PDB-9kyp: GH57 family amylopullulanase from Aquifex aeolicus wild type comp...

ID or keywords:

Entry

Database: PDB / ID: 9kyp

Title

GH57 family amylopullulanase from Aquifex aeolicus wild type complex with beta-cyclodextrin

Components

(Glycoside hydrolase family 57 N-terminal domain-containing ...) x 2

Keywords

HYDROLASE / GH57 family / amylopullulanase / Aquifex aeolicus

Function / homology

Function and homology information

catalytic activity / carbohydrate metabolic process
Similarity search - Function

Biological species

Aquifex aeolicus VF5 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.79 Å

Authors

Zhu, Z.M. / Wang, W.W. / Yu, F. / Li, M.J. / Xu, Q. / Zhou, H. / Huang, L.Q. / Wang, Q.S.

Funding support

China, 1items

Citation

Journal: J.Struct.Biol. / Year: 2025
Title: Mechanistic insights into cyclodextrins as substrates and inhibitors of GH57 family amylopullulanase from Aquifex aeolicus.
Authors: Zhu, Z. / Li, M. / Xu, Q. / Huang, L. / Zhou, H. / Wang, W. / Wang, Q. / Yu, F.

History

Deposition	Dec 9, 2024	Deposition site: PDBJ / Processing site: PDBC
Revision 1.0	Jun 4, 2025	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	9kyp.cif.gz	824.9 KB	Display	PDBx/mmCIF format
PDB format	pdb9kyp.ent.gz	684.4 KB	Display	PDB format
PDBx/mmJSON format	9kyp.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/ky/9kyp ftp://data.pdbj.org/pub/pdb/validation_reports/ky/9kyp	HTTPS FTP

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Related structure data

Related structure data	9jltC 9jluC 9jlvC 9kyqC 9kyrC 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	#155 - Nov 2012 Vitamin D Receptor similarity (1) #203 - Nov 2016 Aminopeptidase 1 and Autophagy similarity (2)

Deposited unit

A: Glycoside hydrolase family 57 N-terminal domain-containing protein

B: Glycoside hydrolase family 57 N-terminal domain-containing protein

C: Glycoside hydrolase family 57 N-terminal domain-containing protein

D: Glycoside hydrolase family 57 N-terminal domain-containing protein

hetero molecules

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

1

A: Glycoside hydrolase family 57 N-terminal domain-containing protein

hetero molecules

defined by author
Evidence: native gel electrophoresis
60 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Glycoside hydrolase family 57 N-terminal domain-containing protein

hetero molecules

defined by author
59.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: Glycoside hydrolase family 57 N-terminal domain-containing protein

hetero molecules

defined by author
59.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: Glycoside hydrolase family 57 N-terminal domain-containing protein

hetero molecules

defined by author
59.2 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	40.830, 61.500, 195.540
Angle α, β, γ (deg.)	84.04, 89.46, 89.09
Int Tables number	1
Space group name H-M	P1

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Glycoside hydrolase family 57 N-terminal domain-containing ... , 2 types, 4 molecules ABCD

#1: Protein	Glycoside hydrolase family 57 N-terminal domain-containing protein Mass: 58206.355 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aquifex aeolicus VF5 (bacteria) / Gene: aq_720 / Production host: Escherichia coli (E. coli) / References: UniProt: O66934
#2: Protein	Glycoside hydrolase family 57 N-terminal domain-containing protein / GH57 family amylopullulanase Mass: 57253.234 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aquifex aeolicus VF5 (bacteria) / Gene: aq_720 / Production host: Escherichia coli (E. coli) / References: UniProt: O66934

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Sugars , 1 types, 4 molecules

#3: Polysaccharide

Cycloheptakis-(1-4)-(alpha-D-glucopyranose)

Type: oligosaccharide, Oligosaccharide / Class: Drug delivery / Mass: 1153.001 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: cyclic oligosaccharide / References: beta-cyclodextrin

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Non-polymers , 4 types, 1082 molecules

#4: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 14 Source method: isolated from a genetically manipulated source Formula: C₃H₈O₃
#5: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 9 Source method: isolated from a genetically manipulated source Formula: C₂H₆O₂
#6: Chemical	ChemComp-PEG / DI(HYDROXYETHYL)ETHER Mass: 106.120 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Formula: C₄H₁₀O₃
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1057 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y
Has protein modification	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: 2.13 Å³/Da / Density % sol: 42.31 %
Crystal grow	Temperature: 338 K / Method: vapor diffusion, sitting drop / Details: 0.1M Sodium citrate, pH 4.2, 20% PEG 3350

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: SSRF / Beamline: BL10U2 / Wavelength: 0.97918 Å
Detector	Type: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Nov 10, 2024
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97918 Å / Relative weight: 1
Reflection	Resolution: 1.79→64.83 Å / Num. obs: 169216 / % possible obs: 94.9 % / Redundancy: 3.5 % / CC_1/2: 0.992 / R_merge(I) obs: 0.136 / R_pim(I) all: 0.086 / R_rim(I) all: 0.161 / Χ²: 0.84 / Net I/σ(I): 7.5 / Num. measured all: 584041
Reflection shell	Resolution: 1.79→1.84 Å / % possible obs: 94.3 % / Redundancy: 3.4 % / R_merge(I) obs: 0.954 / Num. measured all: 41650 / Num. unique obs: 12393 / CC_1/2: 0.512 / R_pim(I) all: 0.607 / R_rim(I) all: 1.134 / Χ²: 0.73 / Net I/σ(I) obs: 1.6

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Processing

Software

Name	Version	Classification
PHENIX	(1.13_2998: ???)	refinement
Aimless		data scaling
XDS		data reduction
PHENIX		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.79→24.32 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 19.42 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.189	8300	4.91 %
R_work	0.154	-	-
obs	0.1557	169138	94.92 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 1.79→24.32 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	16088	0	442	1057	17587

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.01	17075
X-RAY DIFFRACTION	f_angle_d	1.038	23130
X-RAY DIFFRACTION	f_dihedral_angle_d	5.473	14172
X-RAY DIFFRACTION	f_chiral_restr	0.062	2487
X-RAY DIFFRACTION	f_plane_restr	0.007	2859

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 (%)
1.79-1.8103	0.316	310	0.2478	5294	X-RAY DIFFRACTION	94
1.8103-1.8316	0.2806	262	0.232	5285	X-RAY DIFFRACTION	94
1.8316-1.854	0.2563	280	0.2123	5403	X-RAY DIFFRACTION	95
1.854-1.8774	0.2372	271	0.2037	5330	X-RAY DIFFRACTION	95
1.8774-1.9021	0.2402	289	0.2025	5250	X-RAY DIFFRACTION	95
1.9021-1.9282	0.2548	283	0.1969	5479	X-RAY DIFFRACTION	95
1.9282-1.9557	0.2165	282	0.1859	5390	X-RAY DIFFRACTION	95
1.9557-1.9849	0.2368	289	0.1808	5359	X-RAY DIFFRACTION	95
1.9849-2.0159	0.2231	263	0.1729	5370	X-RAY DIFFRACTION	95
2.0159-2.0489	0.2143	283	0.1668	5458	X-RAY DIFFRACTION	96
2.0489-2.0842	0.2265	296	0.161	5263	X-RAY DIFFRACTION	95
2.0842-2.1221	0.1886	344	0.1588	5382	X-RAY DIFFRACTION	95
2.1221-2.1629	0.1889	291	0.1566	5375	X-RAY DIFFRACTION	96
2.1629-2.207	0.1915	238	0.1518	5440	X-RAY DIFFRACTION	96
2.207-2.255	0.209	243	0.1576	5479	X-RAY DIFFRACTION	96
2.255-2.3074	0.2042	256	0.1556	5417	X-RAY DIFFRACTION	96
2.3074-2.365	0.1997	293	0.1568	5442	X-RAY DIFFRACTION	96
2.365-2.4289	0.2034	235	0.1621	5415	X-RAY DIFFRACTION	96
2.4289-2.5003	0.2014	292	0.1575	5381	X-RAY DIFFRACTION	96
2.5003-2.5809	0.2001	282	0.1574	5423	X-RAY DIFFRACTION	95
2.5809-2.6731	0.196	281	0.1525	5401	X-RAY DIFFRACTION	95
2.6731-2.78	0.1906	312	0.1547	5281	X-RAY DIFFRACTION	95
2.78-2.9063	0.2043	283	0.154	5351	X-RAY DIFFRACTION	94
2.9063-3.0592	0.1928	257	0.1541	5315	X-RAY DIFFRACTION	94
3.0592-3.2505	0.1949	258	0.1513	5345	X-RAY DIFFRACTION	94
3.2505-3.5008	0.1677	249	0.1442	5277	X-RAY DIFFRACTION	93
3.5008-3.8518	0.1622	271	0.1316	5241	X-RAY DIFFRACTION	93
3.8518-4.4064	0.1329	286	0.1228	5263	X-RAY DIFFRACTION	93
4.4064-5.5407	0.1529	253	0.1319	5370	X-RAY DIFFRACTION	95
5.5407-24.32	0.1733	268	0.1551	5359	X-RAY DIFFRACTION	94

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	0.4035	0.0602	0.126	1.0165	0.4188	1.0432	0.0026	-0.02	-0.0324	0.0182	0.0029	0.1206	0.0523	-0.0483	-0.002	0.0892	-0.011	0.0062	0.1366	-0.0003	0.1605	-22.1907	-31.9787	30.0903
2	0.4527	-0.7313	-0.7559	1.6304	1.3625	2.0165	0.0216	0.0398	-0.1335	-0.3275	-0.1172	0.3572	0.0676	-0.1911	0.0644	0.2014	-0.0155	-0.0387	0.1748	0.0009	0.1917	-27.3418	-39.1414	14.364
3	0.8422	0.2925	0.1909	1.5802	0.9288	1.8022	-0.0603	0.1361	-0.0191	-0.3465	0.0484	-0.3289	0.0095	0.3336	-0.0215	0.2118	0.0135	0.0581	0.2386	-0.0059	0.217	-9.0882	-43.592	11.5555
4	0.4904	-0.3435	-0.3245	1.6035	0.9154	1.7987	0.0128	0.0282	-0.097	0.0043	0.0038	0.0406	0.2445	-0.0501	-0.0082	0.1627	-0.0132	-0.0105	0.1375	0.0084	0.2099	-21.2588	-47.7096	23.5616
5	0.2515	0.0841	0.0375	1.2253	-0.1824	0.9469	-0.0216	-0.0111	0.0306	-0.0182	-0.0162	0.0923	-0.0855	-0.0713	0.0228	0.0954	0.0081	0.005	0.1583	-0.011	0.183	-26.4702	-13.4274	30.0562
6	0.9272	-0.5301	0.0552	1.3376	0.1898	0.8467	-0.0201	0.056	0.0624	0.0854	0.0106	-0.0802	-0.0841	0.0779	-0.0051	0.0993	-0.0185	0.005	0.1601	-0.0021	0.1789	-11.6027	-16.8562	40.336
7	0.9803	0.1972	0.209	1.6397	0.8236	2.1446	0.0444	-0.0972	-0.0556	0.2596	0.0013	-0.1018	0.1174	0.0338	-0.0359	0.1355	-0.0048	-0.0035	0.1492	0.0223	0.1578	-11.7898	-29.8463	44.4539
8	0.8457	-0.0459	-0.1612	1.1682	0.024	1.9303	-0.0394	0.0373	0.0775	-0.1364	-0.0155	-0.0846	-0.1381	0.2117	0.0587	0.1568	-0.0149	0.0005	0.1363	0.0218	0.2024	-17.7272	-9.4795	22.0442
9	1.512	-0.3062	0.24	2.9799	0.0628	2.4803	0.0453	0.065	-0.0515	-0.3413	-0.0338	0.0472	0.0335	0.0438	0.0044	0.1983	-0.0074	-0.0218	0.149	0.0081	0.1593	-23.7315	-19.7233	12.2684
10	0.7157	-0.191	-0.0003	1.092	0.2641	0.4729	-0.0091	-0.0006	0.0251	-0.0073	-0.0369	0.0916	-0.0361	-0.0365	0.0392	0.1683	0.016	-0.0102	0.1376	-0.0049	0.1551	-28.321	-31.7028	-25.0801
11	0.4876	0.4899	-0.0658	0.7056	0.4	1.0428	0.0683	-0.0856	0.0815	0.189	-0.0589	-0.0298	-0.0972	-0.0401	-0.0082	0.2739	0.0022	-0.0099	0.1891	0.0048	0.1704	-21.4307	-22.1079	-5.7344
12	0.6359	0.1907	0.0564	2.1354	1.3769	2.1881	-0.017	0.0452	0.1227	-0.09	0.1117	-0.2564	-0.1961	0.3044	-0.0682	0.2358	-0.0151	0.0085	0.1915	-0.0095	0.2335	-14.3527	-14.8829	-16.3036
13	1.0819	1.0557	1.256	2.573	2.1683	2.4075	-0.0548	-0.069	0.1158	-0.159	-0.1427	0.2732	-0.2071	-0.1849	0.2185	0.2114	0.0472	0.0021	0.1739	0.0166	0.214	-32.1963	-19.5043	-22.8153
14	0.5946	-0.2483	0.133	1.6311	-0.3517	1.2928	0.0679	-0.0455	-0.0994	-0.0183	-0.0077	0.1812	0.1686	-0.1119	-0.055	0.1878	-0.0091	-0.0078	0.184	-0.0091	0.1958	-31.4276	-50.3639	-22.1365
15	1.1226	-0.551	-0.2114	0.903	0.4504	0.7307	0.078	0.1135	-0.0452	-0.0828	-0.0649	0.2072	0.0882	-0.1563	-0.0031	0.2185	-0.0125	-0.0456	0.2023	-0.0029	0.226	-32.8199	-49.6201	-31.3682
16	1.2663	0.8937	-0.1176	1.2825	-0.005	0.7643	-0.1258	0.0134	-0.0561	-0.1992	0.0604	-0.0566	0.0625	0.0625	0.0297	0.1953	0.0383	-0.0104	0.1849	-0.0131	0.1709	-19.3391	-47.3014	-38.5237
17	0.8322	0.0195	-0.0105	1.3857	0.3761	1.3752	0.0461	0.1601	0.0249	-0.1619	-0.0148	-0.0428	0.047	0.0383	-0.0302	0.2347	0.0341	-0.001	0.209	0.0058	0.1576	-19.5947	-34.1135	-42.3931
18	0.987	-0.0413	0.1461	1.2055	-0.2406	1.6888	-0.0064	-0.0307	-0.0255	0.1626	0.0064	-0.0787	0.1931	0.1877	0.0088	0.2231	0.0114	-0.0183	0.14	0.0049	0.2089	-21.9896	-54.2792	-19.2025
19	1.2844	0.3665	0.191	3.2486	-0.0365	1.9707	0.0299	-0.0724	-0.0549	0.3628	-0.0436	-0.0632	0.0173	0.0808	0.0015	0.2037	0.0208	-0.012	0.1433	0.0047	0.1268	-25.8982	-43.9916	-8.5838
20	0.7216	0.0371	-0.0215	1.6879	0.7567	1.1011	-0.0406	0.0264	-0.0513	-0.1566	0.0615	0.1544	0.0118	-0.0645	-0.0117	0.1628	-0.0199	-0.0052	0.1732	0.0058	0.1807	-8.7536	-15.7481	-68.5422
21	0.7753	-0.4903	-0.3907	0.8127	0.3152	1.4425	0.0806	0.0912	-0.0644	-0.3844	-0.0455	0.1595	-0.0052	-0.0282	0.0042	0.4183	-0.0045	-0.0186	0.2577	-0.0019	0.2273	-3.0494	-22.3347	-89.644
22	0.629	-0.3655	-0.6948	1.2836	1.4658	2.0769	-0.0677	0.0321	-0.1357	-0.4381	0.1638	-0.5423	0.2375	0.6769	-0.0468	0.3206	0.0119	0.0674	0.3206	-0.039	0.2615	10.202	-28.5555	-83.0508
23	0.6281	-0.2473	-0.3938	1.5204	0.2299	1.4809	-0.0173	-0.0106	-0.1242	-0.1233	0.0216	0.1213	0.279	-0.0535	0.026	0.2586	-0.0429	-0.0231	0.1954	-0.0039	0.22	-6.1462	-30.726	-76.4407
24	0.7847	-0.2473	-0.0213	1.8627	0.6918	1.8849	0.0003	0.0363	0.0967	-0.1991	0.0388	0.1797	-0.2938	-0.0385	-0.0454	0.2217	0.004	-0.0157	0.2009	0.0104	0.2171	-11.5114	2.4265	-64.9437
25	0.7261	0.0024	-0.297	1.2695	0.155	1.16	-0.0415	-0.1117	0.0577	0.125	0.095	-0.1528	-0.0329	0.2493	-0.0484	0.1859	-0.0106	-0.0203	0.2686	-0.0225	0.2121	3.0699	-8.1728	-53.106
26	0.693	0.2889	0.095	1.557	0.5423	2.3335	-0.0982	-0.173	-0.0571	0.3693	0.0776	0.0418	0.2136	0.0443	0.0113	0.1962	0.0096	-0.0064	0.1831	0.0261	0.1941	-3.1491	-18.0253	-50.3162
27	1.2841	-0.1061	-0.3855	1.6965	-0.2474	2.3417	0.0876	0.0942	0.128	-0.5128	0.1261	-0.1375	-0.3928	0.3224	-0.1402	0.3677	-0.0504	0.0498	0.1524	0.0157	0.2227	-1.5785	7.3018	-71.0678
28	1.1911	-0.1559	-0.1858	3.2905	0.3988	2.6836	0.0265	0.2886	0.0614	-0.6751	0.0198	0.0039	-0.3853	-0.0101	-0.0719	0.4563	-0.0493	-0.0152	0.2331	0.027	0.1815	-6.5467	-1.1176	-82.9675
29	0.6818	-0.1231	-0.1694	1.1551	0.3206	0.6706	-0.0179	-0.0385	0.0256	0.143	0.019	0.0465	-0.0024	-0.094	-0.0059	0.1159	0.014	0.0111	0.1603	-0.0079	0.1513	-4.3198	-47.6993	71.3275
30	0.6732	0.3027	0.3289	1.912	0.615	2.2596	0.0475	-0.1144	0.0665	0.4273	0.0171	-0.0817	-0.2064	0.0415	-0.0691	0.2611	0.0086	0.0057	0.1772	-0.015	0.192	0.6523	-35.6349	85.347
31	0.9011	-0.1968	-0.0159	1.4434	0.2005	1.4625	-0.0113	-0.0064	-0.0742	0.0914	0.0127	0.1002	0.1818	-0.0886	-0.0109	0.1275	-0.0175	0.0151	0.1733	0.0055	0.1696	-7.1415	-65.7738	67.7812
32	1.4304	0.7743	0.0446	1.7567	-0.0998	0.7107	-0.049	-0.1149	-0.0987	-0.1728	-0.0414	-0.2357	0.0428	0.0436	0.0452	0.1268	0.0234	0.0211	0.1894	-0.0063	0.2142	7.4396	-60.6284	57.87
33	0.9009	-0.3135	-0.0781	1.6253	0.3913	2.1066	0.022	0.1016	0.0671	-0.1949	0.0394	-0.1906	-0.0561	0.0903	-0.0684	0.1358	-0.0087	0.0466	0.183	0.0066	0.2012	7.1077	-47.0874	56.1047
34	0.9284	-0.0332	-0.0611	1.7582	-0.1415	1.8205	-0.0465	-0.1369	-0.0803	0.3247	-0.002	-0.1684	0.2051	0.2504	0.0463	0.2095	0.0237	-0.0233	0.1638	0.0142	0.1953	1.8736	-70.8516	74.9484
35	1.8247	0.4082	-0.1625	3.0457	0.3839	2.2018	-0.0108	-0.172	0.0318	0.4641	0.022	-0.0201	0.1142	0.045	-0.0327	0.3455	0.0273	0.0171	0.2156	0.0261	0.1744	-4.3881	-62.4702	86.386

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 2 through 57 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 58 through 88 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 89 through 123 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 124 through 185 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 186 through 278 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 279 through 322 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 323 through 396 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 397 through 435 )
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 436 through 477 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 2 through 68 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 69 through 102 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 103 through 158 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 159 through 185 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 186 through 245 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 246 through 278 )
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 279 through 322 )
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 323 through 396 )
18	X-RAY DIFFRACTION	18	chain 'B' and (resid 397 through 435 )
19	X-RAY DIFFRACTION	19	chain 'B' and (resid 436 through 477 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 2 through 68 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 69 through 102 )
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 103 through 123 )
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 124 through 185 )
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 186 through 278 )
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 279 through 360 )
26	X-RAY DIFFRACTION	26	chain 'C' and (resid 361 through 396 )
27	X-RAY DIFFRACTION	27	chain 'C' and (resid 397 through 435 )
28	X-RAY DIFFRACTION	28	chain 'C' and (resid 436 through 477 )
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 1 through 68 )
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 69 through 185 )
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 186 through 278 )
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 279 through 322 )
33	X-RAY DIFFRACTION	33	chain 'D' and (resid 323 through 396 )
34	X-RAY DIFFRACTION	34	chain 'D' and (resid 397 through 435 )
35	X-RAY DIFFRACTION	35	chain 'D' and (resid 436 through 477 )

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