PDB-5sb4: Tubulin-todalam-8-complex

ID or keywords:

Entry

Database: PDB / ID: 5sb4

Title

Tubulin-todalam-8-complex

Components

Stathmin-4
Tubulin alpha-1B chain
Tubulin beta-2B chain
Tubulin-Tyrosine LigaseTubulin—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 /

tubulin binding /

Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton ...
Similarity search - Function

Biological species

Rattus norvegicus (Norway rat)

Gallus gallus (chicken)

Bos taurus (cattle)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

FOURIER SYNTHESIS / Resolution: 2.5 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	5sb4.cif.gz	899 KB	Display	PDBx/mmCIF format
PDB format	pdb5sb4.ent.gz	738.1 KB	Display	PDB format
PDBx/mmJSON format	5sb4.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/sb/5sb4 ftp://data.pdbj.org/pub/pdb/validation_reports/sb/5sb4	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)	104.575, 157.329, 180.728
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 (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 (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 / 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, 346 molecules

#5: Chemical	ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / Guanosine 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 / Guanosine 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 / MES (buffer) Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₆H₁₃NO₄S / Comment: pH buffer*YM
#10: Chemical	ChemComp-4B6 / N-{4-[2-(2-fluoroanilino)-1,3-thiazol-4-yl]phenyl}acetamide Mass: 327.376 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₁₇H₁₄FN₃OS / 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 / Water Mass: 18.015 Da / Num. of mol.: 330 / 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: 2.5→49.62 Å / Num. obs: 103407 / % possible obs: 99.9 % / Redundancy: 13.557 % / B_iso Wilson estimate: 52.62 Å² / CC_1/2: 0.996 / R_merge(I) obs: 0.277 / R_rim(I) all: 0.287 / Χ²: 0.751 / Net I/σ(I): 10.14 / Num. measured all: 1401930 / Scaling rejects: 87

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
2.5-2.57	13.274	3.265	0.76	100193	7596	7548	0.27	3.395	99.4
2.57-2.64	13.557	2.513	1.06	99696	7355	7354	0.406	2.611	100
2.64-2.71	13.285	2.163	1.27	95347	7177	7177	0.474	2.25	100
2.71-2.8	13.321	1.757	1.6	92808	6967	6967	0.591	1.827	100
2.8-2.89	13.986	1.448	2.05	94865	6784	6783	0.694	1.503	100
2.89-2.99	13.548	1.158	2.58	88996	6569	6569	0.78	1.203	100
2.99-3.1	13.417	0.84	3.58	84918	6329	6329	0.871	0.873	100
3.1-3.23	14.284	0.684	4.57	87058	6095	6095	0.92	0.71	100
3.23-3.37	14.173	0.515	6	83368	5882	5882	0.957	0.534	100
3.37-3.54	13.969	0.368	8.28	77749	5566	5566	0.975	0.382	100
3.54-3.73	13.688	0.27	11.09	73301	5355	5355	0.985	0.28	100
3.73-3.95	12.745	0.184	14.7	64374	5052	5051	0.993	0.192	100
3.95-4.23	13.87	0.143	18.91	66231	4774	4775	0.996	0.149	100
4.23-4.57	13.021	0.104	23.63	57761	4436	4436	0.998	0.108	100
4.57-5	13.902	0.092	26.99	57302	4123	4122	0.998	0.096	100
5-5.59	13.951	0.107	24.01	52078	3733	3733	0.997	0.111	100
5.59-6.46	13.481	0.114	22.5	44715	3317	3317	0.997	0.118	100
6.46-7.91	12.672	0.079	29.05	36027	2843	2843	0.998	0.082	100
7.91-11.19	12.897	0.047	44.85	28593	2217	2217	0.999	0.049	100
11.19-49.62	12.849	0.043	50.69	16550	1307	1288	0.999	0.045	98.5

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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: 2.5→49.62 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.18 / Phase error: 25.36 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2302	9954	5.01 %
R_work	0.1983	188885	-
obs	0.1999	198839	99.91 %

Solvent computation

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

Displacement parameters

B_iso max: 198.16 Å² / B_iso mean: 66.7152 Å² / B_iso min: 31.04 Å²

Refinement step

Cycle: final / Resolution: 2.5→49.62 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	17268	0	195	330	17793
B_iso mean	-	-	59.72	53.54	-
Num. residues	-	-	-	-	2182

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 (%)
2.5-2.53	0.3577	328	0.358	6202	6530	98
2.53-2.56	0.3734	330	0.347	6301	6631	100
2.56-2.59	0.3462	333	0.3266	6322	6655	100
2.59-2.62	0.3482	331	0.3263	6295	6626	100
2.62-2.66	0.3705	329	0.3152	6257	6586	100
2.66-2.69	0.3374	335	0.3193	6379	6714	100
2.69-2.73	0.3421	329	0.3239	6228	6557	100
2.73-2.77	0.3039	333	0.3008	6329	6662	100
2.77-2.82	0.2978	335	0.2924	6342	6677	100
2.82-2.86	0.3167	331	0.2816	6262	6593	100
2.86-2.91	0.3192	332	0.2758	6307	6639	100
2.91-2.97	0.3058	330	0.2669	6298	6628	100
2.97-3.02	0.2945	331	0.2512	6273	6604	100
3.02-3.08	0.2969	334	0.2421	6317	6651	100
3.08-3.15	0.2385	329	0.2367	6339	6668	100
3.15-3.22	0.2646	327	0.2513	6223	6550	100
3.22-3.31	0.2696	331	0.2266	6335	6666	100
3.31-3.39	0.2655	336	0.2221	6304	6640	100
3.39-3.49	0.2197	335	0.2045	6340	6675	100
3.49-3.61	0.2265	333	0.187	6244	6577	100
3.61-3.74	0.2113	340	0.1833	6354	6694	100
3.74-3.89	0.2077	329	0.1714	6246	6575	100
3.89-4.06	0.1902	333	0.1628	6294	6627	100
4.06-4.28	0.1899	331	0.1518	6307	6638	100
4.28-4.54	0.1792	336	0.1397	6315	6651	100
4.54-4.89	0.1796	335	0.1357	6281	6616	100
4.89-5.39	0.1811	335	0.1558	6291	6626	100
5.39-6.16	0.2702	331	0.1722	6322	6653	100
6.17-7.76	0.1858	331	0.1711	6279	6610	100
7.76-49.62	0.1544	321	0.1461	6299	6620	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	1.3562	0.0366	-0.1948	3.6059	0.8809	2.2317	0.0188	0.0529	0.2221	-0.6525	0.3235	-0.4458	-0.8168	0.4254	-0.3303	0.6117	-0.1523	0.1337	0.5157	-0.1602	0.4728	32.239	89.435	51.041
2	1.462	0.1652	-1.3316	4.0432	0.4091	2.6299	0.1407	-0.0058	-0.006	0.6042	0.0149	-0.0011	0.4059	0.3917	-0.1012	0.4456	0.0268	0.0065	0.4748	-0.1528	0.4703	30.126	74.017	59.132
3	1.8917	0.0799	0.2758	3.2453	0.7906	3.8603	0.1091	-0.0569	0.0914	0.2976	-0.0869	0.2003	-0.1742	-0.0615	-0.021	0.4303	0.0137	0.074	0.3529	-0.1015	0.4549	17.121	84.328	67.005
4	0.8214	-0.0933	0.4011	3.7055	1.6343	3.0057	-0.0778	-0.1713	0.0965	0.7324	0.0054	0.3418	-0.0048	-0.0588	0.0658	0.4831	-0.0323	0.1232	0.475	-0.0811	0.4732	19.02	82.998	73.395
5	1.5229	0.1319	-0.0635	3.2178	2.0082	4.4558	-0.0946	-0.0718	-0.3617	0.6778	0.3873	-0.3973	0.6722	1.2125	-0.2997	0.4551	0.1329	-0.1029	0.5217	-0.0959	0.5041	32.632	61.876	60.998
6	3.7234	-1.2914	-0.7915	3.1919	0.1729	3.2061	0.0488	0.123	0.4962	-0.2363	0.0234	0.0742	-0.7393	-0.2465	-0.0757	0.5346	0.0523	0.008	0.3415	-0.0166	0.5007	16.224	69.979	19.317
7	1.519	-0.24	-0.3932	2.1092	1.2704	3.492	0.0173	0.0082	0.2099	-0.1467	-0.024	0.087	-0.2638	-0.0718	-0.0281	0.286	0.0246	-0.0032	0.3548	-0.0688	0.393	20.324	55.933	25.377
8	2.5527	-0.4726	1.0889	2.5136	0.11	3.1753	-0.2366	-0.1427	0.1668	0.1997	-0.0483	0.4026	-0.0961	-0.8789	0.262	0.44	0.0535	0.0486	0.6752	-0.1897	0.5194	6.273	60.005	42.744
9	0.7999	-0.3672	0.4622	3.2361	0.8669	3.1285	-0.0859	-0.1125	-0.1387	0.6479	0.0221	0.0934	0.6721	0.1233	0.0171	0.3245	-0.0409	0.0101	0.3791	-0.0292	0.3523	21.001	40.169	32.099
10	1.089	-0.3493	0.1695	3.3463	0.3145	1.6299	-0.0586	0.1724	0.0559	-0.356	0.0843	-0.0363	-0.1712	0.1767	-0.0192	0.3502	-0.0867	0.0298	0.4417	-0.0299	0.3805	20.157	32.927	-11.986
11	0.81	-0.3216	0.0758	1.6367	0.996	1.7625	-0.021	-0.0487	0.0772	0.0294	-0.0606	0.1582	0.0434	-0.1953	0.0782	0.2802	-0.0695	0.0419	0.3382	-0.0258	0.3582	7.778	25.858	3.144
12	3.3682	-1.0044	0.3238	3.502	-0.0481	1.8336	-0.0634	0.5307	0.169	-0.6552	0.1934	-0.0091	-0.0265	-0.0733	-0.1223	0.7042	-0.1435	0.0344	0.8476	-0.0567	0.4267	17.286	9.525	-43.914
13	1.922	-0.0199	-0.3667	1.4626	0.0297	2.3047	-0.1276	0.371	-0.1561	-0.4122	0.2062	-0.2208	0.3133	0.2541	-0.0749	0.6058	-0.0495	0.0855	0.604	-0.1911	0.4676	22.75	-2.517	-34.036
14	2.7548	-2.3445	-0.2258	3.2888	-0.303	0.497	0.1207	0.1534	-0.1799	-0.5676	-0.2901	0.6204	0.4207	-0.7093	0.1408	0.6993	-0.1723	-0.0295	0.8079	-0.2054	0.6391	2.168	-6.372	-24.703
15	1.6243	-0.2425	-0.2513	1.2482	-0.1344	2.6065	-0.1593	0.2295	-0.2387	-0.096	0.1308	0.0707	0.2194	-0.2826	0.0381	0.4999	-0.0998	0.0339	0.4541	-0.1241	0.3752	8.621	-1.86	-20.765
16	3.4634	-0.6879	-1.363	1.364	-1.1169	2.2953	-0.2064	0.1827	-0.8807	-0.0365	-0.1171	0.061	0.5973	0.311	0.2622	0.8952	0.0114	0.0791	0.6428	-0.2465	0.752	30.231	-17.392	-24.409
17	2.2276	-1.0147	-0.3965	2.6953	0.7047	0.8533	-0.0634	-0.2615	0.0755	0.7279	0.2388	-0.3331	0.1824	0.5361	-0.1631	1.0246	-0.0554	-0.0464	0.7604	-0.2307	0.647	27.563	92.405	82.113
18	0.2097	-0.2645	-0.4688	0.1833	0.428	0.7655	-0.0668	-0.0207	-0.0106	0.2651	0.4972	-0.4527	0.402	0.7252	-0.4483	0.5304	0.0883	0.0169	0.7987	-0.2516	0.6801	43.034	27.818	4.215
19	2.8342	0.2757	-1.9524	3.1117	0.3537	4.001	-0.3299	0.3906	-0.5915	-0.2018	0.0203	-0.042	1.0394	-0.4784	0.2708	0.8381	-0.1015	0.1214	0.5338	-0.117	0.6015	6.104	54.673	69.672
20	3.3649	0.1226	2.0082	2.3	-2.3014	4.4945	-0.131	-0.5709	-0.0047	0.4483	-0.3779	-0.8972	-0.2963	1.4438	0.4496	0.7288	0.0662	-0.1183	1.1817	0.0939	0.7467	15.596	63.872	103.054
21	2.8033	-0.2691	1.1176	2.4907	-0.4097	2.4851	-0.2307	-0.6563	-0.634	0.702	-0.3957	-0.7656	0.9144	1.5212	0.5489	1.1181	0.2632	0.0695	1.2337	0.411	0.9723	10.865	51.505	105.726
22	0.4332	0.4978	-0.4718	0.8189	-0.3292	0.6632	-0.4602	-0.0783	-0.7512	0.1116	0.0481	-0.2648	0.9466	0.0682	0.2172	1.2379	0.1231	0.288	0.5281	0.1273	0.9425	-3.172	49.989	98.708
23	2.8638	0.1984	-1.5628	0.7985	-0.1497	3.2385	-0.3141	-0.0336	-0.4697	0.0735	0.1784	-0.0851	0.6366	-0.0485	0.1137	0.8139	-0.0185	0.1219	0.4629	-0.0301	0.5966	1.057	57.965	87.726
24	2.5196	-0.2807	-0.076	2.6844	-1.1423	8.6058	-0.1506	0.1502	-0.7047	0.161	-0.215	0.1118	0.347	-0.5642	0.3569	0.6616	-0.0603	0.0208	0.5808	0.0426	0.6828	-3.872	59.132	83.27

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 47:143 )	E	47 - 143
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 355:380 )	F	355 - 380

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