PDB-8whl: Crystal structure of CLASP2 in complex with CENP-E

ID or keywords:

Entry

Database: PDB / ID: 8whl

Title

Crystal structure of CLASP2 in complex with CENP-E

Components

CLIP-associating protein 2
Centromere-associated protein E

Keywords

PROTEIN BINDING / Complex

Function / homology

Function and homology information

lateral attachment of mitotic spindle microtubules to kinetochore / presynaptic cytoskeleton organization / cortical microtubule plus-end / microtubule plus-end directed mitotic chromosome migration / negative regulation of wound healing, spreading of epidermal cells / kinetochore binding / microtubule anchoring / cortical microtubule cytoskeleton / mitotic chromosome movement towards spindle pole / : ...lateral attachment of mitotic spindle microtubules to kinetochore / presynaptic cytoskeleton organization / cortical microtubule plus-end / microtubule plus-end directed mitotic chromosome migration / negative regulation of wound healing, spreading of epidermal cells / kinetochore binding / microtubule anchoring / cortical microtubule cytoskeleton / mitotic chromosome movement towards spindle pole / : / mitotic spindle midzone / basal cortex / metaphase chromosome alignment / positive regulation of extracellular matrix disassembly / basement membrane organization / kinetochore microtubule / exit from mitosis / Role of ABL in ROBO-SLIT signaling / microtubule organizing center organization / dystroglycan binding / establishment of mitotic spindle localization / negative regulation of focal adhesion assembly / negative regulation of microtubule depolymerization / microtubule nucleation / attachment of mitotic spindle microtubules to kinetochore / condensed chromosome, centromeric region / negative regulation of stress fiber assembly / microtubule plus-end binding / Kinesins / regulation of microtubule-based process / regulation of axon extension / microtubule motor activity / regulation of mitotic metaphase/anaphase transition / COPI-dependent Golgi-to-ER retrograde traffic / microtubule-based movement / kinetochore assembly / platelet-derived growth factor receptor-beta signaling pathway / spindle midzone / Golgi organization / cell leading edge / establishment or maintenance of cell polarity / positive regulation of epithelial cell migration / microtubule organizing center / regulation of microtubule polymerization / positive regulation of exocytosis / mitotic spindle assembly / chromosome, centromeric region / mitotic metaphase chromosome alignment / regulation of microtubule polymerization or depolymerization / axonal growth cone / cytoplasmic microtubule / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / MHC class II antigen presentation / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / protein tyrosine kinase binding / Resolution of Sister Chromatid Cohesion / mitotic spindle organization / regulation of actin cytoskeleton organization / spindle microtubule / trans-Golgi network / chromosome segregation / RHO GTPases Activate Formins / microtubule cytoskeleton organization / mitotic spindle / ruffle membrane / kinetochore / actin filament binding / microtubule cytoskeleton / Separation of Sister Chromatids / mitotic cell cycle / chromosome / midbody / cell cortex / microtubule binding / microtubule / cell division / centrosome / glutamatergic synapse / Golgi apparatus / ATP binding / membrane / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.2 Å

Authors

Jia, X. / Wei, Z.

Funding support

China, 4items

Organization	Grant number	Country
National Natural Science Foundation of China (NSFC)	31971131	China
National Natural Science Foundation of China (NSFC)	32170697	China
National Natural Science Foundation of China (NSFC)	32370743	China
National Natural Science Foundation of China (NSFC)	32371009	China

Citation

Journal: Nat Commun / Year: 2024
Title: CLASP-mediated competitive binding in protein condensates directs microtubule growth.
Authors: Jia, X. / Lin, L. / Guo, S. / Zhou, L. / Jin, G. / Dong, J. / Xiao, J. / Xie, X. / Li, Y. / He, S. / Wei, Z. / Yu, C.

History

Deposition	Sep 23, 2023	Deposition site: PDBJ / Processing site: PDBC
Revision 1.0	Aug 28, 2024	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	8whl.cif.gz	457.6 KB	Display	PDBx/mmCIF format
PDB format	pdb8whl.ent.gz	381.9 KB	Display	PDB format
PDBx/mmJSON format	8whl.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/wh/8whl ftp://data.pdbj.org/pub/pdb/validation_reports/wh/8whl	HTTPS FTP

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Related structure data

Related structure data	8whhC 8whiC 8whjC 8whkC 8whmC 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	#64 - Apr 2005 Kinesin similarity (11) #175 - Jul 2014 Microtubules similarity (7) #43 - Jul 2003 Src Tyrosine Kinase similarity (2) #205 - Jan 2017 Nuclear Pore Complex similarity (6) #254 - Feb 2021 Cellulose Synthase similarity (1) #18 - Jun 2001 Myosin similarity (1) #224 - Aug 2018 Legumain similarity (1) #247 - Jul 2020 Myelin-associated Glycoprotein similarity (1) #88 - Apr 2007 Clathrin similarity (1) #245 - May 2020 Spliceosomes similarity (1) #241 - Jan 2020 Twenty Years of Molecules similarity (7) #174 - Jun 2014 GFP-like Proteins similarity (1) #12 - Dec 2000 Pepsin similarity (1) #209 - May 2017 Tissue Transglutaminase and Celiac Disease similarity (1) #62 - Feb 2005 Major Histocompatibility Complex similarity (1) #63 - Mar 2005 T-Cell Receptor similarity (1) #60 - Dec 2004 Ubiquitin similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#64 - Apr 2005
Kinesin
similarity (11)
#175 - Jul 2014
Microtubules
similarity (7)
#43 - Jul 2003
Src Tyrosine Kinase
similarity (2)
#205 - Jan 2017
Nuclear Pore Complex
similarity (6)
#254 - Feb 2021
Cellulose Synthase
similarity (1)
#18 - Jun 2001
Myosin
similarity (1)
#224 - Aug 2018
Legumain
similarity (1)
#247 - Jul 2020
Myelin-associated Glycoprotein
similarity (1)
#88 - Apr 2007
Clathrin
similarity (1)
#245 - May 2020
Spliceosomes
similarity (1)
#241 - Jan 2020
Twenty Years of Molecules
similarity (7)
#174 - Jun 2014
GFP-like Proteins
similarity (1)
#12 - Dec 2000
Pepsin
similarity (1)
#209 - May 2017
Tissue Transglutaminase and Celiac Disease
similarity (1)
#62 - Feb 2005
Major Histocompatibility Complex
similarity (1)
#63 - Mar 2005
T-Cell Receptor
similarity (1)
#60 - Dec 2004
Ubiquitin
similarity (1)

Deposited unit

B: CLIP-associating protein 2

D: CLIP-associating protein 2

F: Centromere-associated protein E

H: Centromere-associated protein E

C: CLIP-associating protein 2

G: Centromere-associated protein E

A: CLIP-associating protein 2

E: Centromere-associated protein E

hetero molecules

137 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

B: CLIP-associating protein 2

F: Centromere-associated protein E

A: CLIP-associating protein 2

E: Centromere-associated protein E

hetero molecules

defined by author
Evidence: gel filtration
68.6 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: CLIP-associating protein 2

H: Centromere-associated protein E

C: CLIP-associating protein 2

G: Centromere-associated protein E

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

Unit cell

Length a, b, c (Å)	106.221, 106.221, 327.051
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	169
Space group name H-M	P6₁

#1: Protein	CLIP-associating protein 2 / Cytoplasmic linker-associated protein 2 / Protein Orbit homolog 2 / hOrbit2 Mass: 26443.785 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CLASP2, KIAA0627 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O75122
#2: Protein	Centromere-associated protein E / Centromere protein E / CENP-E / Kinesin-7 / Kinesin-related protein CENPE Mass: 7768.564 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CENPE / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q02224
#3: Chemical	ChemComp-ACT / ACETATE ION Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂H₃O₂
#4: Chemical	ChemComp-MLA / MALONIC ACID / DICARBOXYLIC ACID C3 / PROPANEDIOLIC ACID / METHANEDICARBOXYLIC ACID Mass: 104.061 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₃H₄O₄
Has ligand of interest	N

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 3.89 Å³/Da / Density % sol: 68.4 %
Crystal grow	Temperature: 289 K / Method: vapor diffusion, sitting drop / Details: 0.1 M HEPES pH 6.5 and 1.4 M sodium citrate

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

SSRF

/ Beamline: BL18U1 / Wavelength: 0.987 Å

Detector

Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jun 25, 2021

Radiation

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

Radiation wavelength

Wavelength: 0.987 Å / Relative weight: 1

Reflection

Resolution: 3.2→50 Å / Num. obs: 34412 / % possible obs: 99.9 % / Redundancy: 6.3 % / CC_1/2: 0.991 / CC star: 0.998 / R_merge(I) obs: 0.117 / R_pim(I) all: 0.051 / R_rim(I) all: 0.128 / Χ²: 0.888 / Net I/σ(I): 5.2 / Num. measured all: 217234

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique obs	CC_1/2	CC star	R_pim(I) all	R_rim(I) all	Χ²	% possible all
3.2-3.26	6.3	1.035	1705	0.545	0.84	0.449	1.13	0.704	99.9
3.26-3.31	5.8	0.842	1735	0.607	0.869	0.375	0.925	0.73	99.8
3.31-3.38	6	0.716	1673	0.673	0.897	0.315	0.784	0.73	99.9
3.38-3.45	6.6	0.609	1749	0.816	0.948	0.256	0.661	0.752	100
3.45-3.52	6.6	0.487	1716	0.838	0.955	0.205	0.529	0.791	100
3.52-3.6	6.5	0.372	1701	0.905	0.975	0.158	0.405	0.822	100
3.6-3.69	6.5	0.289	1732	0.935	0.983	0.123	0.315	0.841	100
3.69-3.79	6.4	0.236	1746	0.953	0.988	0.101	0.257	0.89	100
3.79-3.91	6.3	0.212	1693	0.96	0.99	0.092	0.232	0.941	100
3.91-4.03	6.1	0.18	1705	0.969	0.992	0.079	0.197	0.939	100
4.03-4.18	5.7	0.155	1716	0.974	0.993	0.07	0.17	1.013	100
4.18-4.34	6.7	0.135	1712	0.977	0.994	0.057	0.146	1.022	100
4.34-4.54	6.6	0.12	1737	0.981	0.995	0.051	0.13	1.077	99.9
4.54-4.78	6.5	0.109	1717	0.988	0.997	0.047	0.118	1.014	100
4.78-5.08	6.4	0.104	1730	0.981	0.995	0.045	0.114	0.992	99.9
5.08-5.47	5.9	0.1	1705	0.984	0.996	0.045	0.11	0.936	99.7
5.47-6.02	6.6	0.104	1728	0.986	0.996	0.044	0.113	0.947	100
6.02-6.89	6.5	0.095	1723	0.99	0.997	0.04	0.103	0.931	99.9
6.89-8.67	6	0.075	1727	0.992	0.998	0.033	0.082	0.841	99.8
8.67-50	6.1	0.07	1762	0.993	0.998	0.031	0.077	0.815	99.5

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Processing

Software

Name	Version	Classification
PHENIX	(1.18.2_3874: ???)	refinement
HKL-2000		data scaling
HKL-2000		data reduction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 3.2→46.89 Å / SU ML: 0.48 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 31.78 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2775	1707	4.99 %
R_work	0.2463	-	-
obs	0.2479	34200	99.74 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 3.2→46.89 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8740	0	15	0	8755

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.002	8863
X-RAY DIFFRACTION	f_angle_d	0.484	11971
X-RAY DIFFRACTION	f_dihedral_angle_d	19.238	3386
X-RAY DIFFRACTION	f_chiral_restr	0.036	1449
X-RAY DIFFRACTION	f_plane_restr	0.004	1516

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 (%)
3.2-3.29	0.3332	139	0.3152	2708	X-RAY DIFFRACTION	100
3.29-3.4	0.3568	140	0.29	2718	X-RAY DIFFRACTION	100
3.4-3.52	0.3231	143	0.2878	2701	X-RAY DIFFRACTION	100
3.52-3.66	0.3348	145	0.2805	2709	X-RAY DIFFRACTION	100
3.66-3.83	0.3274	145	0.2567	2710	X-RAY DIFFRACTION	100
3.83-4.03	0.2969	143	0.2645	2684	X-RAY DIFFRACTION	100
4.03-4.28	0.2787	141	0.2463	2723	X-RAY DIFFRACTION	100
4.28-4.61	0.2866	145	0.2338	2723	X-RAY DIFFRACTION	100
4.61-5.08	0.2583	141	0.2423	2708	X-RAY DIFFRACTION	100
5.08-5.81	0.278	145	0.2676	2697	X-RAY DIFFRACTION	100
5.81-7.31	0.3058	142	0.2798	2714	X-RAY DIFFRACTION	100
7.32-46.89	0.2179	138	0.1969	2698	X-RAY DIFFRACTION	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	0.9146	0.1504	-2.0382	1.4331	-1.7532	5.9411	-0.9982	-0.8152	1.5833	2.39	0.4579	-0.125	-1.1569	0.4025	0.433	1.3216	0.4142	-0.4106	0.5947	-0.5835	1.7447	-14.9936	-15.6274	0.3418
2	6.7691	-1.7868	2.0189	2.3086	-1.8732	2.4843	0.252	-0.7045	0.0617	0.3456	-0.6489	-0.4288	-0.7367	0.7577	0.8455	1.012	-0.0879	-0.0774	1.1003	-0.2761	1.4199	-15.5713	-14.518	-9.3166
3	6.9124	4.3586	1.4687	5.5721	-4.1694	9.5574	-0.9342	-2.7496	2.0065	0.7291	1.0871	1.1508	-0.8454	-1.7776	0.4698	0.8412	0.0433	-0.0512	0.9829	-0.404	0.5564	-14.3279	-25.7307	-4.9095
4	9.1254	-1.1972	-0.0711	8.2836	-0.0176	6.7743	0.0807	-0.0479	1.1093	-0.2553	0.0207	0.5163	-1.4248	-0.2162	-0.0084	0.7819	0.0506	0.0187	0.515	-0.1194	0.563	-15.0458	-26.7254	-18.0147
5	1.7793	0.1033	-1.8381	3.0315	0.7562	4.5642	0.2651	-0.0373	-0.1688	-0.0016	-0.3265	-0.0566	0.6793	-0.1478	0.1443	0.579	0.119	-0.1271	0.6582	-0.039	0.4336	-10.8339	-44.8205	-28.4416
6	6.0336	0.2562	0.4191	3.7383	2.3619	4.0042	0.0238	0.5998	-0.7404	0.1093	-1.4698	-0.6789	-1.2207	-0.8727	0.7036	1.1081	0.0785	0.0529	1.0324	0.0847	0.5688	-6.6799	-47.1024	-42.7116
7	5.0364	-0.4304	-3.1509	7.4547	2.4071	7.1016	-0.6548	0.4339	-1.6142	-0.2915	0.2024	1.0415	1.7476	-0.2707	0.2172	0.9684	-0.1334	-0.0605	0.6842	-0.0868	1.179	-24.0771	-62.1311	-20.5229
8	6.1738	-1.6088	-2.0945	2.6918	2.3206	5.5145	0.1584	-1.2806	-0.2857	0.6093	-0.388	0.2429	-0.4669	0.0153	0.042	0.8537	-0.2003	0.0619	0.9433	0.0145	0.6237	-33.8159	-39.5569	-5.9783
9	2.8952	0.8549	0.8421	3.4471	1.1125	0.3112	-0.46	0.4692	0.9744	0.949	0.5695	0.3867	-0.1141	0.6965	0.0677	1.4442	-0.0148	-0.1548	0.88	0.2005	0.7811	-5.67	-16.1496	-37.6055
10	0.2011	-0.3915	0.5688	1.3287	-1.0641	1.048	-0.3516	-0.1451	-0.5075	-1.059	0.802	0.4696	0.8528	-0.3619	-0.0497	1.7388	-0.0981	0.3865	1.0062	-0.2265	1.5411	-52.4526	-56.1199	-13.9566
11	7.4795	-7.9652	-1.072	9.6571	2.9096	2.8103	-1.3658	2.4253	0.0346	-2.3511	2.9038	-3.0422	0.272	-2.7031	-0.6639	1.0896	-0.7395	-0.1159	1.6293	0.47	1.4493	-90.4832	-71.5192	-8.8291
12	3.2814	-2.5462	1.2308	3.9344	-3.7717	4.5133	-0.7818	-2.8902	-0.5979	-1.8792	0.0417	0.256	-0.3889	0.7671	0.3569	1.933	-0.0321	0.5422	1.3194	0.1908	2.3259	-83.8695	-64.634	0.3972
13	7.0362	0.4667	-4.1699	0.2761	-0.204	3.4409	-0.1753	-0.4249	-1.7969	-2.1155	-0.1818	-1.2518	0.8832	1.0974	-0.2168	1.2511	-0.1283	0.2968	0.4866	-0.0634	2.155	-81.6183	-69.7547	-13.3757
14	7.198	0.4127	-1.7708	6.6703	-0.9984	4.4275	0.3931	0.8464	-1.5704	-0.1471	0.2356	-0.8615	1.5058	0.438	-0.0214	0.9159	0.2408	0.0686	0.645	-0.1299	1.0253	-84.1696	-60.6193	-13.7011
15	5.5791	1.3312	0.9577	5.9028	-1.737	4.1047	0.6767	0.0781	-1.0752	-0.6571	-0.0061	-0.9177	1.386	0.1823	-0.0179	0.7429	-0.0224	0.0556	0.8324	-0.1815	0.7923	-80.0293	-51.9967	-16.71
16	5.7483	0.3082	-0.1261	6.9647	-1.513	2.9834	-0.0158	1.2665	0.2693	-0.6557	-0.0582	-0.3907	0.1859	0.4738	-0.0212	0.7045	0.0477	0.109	0.9245	-0.0175	0.6164	-77.8626	-37.3524	-27.5721
17	3.2639	-1.8266	-1.1835	1.6267	-1.0454	5.2981	0.1042	1.1028	0.3256	-2.0221	-0.9052	-2.027	0.8674	1.9372	0.5583	1.3506	0.1794	0.6221	1.578	0.2949	1.2377	-64.7486	-31.4608	-33.6805
18	1.4302	-1.1741	-0.1471	1.3968	1.3255	2.8399	-0.7979	0.1725	-0.4648	0.6086	1.4885	0.2933	0.8887	-0.748	-0.6021	1.161	-0.1581	0.3745	0.9676	-0.084	1.2374	-59.3591	-56.4375	-18.6246
19	9.6654	3.983	0.8108	6.2208	-3.3948	7.9099	0.2014	0.5396	0.2346	-0.8186	0.1146	-0.4738	-0.1719	0.7395	-0.0347	0.8928	-0.0373	0.3448	0.8225	0.0335	0.7778	-9.1783	-19.62	-80.3225
20	6.8651	1.0568	-3.6497	2.7245	-0.2893	5.2623	-0.0232	0.0873	0.6671	-0.0552	0.1396	-0.2625	-0.0879	0.0616	-0.1392	0.5903	0.1454	-0.1187	0.5643	-0.0122	0.4715	-25.1877	-27.2109	-65.0002
21	9.5723	0.7557	-2.7034	6.4082	-0.2088	3.0707	-0.151	-0.5504	0.2708	0.8447	0.5286	0.5837	0.6652	-0.6642	-0.336	0.8064	0.1111	-0.079	0.8612	0.107	0.4131	-39.2166	-27.7601	-48.922
22	1.9466	1.6925	0.8681	5.0899	2.4408	2.2431	-1.2867	0.2134	0.4233	-2.2455	0.7347	-0.461	-0.689	0.0938	0.3805	1.0936	0.0992	-0.1576	0.9153	0.0083	0.7426	-10.5001	-12.1033	-39.4517

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'B' and (resid 1253 through 1265 )
2	X-RAY DIFFRACTION	2	chain 'B' and (resid 1266 through 1290 )
3	X-RAY DIFFRACTION	3	chain 'B' and (resid 1291 through 1310 )
4	X-RAY DIFFRACTION	4	chain 'B' and (resid 1311 through 1371 )
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 1372 through 1457 )
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 1458 through 1478 )
7	X-RAY DIFFRACTION	7	chain 'D' and (resid 1253 through 1351 )
8	X-RAY DIFFRACTION	8	chain 'D' and (resid 1352 through 1478 )
9	X-RAY DIFFRACTION	9	chain 'F' and (resid 494 through 548 )
10	X-RAY DIFFRACTION	10	chain 'H' and (resid 494 through 548 )
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 1255 through 1265 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 1266 through 1271 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 1272 through 1293 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 1294 through 1331 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 1332 through 1371 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 1372 through 1459 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 1460 through 1477 )
18	X-RAY DIFFRACTION	18	chain 'G' and (resid 496 through 547 )
19	X-RAY DIFFRACTION	19	chain 'A' and (resid 1251 through 1310 )
20	X-RAY DIFFRACTION	20	chain 'A' and (resid 1311 through 1431 )
21	X-RAY DIFFRACTION	21	chain 'A' and (resid 1432 through 1478 )
22	X-RAY DIFFRACTION	22	chain 'E' and (resid 496 through 547 )

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