIFFRACTION	f_dihedral_angle_d	13.036	4060
X-RAY DIFFRACTION	f_chiral_restr	0.056	984
X-RAY DIFFRACTION	f_plane_restr	0.004	1175

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 15

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.9501-1.9954	0.256	135	0.2356	4479	4614	92
1.9954-2.0453	0.2605	161	0.2121	4803	4964	98
2.0453-2.1006	0.2218	120	0.1866	4892	5012	100
2.1006-2.1624	0.2159	121	0.1689	4951	5072	100
2.1624-2.2322	0.2068	140	0.1686	4892	5032	100
2.2322-2.312	0.2276	155	0.1746	4860	5015	99
2.312-2.4045	0.2168	142	0.1622	4875	5017	100
2.4045-2.5139	0.2076	137	0.1522	4910	5047	100
2.5139-2.6464	0.1981	118	0.1555	4960	5078	100
2.6464-2.8121	0.1759	160	0.1551	4875	5035	100
2.8121-3.0291	0.2066	121	0.1572	4915	5036	100
3.0291-3.3337	0.1928	130	0.1508	4938	5068	100
3.3337-3.8155	0.157	153	0.1395	4863	5016	100
3.8155-4.8048	0.1333	135	0.1131	4943	5078	100
4.8048-33.1569	0.1702	147	0.148	4957	5104	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	1.8191	0.8109	-1.6255	3.8088	-1.5449	7.1559	-0.0116	-0.1803	-0.1278	0.2672	-0.0324	-0.155	-0.0305	0.3906	-0.0335	0.196	0.0719	-0.0361	0.2089	-0.0025	0.2663	-11.7559	-25.2221	10.6991
2	6.6091	3.4438	-4.9378	8.3771	-5.875	5.613	-0.2506	0.1124	-0.3325	-0.3677	0.1471	0.2171	0.8887	-0.1968	0.0656	0.263	0.0359	-0.004	0.1665	-0.0163	0.227	-16.0859	-31.6133	4.2885
3	2.3552	0.7768	0.907	5.1792	-2.1594	2.1035	-0.1628	0.2054	-0.1446	-0.1723	-0.2512	-0.0672	0.1876	0.111	0.3647	0.1911	0.0767	-0.0055	0.1951	-0.0257	0.2586	-7.5841	-26.385	7.0341
4	1.1692	0.7366	-0.1698	7.4036	-2.1568	2.243	0.0065	-0.1227	0.0355	0.7383	0.0677	-0.3212	-0.0047	0.1751	-0.0602	0.2572	0.0573	-0.0562	0.2246	-0.0281	0.2342	-7.9352	-26.0524	17.6224
5	1.2439	-0.4275	1.4989	2.4841	-1.7812	3.0959	0.0736	0.1066	0.0563	-0.0774	-0.0127	-0.0484	0.2063	0.1753	-0.0855	0.1577	0.0302	0.0173	0.1837	-0.0437	0.2181	-14.8116	-21.4037	0.0301
6	3.8051	-0.3248	-0.3484	1.3609	0.9243	3.5941	0.0059	-0.3347	-0.2959	0.1951	-0.03	0.2989	0.1899	-0.3242	-0.0148	0.1476	0.0123	0.0191	0.1781	0.0215	0.2468	-26.3189	-19.02	3.7747
7	2.7049	0.77	1.2293	2.7588	1.1685	7.0202	0.0247	-0.1461	0.11	0.2551	-0.0148	-0.0643	-0.1011	0.3953	0.0009	0.1894	-0.0262	0.0106	0.1793	-0.011	0.2556	-9.4659	-7.9687	8.212
8	6.2953	1.5579	-4.2948	7.1813	-4.3108	9.6747	0.1058	-0.286	0.1737	0.1812	-0.1188	0.2411	-0.6554	-0.1792	-0.0103	0.2808	0.0159	-0.0024	0.2299	-0.0578	0.3456	-18.6529	-4.3216	8.1641
9	5.4398	2.0921	1.1084	5.8799	-0.9313	2.372	0.158	-0.1815	-0.0522	0.3133	0.0767	0.3858	-0.083	-0.282	-0.241	0.1618	0.0592	0.0481	0.1672	-0.0321	0.1669	-24.2917	-17.5306	2.9409
10	2.804	0.6285	1.7666	2.4853	1.5873	4.233	0.0523	-0.1655	0.0115	0.1016	-0.1136	0.1294	-0.1789	-0.0785	0.065	0.2224	-0.0388	0.033	0.1609	-0.0008	0.168	3.4724	18.1981	31.1913
11	3.3034	0.2222	2.3212	1.1875	1.4674	4.8022	0.0443	-0.0268	-0.0331	-0.0694	-0.0052	0.0289	-0.0944	-0.0151	-0.0283	0.1822	-0.016	0.0321	0.1206	0.0109	0.1684	2.2984	11.1461	19.1728
12	4.5875	-2.0167	1.0803	3.6204	-0.6087	3.8874	-0.0505	-0.2188	0.0183	0.3212	-0.0191	-0.083	0.158	0.0768	0.0995	0.2152	-0.0429	0.0206	0.1658	0.0032	0.1902	2.5303	2.567	22.1092
13	1.8527	-1.6069	-1.1977	5.0357	2.1815	1.1305	0.0255	-1.1962	0.0541	1.5751	-0.0804	-0.0825	0.1356	0.1878	-0.0261	0.591	-0.1456	0.1034	0.5968	-0.0579	0.3479	-8.753	1.3345	31.5825
14	5.5283	0.9654	-0.2263	3.1197	1.6004	2.4987	0.1538	-0.1522	-0.2418	0.3501	-0.0628	-0.0105	0.1869	-0.0217	-0.1065	0.2211	-0.0092	0.0179	0.1143	0.0427	0.1328	2.9136	1.4588	20.9356
15	4.1922	0.8853	-2.1255	2.343	-1.4506	6.1944	0.1695	-0.1869	-0.0022	0.2353	-0.199	-0.051	0.1404	-0.044	0.0407	0.2663	-0.0808	-0.0257	0.1482	0.0224	0.1997	23.0416	28.3054	27.1401
16	3.5331	0.8417	-1.3778	1.8307	-0.7977	2.6842	0.3216	-0.6412	0.0386	0.5525	-0.4328	-0.2935	-0.0617	0.4039	0.1052	0.3612	-0.1457	-0.0895	0.3755	0.0967	0.2869	27.8468	26.3992	36.7373
17	3.9721	0.7999	-2.6893	1.7674	-2.3091	4.3299	0.1029	-0.1468	-0.1105	0.1124	-0.1214	-0.0562	-0.0302	0.1017	0.0004	0.2155	-0.0414	-0.0152	0.1357	-0.0058	0.2026	26.2779	34.6719	19.3518
18	3.5423	-1.6284	-1.1157	4.2868	1.08	4.0035	-0.0707	-0.1435	-0.0642	0.3454	-0.0346	0.0082	-0.0777	0.1049	0.0513	0.2452	-0.0414	-0.0273	0.169	0.0275	0.1839	25.7859	43.841	18.6344
19	4.0252	-0.7686	-0.3918	4.6668	-0.4738	5.1013	0.0903	-0.4721	-0.2089	0.7045	-0.191	0.6593	-0.2816	-0.3874	0.0746	0.3319	-0.0411	0.0945	0.2672	-0.0445	0.3794	17.8671	46.12	26.3375
20	4.4176	-1.0585	0.3711	4.2761	0.3528	3.9869	0.0276	-0.3638	-0.2141	0.5433	-0.1624	-0.847	0.0934	0.7621	0.0716	0.2505	-0.0346	-0.0736	0.3434	0.0919	0.3316	38.5017	37.7619	21.6651
21	1.4306	-1.657	1.5248	4.9853	-1.6665	5.846	0.1458	-1.3246	-0.4697	1.6122	-0.4184	-0.2647	-0.0657	-0.1124	0.2379	0.6331	-0.2424	-0.1228	0.616	0.1579	0.4316	37.1509	44.277	31.0934
22	4.3136	0.1178	0.7437	3.2859	-0.853	2.4337	0.1657	-0.2274	-0.0306	0.5234	-0.1577	0.0266	-0.1647	-0.0479	0.0088	0.2718	-0.0585	-0.0045	0.145	-0.0087	0.1322	25.2646	44.2215	22.0919
23	2.2359	-0.7421	-0.5921	4.7402	-1.7778	3.4909	-0.092	0.1008	0.0226	-0.0284	-0.0541	-0.1907	-0.2757	0.3195	0.068	0.1656	-0.055	0.0307	0.185	-0.0238	0.2144	16.4332	10.2093	-11.0902
24	4.9784	-2.3484	3.7553	6.8921	-4.6926	4.4581	-0.0472	-0.0445	0.1715	0.3219	0.2497	0.2845	-0.7839	0.0041	-0.2005	0.2423	-0.0419	0.0506	0.1361	-0.0053	0.1851	12.1326	16.6735	-4.832
25	1.7027	-0.5662	-0.2011	3.4275	-1.5367	8.1748	-0.0245	-0.1205	0.0169	0.0925	-0.0244	-0.225	-0.2114	0.5649	0.0636	0.1779	-0.0585	0.0278	0.2285	-0.0131	0.2336	20.5964	11.2728	-7.4248
26	1.4197	-0.4212	0.5549	4.19	-1.9781	3.3606	-0.0245	0.0841	-0.0578	-0.3272	-0.0279	-0.2534	-0.0998	0.3428	0.0602	0.2028	-0.0488	0.0534	0.236	-0.0165	0.2103	20.3783	11.154	-17.9586
27	6.5323	-1.8708	-0.6728	3.8782	-1.5655	3.5081	0.0881	-0.0434	-0.1229	0.0528	0.002	0.0062	-0.1616	0.2696	-0.0894	0.144	-0.039	0.0099	0.1154	-0.0348	0.1508	13.5996	7.2105	-5.6951
28	5.0191	-0.6293	1.7666	2.0968	-0.6613	5.5116	-0.0131	0.1167	0.1749	-0.0049	0.0171	0.1888	-0.2244	-0.1448	0.006	0.1421	-0.0172	0.0386	0.1311	-0.0086	0.1841	4.82	3.9125	-1.3525
29	2.3346	-1.3932	-1.7502	3.2129	2.1398	8.833	0.0537	0.1193	-0.0577	-0.2351	-0.0818	-0.0359	0.182	0.3085	-0.0154	0.1519	0.0339	0.0043	0.1729	-0.0038	0.222	18.7287	-7.2915	-8.9901
30	9.2449	-1.8417	4.2667	2.9534	-2.6014	3.1629	0.2957	0.5085	-0.7877	-0.2984	-0.0563	0.4576	0.7558	-0.0208	-0.3047	0.2785	0.0081	0.0108	0.2086	-0.069	0.3438	9.4763	-10.8015	-8.9855
31	4.8236	-1.3947	-1.3494	5.5606	-0.9066	2.8793	0.1058	0.1297	-0.0159	-0.3171	0.1056	0.2144	0.0538	-0.2553	-0.2345	0.1465	-0.0453	-0.0255	0.1554	-0.0529	0.1207	4.2851	2.0768	-3.0141

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 10 through 27 )	A	10 - 27
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 28 through 41 )	A	28 - 41
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 42 through 52 )	A	42 - 52
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 53 through 89 )	A	53 - 89
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 90 through 119 )	A	90 - 119
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 120 through 154 )	A	120 - 154
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 155 through 175 )	A	155 - 175
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 176 through 185 )	A	176 - 185
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 186 through 202 )	A	186 - 202
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 11 through 90 )	B	11 - 90
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 91 through 119 )	B	91 - 119
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 120 through 164 )	B	120 - 164
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 165 through 184 )	B	165 - 184
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 185 through 201 )	B	185 - 201
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 11 through 52 )	C	11 - 52
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 53 through 90 )	C	53 - 90
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 91 through 119 )	C	91 - 119
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 120 through 133 )	C	120 - 133
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 134 through 153 )	C	134 - 153
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 154 through 164 )	C	154 - 164
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 165 through 184 )	C	165 - 184
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 185 through 202 )	C	185 - 202
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 10 through 27 )	D	10 - 27
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 28 through 41 )	D	28 - 41
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 42 through 52 )	D	42 - 52
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 53 through 89 )	D	53 - 89
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 90 through 108 )	D	90 - 108
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 109 through 154 )	D	109 - 154
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 155 through 175 )	D	155 - 175
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 176 through 185 )	D	176 - 185
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 186 through 202 )	D	186 - 202

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