PDB-5sb3: Tubulin-todalam-4-complex

ID or keywords:

Entry

Database: PDB / ID: 5sb3

Title

Tubulin-todalam-4-complex

Components

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

Keywords

CELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULE

Function / homology

Function and homology information

tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / cellular response to interleukin-4 / tubulin binding / spindle microtubule / protein modification process ...
Similarity search - Function

Biological species

Rattus norvegicus (Norway rat)

Gallus gallus (chicken)

Bos taurus (domestic cattle)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

FOURIER SYNTHESIS / Resolution: 2.2 Å

Authors

Muehlethaler, T. / Milanos, L. / Ortega, J.A. / Blum, T.B. / Gioia, D. / Prota, A.E. / Cavalli, A. / Steinmetz, M.O.

Funding support

Italy,

Switzerland, 3items

Citation

Journal: Angew.Chem.Int.Ed.Engl. / Year: 2022
Title: Rational Design of a Novel Tubulin Inhibitor with a Unique Mechanism of Action.
Authors: Muhlethaler, T. / Milanos, L. / Ortega, J.A. / Blum, T.B. / Gioia, D. / Roy, B. / Prota, A.E. / Cavalli, A. / Steinmetz, M.O.

History

Deposition	Jul 8, 2021	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 27, 2022	Provider: repository / Type: Initial release
Revision 1.1	May 11, 2022	Group: Database references / Category: citation / citation_author Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2	Jun 22, 2022	Group: Database references / Category: citation / Item: _citation.journal_volume
Revision 1.3	May 22, 2024	Group: Data collection / Category: chem_comp_atom / chem_comp_bond

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5sb3.cif.gz	910.7 KB	Display	PDBx/mmCIF format
PDB format	pdb5sb3.ent.gz	746 KB	Display	PDB format
PDBx/mmJSON format	5sb3.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	5sb3_validation.pdf.gz	1.9 MB	Display	wwPDB validaton report
Full document	5sb3_full_validation.pdf.gz	1.9 MB	Display
Data in XML	5sb3_validation.xml.gz	81.9 KB	Display
Data in CIF	5sb3_validation.cif.gz	112.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/sb/5sb3 ftp://data.pdbj.org/pub/pdb/validation_reports/sb/5sb3	HTTPS FTP

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Group deposition

ID	G_1002214 (5 entries) 5sb3 5sb4 5sb5 5sb6 5sb7
Title	Todalam compounds complexed with T2R-TTL
Description	Crystal structures of Tubulin-todalam-compound complexes

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Related structure data

Related structure data	5lxtS S: Starting model for refinement
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 (28) #176 - Aug 2014 Dynein similarity (19) #241 - Jan 2020 Twenty Years of Molecules similarity (19) #118 - Oct 2009 Sodium-Potassium Pump similarity (1) #168 - Dec 2013 DNA Helicase similarity (1) #195 - Mar 2016 RAF Protein Kinases similarity (1)

Deposited unit

A: Tubulin alpha-1B chain

B: Tubulin beta-2B chain

C: Tubulin alpha-1B chain

D: Tubulin beta-2B chain

E: Stathmin-4

F: Tubulin-Tyrosine Ligase

hetero molecules

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

1

Idetical with deposited unit
defined by author

Unit cell

Length a, b, c (Å)	104.650, 157.714, 180.188
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁

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Protein , 4 types, 6 molecules ACBDEF

#1: Protein	Tubulin alpha-1B chain / Alpha-tubulin ubiquitous / Tubulin K-alpha-1 / Tubulin alpha-ubiquitous chain Mass: 50204.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / Organ: Brain / References: UniProt: P81947
#2: Protein	Tubulin beta-2B chain Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / Organ: Brain / References: UniProt: Q6B856
#3: Protein	Stathmin-4 / Stathmin-like protein B3 / RB3 Mass: 16844.162 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Stmn4 / Production host: Escherichia coli (E. coli) / References: UniProt: P63043
#4: Protein	Tubulin-Tyrosine Ligase Mass: 44378.496 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Gene: TTL / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 8 types, 693 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.: 5 / Source method: obtained synthetically / Formula: Mg
#7: Chemical	ChemComp-CA / CALCIUM ION Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#8: 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
#9: Chemical	ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₆H₁₃NO₄S / Comment: pH buffer*YM
#10: Chemical	ChemComp-47F / N-[4-(2-anilino-1,3-thiazol-4-yl)phenyl]acetamide Mass: 309.386 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₁₇H₁₅N₃OS / Feature type: SUBJECT OF INVESTIGATION
#11: Chemical	ChemComp-ACP / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE Mass: 505.208 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₁₁H₁₈N₅O₁₂P₃ / Comment: AMP-PCP, energy-carrying molecule analogue*YM
#12: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 677 / 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: 2.8 Å³/Da / Density % sol: 56.6 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 2% PEG 4K, 4% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole, 5 mM L-tyrosine

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

SLS

/ Beamline: X06DA / Wavelength: 1.00003 Å

Detector

Type: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Jun 23, 2019

Radiation

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

Radiation wavelength

Wavelength: 1.00003 Å / Relative weight: 1

Reflection

Resolution: 2.2→49.46 Å / Num. obs: 150862 / % possible obs: 99.9 % / Redundancy: 13.66 % / B_iso Wilson estimate: 45.24 Å² / CC_1/2: 0.999 / R_merge(I) obs: 0.172 / R_rim(I) all: 0.179 / Χ²: 0.765 / Net I/σ(I): 13.04 / Num. measured all: 2060719 / Scaling rejects: 263

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
2.2-2.26	13.803	2.879	0.93	151445	11084	10972	0.336	2.988	99
2.26-2.32	14.159	2.329	1.19	152619	10782	10779	0.464	2.415	100
2.32-2.39	14.058	1.856	1.51	147269	10478	10476	0.579	1.924	100
2.39-2.46	13.9	1.468	1.91	141684	10194	10193	0.68	1.523	100
2.46-2.54	13.754	1.193	2.37	136056	9894	9892	0.78	1.238	100
2.54-2.63	13.249	0.916	3	126916	9580	9579	0.843	0.952	100
2.63-2.73	12.704	0.765	3.56	117014	9212	9211	0.87	0.797	100
2.73-2.84	14.045	0.581	4.94	125279	8921	8920	0.938	0.602	100
2.84-2.97	13.716	0.457	6.28	117480	8566	8565	0.959	0.475	100
2.97-3.11	12.866	0.32	8.53	105296	8184	8184	0.977	0.333	100
3.11-3.28	13.968	0.238	11.72	108937	7799	7799	0.989	0.247	100
3.28-3.48	14.272	0.169	16.36	105368	7383	7383	0.994	0.175	100
3.48-3.72	14.12	0.119	22.46	98094	6947	6947	0.997	0.123	100
3.72-4.02	13.881	0.081	29.81	90434	6516	6515	0.999	0.084	100
4.02-4.4	13.578	0.062	36.55	80982	5964	5964	0.999	0.064	100
4.4-4.92	12.45	0.047	41.66	67778	5444	5444	0.999	0.049	100
4.92-5.69	13.715	0.054	40.76	66271	4832	4832	0.999	0.056	100
5.69-6.96	12.778	0.058	39.12	52567	4114	4114	0.999	0.06	100
6.96-9.85	14.214	0.043	54.83	45995	3236	3236	0.999	0.045	100
9.85-49.46	12.512	0.037	60.94	23235	1878	1857	0.999	0.039	98.9

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Processing

Software

Name	Version	Classification
PHENIX	1.19.1_4122	refinement
XSCALE		data scaling
PDB_EXTRACT	3.28	data extraction
XDS		data reduction
PHENIX	1.19.1_4122	phasing

Refinement

Method to determine structure:

FOURIER SYNTHESIS
Starting model: 5LXT

5lxt

Resolution: 2.2→49.46 Å / SU ML: 0.34 / Cross valid method: THROUGHOUT / σ(F): 1.31 / Phase error: 25.4 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2249	14556	4.99 %
R_work	0.1952	276888	-
obs	0.1967	291444	99.89 %

Solvent computation

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

Displacement parameters

B_iso max: 166.78 Å² / B_iso mean: 60.6471 Å² / B_iso min: 26.31 Å²

Refinement step

Cycle: final / Resolution: 2.2→49.46 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	17297	0	194	677	18168
B_iso mean	-	-	54.17	53.15	-
Num. residues	-	-	-	-	2185

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 30

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.2-2.23	0.3777	482	0.3787	9105	9587	98
2.23-2.25	0.3415	481	0.3433	9216	9697	100
2.25-2.28	0.3474	482	0.3412	9215	9697	100
2.28-2.31	0.3747	480	0.3341	9247	9727	100
2.31-2.34	0.3452	478	0.3181	9255	9733	100
2.34-2.37	0.3325	488	0.3101	9230	9718	100
2.37-2.41	0.3207	488	0.2991	9194	9682	100
2.41-2.44	0.3268	488	0.2827	9252	9740	100
2.44-2.48	0.2844	484	0.2726	9198	9682	100
2.48-2.52	0.2966	486	0.2666	9239	9725	100
2.52-2.56	0.2845	490	0.2637	9261	9751	100
2.56-2.61	0.2731	487	0.249	9240	9727	100
2.61-2.66	0.3015	486	0.2566	9222	9708	100
2.66-2.72	0.3161	480	0.2583	9196	9676	100
2.72-2.77	0.2897	489	0.2497	9247	9736	100
2.77-2.84	0.2657	490	0.2345	9239	9729	100
2.84-2.91	0.2714	484	0.2253	9317	9801	100
2.91-2.99	0.2424	485	0.2113	9175	9660	100
2.99-3.08	0.2341	485	0.2002	9272	9757	100
3.08-3.18	0.2225	481	0.1946	9206	9687	100
3.18-3.29	0.22	482	0.2019	9272	9754	100
3.29-3.42	0.2394	484	0.1979	9216	9700	100
3.42-3.58	0.2195	489	0.183	9272	9761	100
3.58-3.76	0.2111	475	0.1649	9203	9678	100
3.76-4	0.1916	498	0.1568	9242	9740	100
4-4.31	0.1621	481	0.1501	9225	9706	100
4.31-4.74	0.1623	494	0.1322	9289	9783	100
4.74-5.43	0.1932	484	0.1512	9205	9689	100
5.43-6.84	0.2061	485	0.1767	9214	9699	100
6.84-49.46	0.1695	490	0.1561	9224	9714	100

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	0.9196	-0.3525	-0.3133	3.5501	1.0191	2.4043	-0.0029	0.0958	0.1621	-0.5592	0.3157	-0.3865	-0.7769	0.4051	-0.2908	0.6066	-0.1557	0.1273	0.4997	-0.1535	0.4754	32.139	89.514	50.931
2	0.8609	-0.3049	-1.0359	2.316	0.3537	1.5521	0.0224	-0.1039	-0.0749	0.4894	0.1401	-0.2467	0.1855	0.3238	-0.1053	0.4702	0.0188	-0.0037	0.4496	-0.1389	0.4694	30.09	74.129	59.133
3	1.2395	-0.035	0.2469	2.8193	0.9058	3.4044	0.1168	-0.0804	0.0304	0.3712	-0.132	0.2981	-0.0518	-0.2018	-0.0019	0.364	-0.0047	0.0803	0.3094	-0.1004	0.3919	17.083	84.431	66.959
4	0.9025	0.0156	0.0875	2.8512	1.3734	2.416	-0.0245	-0.1169	0.0738	0.5907	-0.0212	0.3022	0.0286	-0.017	0.038	0.5181	-0.0155	0.1035	0.4532	-0.0901	0.4217	18.98	83.15	73.359
5	0.7625	0.1981	-0.275	2.0928	0.3777	1.5494	-0.0163	-0.089	-0.1629	0.5665	0.2363	-0.2585	0.252	0.5139	-0.212	0.4547	0.1117	-0.0501	0.4259	-0.1394	0.425	31.628	64.227	59.745
6	2.3939	-0.8701	-0.7568	2.5632	-0.0941	1.9667	0.1322	0.1169	0.4168	-0.3128	-0.126	0.2982	-0.7343	-0.2743	-0.0042	0.5676	0.0716	0.0053	0.3964	-0.0326	0.5142	16.263	70.017	19.465
7	1.5029	0.0324	-0.1392	2.1051	1.4224	3.1012	0.0172	0.0354	0.1143	-0.0844	-0.0697	0.0942	-0.2267	-0.0574	-0.0088	0.2565	0.0172	0.0213	0.3264	-0.0767	0.3435	20.392	55.918	25.466
8	2.0523	-0.598	0.7737	1.9566	0.1431	2.722	-0.1879	-0.1187	0.0328	0.2039	-0.1161	0.3836	-0.029	-0.8685	0.2729	0.386	0.0206	0.0632	0.5901	-0.1974	0.4798	6.346	60.011	42.842
9	0.7957	-0.4507	0.0217	2.8528	1.4492	2.5917	0.0016	-0.1235	-0.0576	0.5529	-0.0013	0.0058	0.4539	0.1782	-0.0357	0.3293	-0.0246	0.0099	0.3684	-0.0431	0.356	21.025	41.17	31.314
10	1.0455	-0.2671	0.0995	2.9613	0.4842	1.7441	-0.0539	0.1362	0.0887	-0.2737	0.1326	-0.0313	-0.1623	0.1535	-0.0701	0.2813	-0.0785	0.0403	0.3808	-0.0414	0.3422	20.271	33.083	-12.007
11	0.771	-0.1289	0.0704	1.5328	1.0542	1.6607	-0.0044	-0.0179	0.0551	0.0797	-0.0768	0.1089	0.0853	-0.1882	0.0729	0.239	-0.0529	0.0442	0.3139	-0.0263	0.3397	7.88	25.94	3.101
12	2.9005	-0.7119	0.7432	2.8351	0.0944	1.4981	-0.1363	0.4871	0.0818	-0.7241	0.2239	0.011	0.0751	0.055	-0.0732	0.6618	-0.1226	0.0572	0.758	-0.067	0.3852	17.394	9.936	-43.999
13	1.5318	0.1458	-0.544	1.3923	0.2206	2.0687	-0.1097	0.3812	-0.1634	-0.4041	0.2178	-0.222	0.2519	0.2069	-0.0973	0.5563	-0.0346	0.0703	0.5781	-0.1919	0.4462	22.9	-2.184	-34.256
14	1.4774	-1.2329	-0.2186	2.1596	0.1789	1.423	-0.0434	0.1242	-0.3462	-0.3121	-0.0902	0.6078	0.613	-0.5385	0.1446	0.6047	-0.1231	-0.0277	0.6827	-0.1998	0.5987	2.249	-6.17	-24.895
15	1.7999	-0.1164	0.0153	1.2334	0.087	2.3441	-0.1827	0.2432	-0.1936	-0.0392	0.1116	0.1049	0.2535	-0.2589	0.0545	0.4819	-0.0997	0.0302	0.4598	-0.1126	0.4032	8.749	-1.627	-20.957
16	2.0789	0.0283	0.053	1.7487	0.0292	1.806	-0.2137	0.2983	-0.8913	0.0388	0.0397	-0.1213	0.7324	0.3461	0.0043	0.8053	0.0682	0.0422	0.5696	-0.2601	0.7064	30.398	-17.18	-24.717
17	2.0666	-0.8534	-0.4185	1.6226	0.8863	0.8556	-0.1322	-0.192	0.1872	0.7329	0.2554	-0.4475	0.3067	0.4794	-0.1186	0.9717	-0.0295	-0.0181	0.6214	-0.1703	0.5654	27.52	92.689	81.976
18	0.1872	-0.1794	-0.3098	0.0024	0.1254	0.4354	-0.0366	-0.0386	-0.0502	0.3219	0.5189	-0.5552	0.4623	0.6958	-0.5132	0.4747	0.0696	0.0305	0.7884	-0.257	0.716	42.992	28.845	4.982
19	2.186	0.2732	-2.0657	2.0667	0.4823	3.0184	-0.3364	0.37	-0.6134	-0.1162	-0.0256	-0.1383	0.8936	-0.4153	0.3246	0.9208	-0.0805	0.1303	0.5811	-0.1077	0.6536	6.156	54.766	69.849
20	1.4052	0.5357	0.784	1.0164	-0.9779	2.4732	-0.0002	-0.6679	-0.0715	0.3947	-0.369	-0.801	-0.2318	1.41	0.3635	0.8206	0.0058	-0.1488	1.2435	0.0923	0.7684	15.572	64.39	103.142
21	2.1267	0.3933	0.8817	1.3774	-0.3667	2.5204	-0.0759	-0.6338	-0.9114	0.4887	-0.3033	-0.6203	0.786	1.6139	0.3184	1.0532	0.2182	0.0342	1.2594	0.374	1.0253	10.979	51.931	105.777
22	1.1099	0.7791	-0.9042	0.8824	-0.0865	1.5583	-0.3856	-0.0191	-0.7404	0.1937	0.1366	-0.1241	0.8566	-0.0261	0.1122	1.1321	0.0886	0.2267	0.4945	0.0987	0.8617	-2.887	50.092	99.144
23	2.5073	-0.135	-1.3976	0.7909	0.572	2.3648	-0.2762	0.0229	-0.4544	0.0307	0.2322	-0.0643	0.5133	0.0123	0.0235	0.7927	-0.0301	0.0826	0.4749	0.0052	0.5604	0.995	58.231	87.874
24	2.8034	-0.0525	-0.0236	1.4006	-0.1881	4.0743	-0.0949	0.1478	-0.5337	0.0641	0.0049	0.2282	0.1574	-0.1607	0.0974	0.6427	-0.0322	0.0497	0.637	0.0103	0.723	-3.971	60.367	83.714

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 1:160 )	A	1 - 160
2	X-RAY DIFFRACTION	2	( CHAIN A AND RESID 161:199 )	A	161 - 199
3	X-RAY DIFFRACTION	3	( CHAIN A AND RESID 200:311 )	A	200 - 311
4	X-RAY DIFFRACTION	4	( CHAIN A AND RESID 312:401 )	A	312 - 401
5	X-RAY DIFFRACTION	5	( CHAIN A AND RESID 402:437 )	A	402 - 437
6	X-RAY DIFFRACTION	6	( CHAIN B AND RESID 1:88 )	B	1 - 88
7	X-RAY DIFFRACTION	7	( CHAIN B AND RESID 89:259 )	B	89 - 259
8	X-RAY DIFFRACTION	8	( CHAIN B AND RESID 260:372 )	B	260 - 372
9	X-RAY DIFFRACTION	9	( CHAIN B AND RESID 373:437 )	B	373 - 437
10	X-RAY DIFFRACTION	10	( CHAIN C AND RESID 1:197 )	C	1 - 197
11	X-RAY DIFFRACTION	11	( CHAIN C AND RESID 198:440 )	C	198 - 440
12	X-RAY DIFFRACTION	12	( CHAIN D AND RESID 1:88 )	D	1 - 88
13	X-RAY DIFFRACTION	13	( CHAIN D AND RESID 89:273 )	D	89 - 273
14	X-RAY DIFFRACTION	14	( CHAIN D AND RESID 274:311 )	D	274 - 311
15	X-RAY DIFFRACTION	15	( CHAIN D AND RESID 312:399 )	D	312 - 399
16	X-RAY DIFFRACTION	16	( CHAIN D AND RESID 400:441 )	D	400 - 441
17	X-RAY DIFFRACTION	17	( CHAIN E AND RESID 6:46 )	E	6 - 46
18	X-RAY DIFFRACTION	18	( CHAIN E AND RESID 47:141 )	E	47 - 141
19	X-RAY DIFFRACTION	19	( CHAIN F AND RESID 1:66 )	F	1 - 66
20	X-RAY DIFFRACTION	20	( CHAIN F AND RESID 67:140 )	F	67 - 140
21	X-RAY DIFFRACTION	21	( CHAIN F AND RESID 141:207 )	F	141 - 207
22	X-RAY DIFFRACTION	22	( CHAIN F AND RESID 208:297 )	F	208 - 297
23	X-RAY DIFFRACTION	23	( CHAIN F AND RESID 298:354 )	F	298 - 354
24	X-RAY DIFFRACTION	24	( CHAIN F AND RESID 355:381 )	F	355 - 381

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