PDB-6lsn: Crystal structure of tubulin-inhibitor complex

ID or keywords:

Entry

Database: PDB / ID: 6lsn

Title

Crystal structure of tubulin-inhibitor complex

Components

Stathmin-4
Tubulin alpha-1B chain
Tubulin beta chain
Tubulin tyrosine ligase

Keywords

CELL CYCLE / Inhibitor

Function / homology

Function and homology information

tubulin-tyrosine ligase activity / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Resolution of Sister Chromatid Cohesion / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Mitotic Prometaphase / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle ...
Similarity search - Function

Biological species

Sus scrofa (pig)

Mus musculus (house mouse)

Gallus gallus (chicken)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.445 Å

Authors

Gang, L. / Wang, Y.X. / Cheng, J.J.

Citation

Journal: To Be Published
Title: Design, Synthesis, and Bioevaluation of Pyrazolo[1,5-a]Pyrimidine Derivatives as Tubulin Polymerization Inhibitors Targeting the Colchicine Binding Site with Potent Anticancer Activities
Authors: Gang, L. / Wang, Y.X. / Chen, J.J.

History

Deposition	Jan 17, 2020	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Jan 20, 2021	Provider: repository / Type: Initial release
Revision 1.1	Nov 29, 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	6lsn.cif.gz	898.3 KB	Display	PDBx/mmCIF format
PDB format	pdb6lsn.ent.gz	738.5 KB	Display	PDB format
PDBx/mmJSON format	6lsn.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	6lsn_validation.pdf.gz	2.3 MB	Display	wwPDB validaton report
Full document	6lsn_full_validation.pdf.gz	2.3 MB	Display
Data in XML	6lsn_validation.xml.gz	83.8 KB	Display
Data in CIF	6lsn_validation.cif.gz	113.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ls/6lsn ftp://data.pdbj.org/pub/pdb/validation_reports/ls/6lsn	HTTPS FTP

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Related structure data

Related structure data	6lsmC 4i55S S: Starting model for refinement C: citing same article (ref.)
Similar structure data	6fjf-d 4zi7-d 6d88-d 6qqn-d 6jcj-d 5xlz-d 5gon-d 6fii-d 4o2a-d 5zxh-d 6y4m-d 4o4l-d 6hx8-d 5jcb-d 6ses-d 7dae-d 5xag-d 5ca1-d 6bs2-d 4i50-d 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	#175 - Jul 2014 Microtubules similarity (25) #176 - Aug 2014 Dynein similarity (17) #118 - Oct 2009 Sodium-Potassium Pump similarity (1) #168 - Dec 2013 DNA Helicase similarity (1) #195 - Mar 2016 RAF Protein Kinases similarity (1) #241 - Jan 2020 Twenty Years of Molecules similarity (17)

Deposited unit

A: Tubulin alpha-1B chain

B: Tubulin beta chain

C: Tubulin alpha-1B chain

D: Tubulin beta 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
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	105.296, 158.458, 181.959
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: 50041.273 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Gene: TUBA1B / Production host: Escherichia coli (E. coli) / References: UniProt: Q2XVP4
#2: Protein	Tubulin beta chain Mass: 49999.887 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Gene: TUBB2B / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: A0A287AGU7, UniProt: P02554*PLUS
#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.) Mus musculus (house mouse) / Gene: Stmn4 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P63042
#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 , 9 types, 395 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.: 6 / 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-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#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: Chemical	ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₆H₁₃NO₄S / Comment: pH buffer*YM
#11: Chemical	ChemComp-ERR / 2-(1-methylindol-5-yl)-7-(3,4,5-trimethoxyphenyl)pyrazolo[1,5-a]pyrimidine Mass: 414.456 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂₄H₂₂N₄O₃ / Feature type: SUBJECT OF INVESTIGATION
#12: 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
#13: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 376 / 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: 2.9 Å³/Da / Density % sol: 57.65 %
Crystal grow	Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.7 Details: 6% PEG, 5% glycerol, 0.1M MES, 30 mM CaCl2, 30 mM MgCl2, pH 6.7

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

SSRF

/ Beamline: BL18U1 / Wavelength: 0.9793 Å

Detector

Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Nov 20, 2019

Radiation

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

Radiation wavelength

Wavelength: 0.9793 Å / Relative weight: 1

Reflection

Resolution: 2.445→50 Å / Num. obs: 112697 / % possible obs: 100 % / Redundancy: 6.6 % / R_merge(I) obs: 0.131 / R_pim(I) all: 0.055 / R_rim(I) all: 0.143 / Χ²: 0.423 / Net I/σ(I): 2.7

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	Χ²	% possible all
2.45-2.49	5.9	1.069	5556	0.62	0.472	1.17	0.409	100
2.49-2.54	6	0.95	5564	0.656	0.422	1.041	0.406	99.8
2.54-2.59	6.3	0.815	5571	0.732	0.35	0.888	0.407	100
2.59-2.64	6.4	0.683	5577	0.796	0.291	0.743	0.406	100
2.64-2.7	6.9	0.654	5594	0.835	0.267	0.707	0.416	100
2.7-2.76	6.8	0.563	5566	0.861	0.23	0.609	0.416	100
2.76-2.83	6.8	0.478	5562	0.905	0.196	0.517	0.423	100
2.83-2.9	6.7	0.391	5586	0.933	0.162	0.424	0.421	100
2.9-2.99	6.6	0.343	5609	0.938	0.143	0.372	0.432	100
2.99-3.09	6.4	0.266	5592	0.958	0.114	0.29	0.431	100
3.09-3.2	6.4	0.219	5605	0.97	0.094	0.239	0.437	100
3.2-3.32	6.8	0.184	5608	0.982	0.076	0.2	0.435	100
3.32-3.48	6.9	0.15	5613	0.989	0.061	0.162	0.443	100
3.48-3.66	6.9	0.124	5659	0.991	0.051	0.134	0.454	100
3.66-3.89	6.8	0.099	5642	0.994	0.041	0.107	0.445	100
3.89-4.19	6.4	0.08	5650	0.995	0.034	0.088	0.433	100
4.19-4.61	6.8	0.066	5675	0.997	0.027	0.072	0.424	100
4.61-5.28	6.9	0.063	5722	0.997	0.026	0.069	0.413	100
5.28-6.65	6.3	0.068	5752	0.996	0.029	0.074	0.399	100
6.65-50	6.3	0.048	5994	0.998	0.02	0.052	0.404	99.9

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Processing

Software

Name	Version	Classification
PHENIX	1.14_3260	refinement
HKL-2000		data reduction
HKL-2000		data scaling
PDB_EXTRACT	3.25	data extraction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 4I55

4i55

Resolution: 2.445→33.167 Å / SU ML: 0.26 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 22.8

	R_factor	Num. reflection	% reflection
R_free	0.22	2000	1.78 %
R_work	0.1766	-	-
obs	0.1774	112322	99.54 %

Solvent computation

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

Displacement parameters

B_iso max: 178.45 Å² / B_iso mean: 61.2834 Å² / B_iso min: 17.41 Å²

Refinement step

Cycle: final / Resolution: 2.445→33.167 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	17401	0	217	376	17994
B_iso mean	-	-	58.97	52.71	-
Num. residues	-	-	-	-	2200

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	% reflection obs (%)
2.4453-2.5064	0.2949	138	0.2619	7576	97
2.5064-2.5742	0.2843	141	0.2496	7793	100
2.5742-2.6499	0.2682	141	0.2298	7815	100
2.6499-2.7354	0.257	142	0.2234	7844	100
2.7354-2.8331	0.275	143	0.2303	7868	100
2.8331-2.9465	0.3063	142	0.2255	7805	100
2.9465-3.0805	0.2637	142	0.2084	7869	100
3.0805-3.2428	0.2498	143	0.2058	7867	100
3.2428-3.4457	0.2447	143	0.192	7903	100
3.4457-3.7114	0.2438	143	0.1711	7908	100
3.7114-4.0843	0.1974	143	0.1478	7911	100
4.0843-4.674	0.1655	145	0.1329	7980	100
4.674-5.8833	0.1831	146	0.1481	8042	100
5.8833-33.167	0.1781	148	0.1567	8141	98

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	0.1873	-0.018	0.0544	0.0429	-0.0268	0.0497	0.0031	0.0879	-0.0749	-0.2778	0.1888	-0.1627	-0.384	0.0556	0.0312	0.4994	-0.107	0.1106	0.2989	-0.091	0.3174	29.4224	97.8344	53.9046
2	0.0623	-0.0105	0.0366	0.0065	0.0061	0.0214	-0.046	0.2061	-0.1201	-0.168	0.2714	-0.041	-0.2948	0.0411	-0	0.5727	-0.1022	0.0696	0.3182	-0.0247	0.3014	28.5668	87.813	42.527
3	0.241	-0.0628	-0.0101	0.4336	-0.0808	0.5224	0.01	0.0277	-0.0062	-0.0008	0.18	-0.1617	-0.0159	0.2439	0.4073	0.2177	-0.0481	0.0501	0.3483	-0.1598	0.3471	35.1166	78.7301	55.2357
4	0.0051	-0.0067	0.0028	0.0334	0.0202	0.027	0.1477	-0.1213	-0.0729	0.0634	-0.0024	-0.0315	-0.1208	-0.0889	0	0.2975	0.0425	-0.0047	0.342	-0.0699	0.3659	11.9118	80.239	60.1192
5	-0.0038	0.0619	0.0263	0.1586	0.124	0.265	0.0127	-0.0185	-0.0352	0.0795	0.0032	-0.0091	-0.1233	-0.0204	0	0.262	0.0028	0.0413	0.2315	-0.0658	0.2493	18.8191	87.6033	68.5107
6	0.0575	0.0066	0.007	0.0058	0.0524	0.0403	-0.0646	-0.1298	0.0631	0.1603	0.0697	0.1341	0.014	0.0801	-0	0.5946	0.043	0.0616	0.3476	-0.0697	0.3802	16.6724	88.1141	80.6973
7	0.1368	0.2292	0.025	0.1344	0.1002	0.2354	0.006	0.0206	-0.0224	0.1216	0.027	-0.0032	0.0097	0.0659	0	0.2628	0.0301	0.0071	0.2262	-0.0609	0.2237	22.276	77.0491	66.443
8	0.011	-0.0067	0.0174	0.0031	-0.0086	0.01	-0.0176	0.0891	-0.0955	0.2989	0.0182	-0.1109	0.1011	0.0544	0	0.4382	0.1137	-0.0564	0.4265	-0.0498	0.3952	30.9731	64.0488	70.5813
9	0.0026	-0.0122	0.0284	0.011	-0.0129	0.0176	0.1697	0.0758	0.1133	0.0305	0.0712	-0.0041	-0.1354	-0.0646	-0	0.3005	0.0099	0.0803	0.2954	-0.0447	0.3859	15.2645	64.9305	21.3434
10	0.1465	0.027	0.0123	0.0163	-0.0082	0.0104	0.2386	0.1911	0.1975	-0.2022	-0.1611	-0.1312	-0.2327	0.0061	0	0.5246	0.041	0.1166	0.3461	-0.0064	0.4859	15.9507	72.791	17.4362
11	0.138	-0.031	0.1043	0.0229	0.0067	0.1433	0.2723	0.1277	-0.1028	-0.1394	-0.0852	-0.092	-0.094	0.2806	0.0246	0.2706	-0.0688	0.1026	0.3552	-0.0601	0.3006	28.7894	56.7093	14.3348
12	0.0707	-0.0587	-0.095	-0.0062	0.1051	0.0921	0.0328	-0.0027	0.1039	-0.0844	0.0222	0.0664	-0.0425	0.0308	0	0.2325	-0.0402	0.0436	0.3192	-0.0908	0.3259	23.9044	56.3498	25.2163
13	0.001	-0.0768	0.029	0.0298	0.0416	0.1127	0.0446	-0.1235	0.0277	0.13	-0.1309	0.0308	0.1271	-0.0774	0	0.2442	0.0002	0.0295	0.33	-0.1081	0.3522	15.4751	48.9123	29.0646
14	0.0942	-0.1012	-0.2213	0.0961	0.0707	0.2019	0.0905	-0.0866	0.054	0.0624	-0.1429	0.0927	-0.1116	-0.1893	-0	0.2862	0.0022	0.0246	0.3681	-0.124	0.4228	10.4965	63.161	30.9965
15	0.0308	-0.0003	-0.0116	0.0455	0.043	0.0887	0.0829	0.1199	0.0301	-0.006	-0.1514	0.0066	0.005	-0.0528	-0	0.2166	0.0273	-0.0006	0.3226	-0.1184	0.3219	5.4823	59.6464	37.253
16	0.0444	0.0041	-0.0066	0.0151	-0.0071	0.0996	-0.0823	-0.1018	0.0074	0.0622	0.0098	-0.0722	-0.0115	-0.3396	0	0.3256	0.0311	0.0555	0.4326	-0.1096	0.3787	6.3537	61.5303	44.6566
17	-0.0378	-0.1011	0.0864	-0.0309	-0.0048	0.0863	0.0619	0.0459	-0.0099	0.0983	-0.0933	0.134	0.1668	-0.1855	-0	0.1859	0.009	0.0441	0.2651	-0.0613	0.2752	14.2849	44.0212	34.1131
18	-0.0097	0.0549	-0.0229	0.1224	-0.054	0.0173	0.0433	0.0149	-0.0806	0.1746	0.0117	-0.1224	0.2363	0.0691	0	0.2194	0.0211	-0.031	0.2985	-0.0414	0.2841	25.1872	38.7611	30.9124
19	0.1203	0.0362	-0.0617	0.2808	0.164	0.4734	-0.0788	0.0487	0.0046	-0.1042	0.0841	-0.0059	-0.0422	0.0347	-0	0.2234	-0.0418	0.006	0.2491	-0.0032	0.2478	19.9172	33.2899	-12.0688
20	0.1602	-0.1568	-0.0107	0.3369	0.4103	0.6071	-0.0281	-0.0325	0.0093	-0.0141	-0.0354	0.012	0.0309	-0.0706	-0	0.1457	-0.0199	0.0134	0.1959	-0.0181	0.2144	7.4554	26.3959	3.111
21	0.0988	0.1071	-0.0178	0.1283	-0.0535	0.1954	-0.1726	0.5112	0.0077	-0.319	0.1636	-0.1165	0.0132	-0.1636	0.0132	0.6146	-0.0797	0.1044	0.6271	-0.0978	0.322	22.0517	6.5155	-43.8449
22	0.309	-0.3315	-0.1368	0.3435	0.2131	0.5821	-0.1664	0.1578	0.0291	-0.1144	0.1277	-0.0058	0.2081	-0.2072	-0.0231	0.3465	-0.1037	0.1053	0.258	-0.122	0.1769	16.3215	-4.7633	-26.4163
23	0.1	0.0851	0.106	0.0459	0.0486	0.0452	-0.0065	-0.047	0.3024	0.2312	0.1104	-0.0952	0.1747	0.237	0	0.6911	-0.0304	-0.0057	0.4943	-0.096	0.4249	27.6404	93.2403	82.2078
24	0.0752	-0.0991	-0.2326	-0.6146	1.2079	-0.4294	-0.1246	-0.0657	0.0672	-0.4385	0.1428	-0.1174	0.4328	0.2557	-0.0723	0.2246	0.0545	0.1642	0.4236	-0.1958	0.3949	42.67	27.7879	3.9288
25	0.2024	0.0996	-0.2411	0.0209	-0.0534	0.1019	-0.1742	0.0491	-0.0827	-0.0419	-0.0564	-0.1499	0.4302	-0.0075	-0.0038	0.5582	-0.034	0.0917	0.2975	-0.0584	0.3772	7.4953	57.2207	74.2757
26	0.0743	-0.0751	0.077	0.0931	0.0821	0.0882	-0.0572	-0.3337	-0.1354	0.3793	-0.077	-0.0273	0.22	0.5755	-0	0.7522	0.2638	0.008	0.9774	0.2004	0.5435	16.3318	57.8795	107.1871
27	0.1912	0.0578	0.069	0.0246	0.005	0.1763	-0.5274	0.2041	-0.3401	0.0216	0.0986	-0.1779	0.5414	-0.2378	-0.0766	0.8803	0.1372	0.3178	0.2562	0.1387	0.5984	-1.8514	48.4943	99.6798
28	0.2605	0.0106	-0.1208	0.0847	0.0015	0.1402	-0.2951	0.0187	-0.0865	0.0958	0.2019	0.0263	0.1434	0.0385	-0.0001	0.4718	0.0303	0.0902	0.2795	0.0303	0.32	-1.4623	61.9713	88.1041

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 through 72 )	A	1 - 72
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 73 through 102 )	A	73 - 102
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 103 through 199 )	A	103 - 199
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 200 through 223 )	A	200 - 223
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 224 through 306 )	A	224 - 306
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 307 through 338 )	A	307 - 338
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 339 through 414 )	A	339 - 414
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 415 through 440 )	A	415 - 440
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 2 through 27 )	B	2 - 27
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 28 through 88 )	B	28 - 88
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 89 through 127 )	B	89 - 127
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 128 through 182 )	B	128 - 182
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 183 through 215 )	B	183 - 215
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 216 through 259 )	B	216 - 259
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 260 through 295 )	B	260 - 295
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 296 through 372 )	B	296 - 372
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 373 through 401 )	B	373 - 401
18	X-RAY DIFFRACTION	18	chain 'B' and (resid 402 through 438 )	B	402 - 438
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 1 through 197 )	C	1 - 197
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 198 through 440 )	C	198 - 440
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 2 through 127 )	D	2 - 127
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 128 through 441 )	D	128 - 441
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 6 through 46 )	E	6 - 46
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 47 through 144 )	E	47 - 144
25	X-RAY DIFFRACTION	25	chain 'F' and (resid 1 through 83 )	F	1 - 83
26	X-RAY DIFFRACTION	26	chain 'F' and (resid 84 through 198 )	F	84 - 198
27	X-RAY DIFFRACTION	27	chain 'F' and (resid 199 through 283 )	F	199 - 283
28	X-RAY DIFFRACTION	28	chain 'F' and (resid 284 through 384 )	F	284 - 384

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