PDB-8cle: Vinblastine bound to tubulin (T2R-TTL) complex

ID or keywords:

Entry

Database: PDB / ID: 8cle

Title

Vinblastine bound to tubulin (T2R-TTL) complex

Components

Stathmin-4
Tubulin alpha-1B chain
Tubulin beta-2B chain
Tubulin-Tyrosine Ligase

Keywords

CELL CYCLE / Drug-tubulin-complex Cell cycle inhibition

Function / homology

Function and homology information

positive regulation of axon guidance / microtubule-based process / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / microtubule cytoskeleton organization / microtubule cytoskeleton / nervous system development / mitotic cell cycle / microtubule / protein heterodimerization activity ...
Similarity search - Function

Biological species

synthetic construct (others)

Bos taurus (cattle)

Method

X-RAY DIFFRACTION /

FREE ELECTRON LASER /

MOLECULAR REPLACEMENT / Resolution: 3.2 Å

Authors

Wranik, M. / Bertrand, Q. / Kepa, M.W. / Weinert, T. / Steinmetz, M. / Standfuss, J.

Funding support

Switzerland, 3items

Organization	Grant number	Country
Swiss National Science Foundation	31003A_179351	Switzerland
Swiss National Science Foundation	310030_207462	Switzerland
Swiss National Science Foundation	310030_192566	Switzerland

Citation

Journal: Nat Commun / Year: 2023
Title: A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers.
Authors: Wranik, M. / Kepa, M.W. / Beale, E.V. / James, D. / Bertrand, Q. / Weinert, T. / Furrer, A. / Glover, H. / Gashi, D. / Carrillo, M. / Kondo, Y. / Stipp, R.T. / Khusainov, G. / Nass, K. / ...

History

Deposition	Feb 16, 2023	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Dec 13, 2023	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	8cle.cif.gz	892.8 KB	Display	PDBx/mmCIF format
PDB format	pdb8cle.ent.gz	743.2 KB	Display	PDB format
PDBx/mmJSON format	8cle.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	8cle_validation.pdf.gz	2.2 MB	Display	wwPDB validaton report
Full document	8cle_full_validation.pdf.gz	2.2 MB	Display
Data in XML	8cle_validation.xml.gz	83.4 KB	Display
Data in CIF	8cle_validation.cif.gz	110.7 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/cl/8cle ftp://data.pdbj.org/pub/pdb/validation_reports/cl/8cle	HTTPS FTP

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Related structure data

Related structure data	8cl5C 8cl6C 8cl7C 8cl8C 8cl9C 8clbC 8clcC 8cldC 8clfC 8clgC 8clhC C: citing same article (ref.)
Similar structure data	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	#175 - Jul 2014 Microtubules similarity (20) #176 - Aug 2014 Dynein similarity (19) #241 - Jan 2020 Twenty Years of Molecules similarity (19)

Deposited unit

A: Tubulin alpha-1B chain

C: Tubulin alpha-1B chain

D: Tubulin beta-2B chain

E: Stathmin-4

F: Tubulin-Tyrosine Ligase

B: Tubulin beta-2B chain

hetero molecules

250 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	106.390, 159.740, 182.240
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

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Protein , 4 types, 6 molecules ACDBEF

#1: Protein	Tubulin alpha-1B chain Mass: 48966.324 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P81947
#2: Protein	Tubulin beta-2B chain Mass: 48391.410 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: Q6B856
#3: Protein	Stathmin-4 Mass: 14207.262 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)
#4: Protein	Tubulin-Tyrosine Ligase Mass: 38500.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)

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Non-polymers , 6 types, 41 molecules

#5: Chemical	ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₁₀H₁₆N₅O₁₄P₃ / Comment: GTP, energy-carrying molecule*YM
#6: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: Mg
#7: Chemical	ChemComp-CA / CALCIUM ION Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#8: Chemical	ChemComp-VLB / (2ALPHA,2'BETA,3BETA,4ALPHA,5BETA)-VINCALEUKOBLASTINE / VINBLASTINE Mass: 810.974 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₄₆H₅₈N₄O₉ / Feature type: SUBJECT OF INVESTIGATION / Comment: medication, chemotherapy*YM
#9: Chemical	ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₁₀H₁₅N₅O₁₁P₂ / Comment: GDP, energy-carrying molecule*YM
#10: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 32 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	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: 3.15 Å³/Da / Density % sol: 60.91 %
Crystal grow	Temperature: 293 K / Method: batch mode / pH: 6.5 Details: 6% PEG4000 (w/v), 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole, 5 mM L-tyrosine

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Data collection

Diffraction	Mean temperature: 293 K / Serial crystal experiment: Y
Diffraction source	Source: FREE ELECTRON LASER / Site: SwissFEL ARAMIS / Beamline: ESA / Wavelength: 1.03 Å
Detector	Type: PSI JUNGFRAU 16M / Detector: PIXEL / Date: Feb 28, 2020
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.03 Å / Relative weight: 1
Reflection	Resolution: 3.1→15.13 Å / Num. obs: 56577 / % possible obs: 100 % / Redundancy: 42.8 % / CC_1/2: 0.771 / Net I/σ(I): 3.07
Reflection shell	Resolution: 3.1→3.2 Å / Mean I/σ(I) obs: 0.9 / Num. unique obs: 5570 / CC_1/2: 0.26
Serial crystallography sample delivery	Method: injection
Serial crystallography sample delivery injection	Carrier solvent: Hydroxyethylcellulose / Description: High-viscosity injection / Injector diameter: 75 µm

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Processing

Software

Name	Version	Classification
PHENIX	1.20_4487	refinement
CrystFEL	0.8.0	data reduction
CrystFEL	0.8.0	data scaling
PHENIX	1.20_4487	phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 3.2→15.13 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 24.49 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2479	1261	2.46 %
R_work	0.1995	-	-
obs	0.2007	51318	99.88 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 3.2→15.13 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	17256	0	183	32	17471

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.006
X-RAY DIFFRACTION	f_angle_d	0.995
X-RAY DIFFRACTION	f_dihedral_angle_d	10.653	2479
X-RAY DIFFRACTION	f_chiral_restr	0.061	2686
X-RAY DIFFRACTION	f_plane_restr	0.006	3168

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
3.2-3.33	0.3328	138	0.302	5490	X-RAY DIFFRACTION	100
3.33-3.48	0.3477	139	0.265	5484	X-RAY DIFFRACTION	100
3.48-3.66	0.279	139	0.2379	5504	X-RAY DIFFRACTION	100
3.66-3.88	0.2704	139	0.213	5537	X-RAY DIFFRACTION	100
3.88-4.18	0.2616	140	0.1868	5543	X-RAY DIFFRACTION	100
4.18-4.59	0.2146	140	0.1725	5562	X-RAY DIFFRACTION	100
4.59-5.23	0.2128	139	0.1659	5568	X-RAY DIFFRACTION	100
5.23-6.5	0.2415	142	0.1926	5625	X-RAY DIFFRACTION	100
6.5-15.13	0.2155	145	0.1825	5744	X-RAY DIFFRACTION	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	3.5611	-0.9612	-0.5522	4.5033	-0.8199	2.7086	0.2415	0.1663	0.1725	-0.6963	-0.1491	-0.392	-0.8882	0.0686	-0.059	0.7135	-0.1512	0.1648	0.431	-0.1584	0.5322	30.349	98.8774	54.2643
2	0.7587	0.1698	0.6543	2.9043	0.9955	2.8086	-0.2135	0.2035	0.1929	-0.6802	0.4974	-0.3003	-0.6291	0.3828	-0.2442	0.568	-0.1176	0.1089	0.67	-0.2044	0.6242	35.69	84.6414	49.1011
3	0.0477	-0.225	0.2538	2.7134	-0.0513	1.9039	0.1168	-0.1087	-0.0878	0.1044	0.1174	-0.0743	-0.1349	0.1215	-0.1598	0.3402	0.0335	0.0973	0.4449	-0.2303	0.4678	24.3605	82.7066	61.6918
4	0.8936	0.9217	-1.5841	3.3853	-0.5279	3.292	0.4315	-0.2228	0.2141	0.4347	-0.1246	0.5489	-0.4813	-0.1646	-0.2617	0.4907	-0.0121	0.019	0.548	-0.2136	0.6005	15.0704	85.7771	71.2153
5	1.0156	-0.6261	-0.4599	2.8968	1.1935	2.6736	-0.0544	-0.1018	0.2748	0.7279	0.1667	0.0532	0.0633	0.2225	-0.16	0.3937	0.0038	0.0474	0.4687	-0.1258	0.465	21.443	81.2822	70.8313
6	3.3167	1.0002	2.3879	6.9767	1.8952	2.3585	-0.0103	-1.0853	-0.327	1.0235	-0.3321	-0.0206	1.4114	-0.0955	0.2738	0.595	0.1072	-0.0633	0.6349	-0.1181	0.6395	32.1212	64.885	69.6823
7	3.6485	-0.9302	-0.8167	2.0082	-0.2645	2.4063	-0.089	0.106	0.3116	-0.2633	0.019	0.1781	-0.3544	0.087	0.0894	0.4099	-0.0399	-0.0103	0.3883	0.0187	0.3322	13.5197	43.1614	-13.3706
8	3.2186	-2.4779	1.483	7.1145	-0.4071	3.3154	-0.0774	0.9458	0.1739	-1.349	-0.027	-0.3079	-0.4868	-0.1585	0.0984	0.604	-0.1156	0.0567	0.6299	0.0047	0.4535	17.6896	32.056	-22.6139
9	1.1879	0.335	0.6639	1.9463	1.058	1.5921	-0.012	0.0807	-0.1445	-0.2942	0.0548	-0.138	0.0047	0.1318	-0.0374	0.3045	-0.0646	0.0114	0.3174	-0.004	0.2927	19.5261	26.1507	-7.4551
10	1.0019	-0.031	0.9364	0.6826	0.5737	1.3947	0.0023	0.1026	0.1421	-0.1186	-0.0223	0.0879	-0.1191	0.0534	0.0664	0.3062	0.0118	0.0105	0.3643	-0.0505	0.4269	7.3036	34.1977	0.6611
11	2.0308	0.0349	1.3616	1.4681	0.5317	1.605	-0.2127	0.051	-0.1861	0.2161	-0.0334	0.1814	0.0536	-0.3167	0.0645	0.4138	-0.0834	0.0559	0.4912	-0.1009	0.4196	-1.9605	29.8971	6.6975
12	5.9647	-3.5789	1.188	3.2464	-0.4422	1.8102	-0.7953	-0.5892	-0.2437	0.482	0.5449	0.118	0.2346	-0.396	0.195	0.4383	-0.0033	0.0306	0.4696	-0.0803	0.4877	0.7535	32.2845	18.2544
13	2.4797	-0.1896	0.4408	2.4424	0.5536	3.2199	-0.0369	-0.0293	0.162	-0.266	0.0694	0.1412	0.0173	-0.1125	0.0944	0.3897	0.0193	-0.0396	0.2779	-0.049	0.4123	-0.2431	37.5323	0.0059
14	2.6564	-0.5305	-1.7342	1.5252	1.2951	2.5233	-0.1131	-0.3478	-0.1979	0.2531	0.1646	-0.0136	0.6212	0.5127	-0.0597	0.4855	0.0028	0.001	0.3938	-0.0038	0.3759	22.1027	11.8936	2.4564
15	2.9787	-0.8303	-0.186	2.1653	-0.0284	1.2704	-0.0218	0.9137	0.0984	-0.7446	-0.1421	-0.0569	0.1166	-0.8322	0.0793	0.935	-0.1392	0.0333	1.0538	-0.179	0.6304	14.435	11.3352	-40.6186
16	3.1061	-0.4543	-1.2413	2.2989	0.3803	1.7987	-0.2043	1.0444	-0.0165	-0.6811	0.2955	-0.5353	-0.1531	0.0136	-0.1325	1.0164	-0.2647	0.2147	1.0984	-0.2552	0.5947	27.2553	3.4512	-44.1792
17	1.3386	0.4249	0.0408	0.4499	-0.1935	0.9549	-0.2693	0.2161	-0.6487	-0.667	0.2291	-0.1964	0.5931	-0.1081	0.1263	0.7745	-0.2014	0.1913	0.7335	-0.3314	0.6554	24.0229	-6.9789	-32.2187
18	2.2772	-0.6365	-0.8965	1.091	0.7518	1.8864	-0.1786	0.4537	-0.1729	-0.2477	-0.0276	0.0512	0.3816	-0.416	-0.0628	0.6386	-0.1894	0.0758	0.7303	-0.1506	0.4803	12.9713	0.6319	-28.9521
19	2.1715	-0.7778	-2.0174	3.9775	0.7973	1.8722	-0.1329	0.328	-0.7515	-0.199	0.3793	0.2887	0.321	-0.0306	-0.1389	0.6823	-0.162	0.0466	0.6924	-0.1971	0.5963	2.3896	-5.4478	-23.6514
20	4.0719	-0.7721	-0.851	2.4518	0.0692	1.6217	-0.2932	0.3325	-0.5514	0.2535	0.3377	0.662	0.1038	-0.1921	-0.0555	0.5698	-0.1625	0.0098	0.6664	-0.1061	0.5859	1.0065	5.1428	-17.6395
21	1.5692	0.2288	-1.4194	2.4673	0.4816	1.7989	-0.2628	0.4566	-0.3657	-0.1178	0.1474	-0.0971	0.4971	-0.1028	0.1219	0.6473	-0.1542	0.0627	0.5606	-0.1731	0.5705	12.9186	-6.1957	-21.8396
22	4.3048	-0.8959	-2.4293	2.8434	0.5568	2.9539	-0.4788	-0.5195	-1.0986	0.2063	0.2576	-0.3072	0.8972	1.0134	0.0017	0.9628	0.0103	0.1562	0.6447	-0.1837	0.9006	30.0495	-15.9655	-23.2494
23	5.1671	0.513	0.512	2.3764	1.6788	3.3368	0.1967	-0.1024	-0.0758	0.7462	-0.2945	0.1573	-1.1633	1.2275	0.2439	0.8041	-0.2127	0.0377	0.9044	-0.1598	0.6827	26.4434	100.5989	82.6826
24	0.8693	-0.0576	0.8068	2.0602	-0.5107	1.9817	-0.4375	0.2396	-0.561	1.2182	-0.314	-0.4009	0.1994	-0.1798	0.547	0.952	-0.1968	0.0857	0.8112	-0.274	0.7122	32.7576	83.8313	82.4455
25	0.331	-0.1536	-0.3489	0.9907	0.9267	0.9131	-0.254	0.0126	-0.0193	0.3881	0.3587	-0.0324	0.6319	0.6903	-0.2499	0.6645	0.0565	0.07	0.7367	-0.182	0.6481	42.4431	30.2696	5.567
26	3.1628	0.2158	-1.6924	4.2268	-0.7442	4.9936	-0.3645	0.3211	-0.4042	0.0348	0.0171	0.3492	2.2079	-0.488	0.2712	1.1781	-0.1227	0.1037	0.6627	-0.1413	0.8409	5.2862	53.423	69.2956
27	1.5546	-0.003	-0.7526	0.5727	-0.6615	1.124	0.0202	0.019	-0.4036	0.1686	0.1878	-0.2011	-0.1141	0.3585	-0.3202	0.7219	0.0716	0.1144	0.5125	-0.0661	0.6744	11.5454	64.9494	80.8134
28	1.7611	1.498	1.1197	2.1806	-0.3597	2.5926	0.2438	-0.7658	0.7063	0.5195	-0.027	-0.6268	0.055	0.8739	-0.1772	1.0173	0.1094	0.0911	1.2979	0.0468	0.8292	15.0423	66.5704	101.7219
29	3.2109	0.9085	-0.1321	0.9586	-0.8791	1.219	0.5887	-0.8084	-0.4453	0.8734	-0.0692	-0.9771	1.215	0.9723	-0.6542	1.2868	0.3516	-0.1465	1.1812	0.0677	1.0082	21.831	56.1213	109.5318
30	1.5406	0.7665	-1.0857	1.8314	0.0833	2.4238	-0.035	-0.4556	-0.4439	0.3858	-0.0838	0.1461	1.1357	0.5861	0.2962	1.0959	0.0792	0.2689	0.7129	0.0684	0.7878	2.195	55.0557	97.2392
31	1.7596	0.3381	0.4075	0.4029	0.39	0.3787	0.4569	-0.7818	-1.3898	1.58	0.3271	-0.5084	0.5425	0.7342	-0.3756	1.5601	0.6003	-0.1124	1.4766	0.0627	1.8202	7.9227	43.7129	108.4162
32	0.5887	0.8286	0.5546	2.003	1.2524	0.7881	-0.6093	0.9177	-0.5115	1.3462	0.3856	0.0395	0.6154	-0.5629	-0.3903	1.5124	0.0985	0.1968	0.8304	0.1439	1.1923	-4.7728	44.1798	100.3319
33	2.1134	0.1774	-1.5595	1.158	-0.5897	3.6407	-0.4164	0.0247	-0.2723	0.2796	0.3279	0.2115	0.2052	0.0206	0.0355	0.7785	0.1106	0.1521	0.4919	0.1058	0.5656	0.2096	62.7651	93.1648
34	3.0602	0.2384	-0.472	2.4654	-0.9554	5.4069	-0.6463	0.5798	-0.3626	0.03	0.318	0.4833	0.7357	-0.6884	0.3968	0.758	-0.1328	0.0816	0.9265	-0.0203	0.9668	-7.297	58.0991	79.3031
35	4.0598	-1.5498	-0.2002	2.7507	-0.2476	3.3364	0.0006	-0.0131	0.7075	0.0047	0.0227	0.2687	-0.9407	-0.0488	-0.069	0.6265	0.0195	0.0248	0.3909	-0.0028	0.5708	16.4394	74.7742	22.0547
36	1.7741	-0.8079	0.5632	4.4127	0.9687	2.742	-0.1727	0.3043	0.1438	-0.4385	0.2357	0.1142	-0.4795	0.1187	-0.1479	0.4929	-0.0706	0.0531	0.5377	-0.039	0.3997	24.8132	60.7498	12.937
37	1.2329	0.3845	0.8637	1.6996	0.5368	1.4075	0.0115	-0.028	0.0204	-0.1071	0.0665	-0.3601	-0.1315	0.0993	-0.1248	0.2525	-0.0063	0.0319	0.3019	-0.1164	0.3192	21.0545	54.363	26.4893
38	0.4424	-0.8977	-0.9896	2.4992	1.5899	2.5007	-0.0424	-0.7049	-0.5298	-0.8222	-0.3032	0.2257	-0.2123	-0.8441	-0.1163	0.2818	0.066	-0.0634	0.483	-0.0491	0.5433	2.6673	57.6698	24.7163
39	1.7442	1.0516	0.4709	0.8744	0.9575	1.9229	0.0561	-0.1118	0.2754	0.0647	0.1819	-0.125	-0.3176	0.2272	-0.1514	0.372	-0.0314	0.0426	0.3393	-0.161	0.4079	18.8797	64.4932	38.5769
40	1.7566	-0.9847	-0.0932	2.4446	1.9001	4.5518	-0.2601	0.1749	-0.0388	-0.1057	-0.4209	0.0544	-0.3005	-1.3296	0.5662	0.6676	0.1064	0.0325	0.7247	-0.2157	0.7094	-4.1248	65.5182	34.9086
41	2.5132	-1.0934	0.5068	2.2909	0.6436	2.978	-0.1498	-0.3958	0.2413	0.1562	0.0011	0.273	-0.3966	-0.8196	0.2202	0.4155	0.0434	0.0029	0.5432	-0.2066	0.4689	6.5849	63.1926	44.5122
42	0.8024	-0.3739	-0.0055	2.4767	2.2194	3.8238	-0.1647	-0.1941	-0.1707	0.457	0.0435	0.0907	0.6722	0.1665	-0.0579	0.3508	0.0364	0.0228	0.4457	-0.0144	0.4149	20.7555	41.7291	32.074

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 1 through 71 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 72 through 160 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 161 through 259 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 260 through 306 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 307 through 414 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 415 through 439 )
7	X-RAY DIFFRACTION	7	chain 'C' and (resid 1 through 72 )
8	X-RAY DIFFRACTION	8	chain 'C' and (resid 73 through 102 )
9	X-RAY DIFFRACTION	9	chain 'C' and (resid 103 through 223 )
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 224 through 281 )
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 282 through 324 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 325 through 350 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 351 through 381 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 382 through 440 )
15	X-RAY DIFFRACTION	15	chain 'D' and (resid 1 through 56 )
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 57 through 140 )
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 141 through 214 )
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 215 through 268 )
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 269 through 311 )
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 312 through 338 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 339 through 401 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 402 through 441 )
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 6 through 20 )
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 21 through 46 )
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 47 through 140 )
26	X-RAY DIFFRACTION	26	chain 'F' and (resid 1 through 48 )
27	X-RAY DIFFRACTION	27	chain 'F' and (resid 49 through 83 )
28	X-RAY DIFFRACTION	28	chain 'F' and (resid 84 through 127 )
29	X-RAY DIFFRACTION	29	chain 'F' and (resid 128 through 175 )
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 176 through 222 )
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 223 through 242 )
32	X-RAY DIFFRACTION	32	chain 'F' and (resid 243 through 274 )
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 275 through 339 )
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 340 through 380 )
35	X-RAY DIFFRACTION	35	chain 'B' and (resid 1 through 64 )
36	X-RAY DIFFRACTION	36	chain 'B' and (resid 65 through 128 )
37	X-RAY DIFFRACTION	37	chain 'B' and (resid 129 through 214 )
38	X-RAY DIFFRACTION	38	chain 'B' and (resid 215 through 238 )
39	X-RAY DIFFRACTION	39	chain 'B' and (resid 239 through 273 )
40	X-RAY DIFFRACTION	40	chain 'B' and (resid 274 through 295 )
41	X-RAY DIFFRACTION	41	chain 'B' and (resid 296 through 373 )
42	X-RAY DIFFRACTION	42	chain 'B' and (resid 374 through 438 )

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