PDB-5nc6: Crystal structure of the polysaccharide deacetylase Bc1974 from B...

ID or keywords:

Entry

Database: PDB / ID: 5nc6

Title

Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide

Components

(Peptidoglycan N-acetylglucosamine ...) x 2

Keywords

HYDROLASE / CE4 fold / polysaccharide deacetylase /

Bacillus cereus /

PgdA / hydroxamate ligand

Function / homology

Function and homology information

peptidoglycan-N-acetylglucosamine deacetylase / hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / carbohydrate metabolic process /

membrane /

metal ion binding /

plasma membrane
Similarity search - Function

Biological species

Bacillus cereus (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.8 Å

Authors

Giastas, P. / Andreou, A. / Balomenou, S. / Bouriotis, V. / Eliopoulos, E.E.

Citation

Journal: Biochemistry / Year: 2018
Title: Structures of the Peptidoglycan N-Acetylglucosamine Deacetylase Bc1974 and Its Complexes with Zinc Metalloenzyme Inhibitors.
Authors: Giastas, P. / Andreou, A. / Papakyriakou, A. / Koutsioulis, D. / Balomenou, S. / Tzartos, S.J. / Bouriotis, V. / Eliopoulos, E.E.

History

Deposition	Mar 3, 2017	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Feb 21, 2018	Provider: repository / Type: Initial release
Revision 1.1	May 8, 2024	Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_conn Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5nc6.cif.gz	353.8 KB	Display	PDBx/mmCIF format
PDB format	pdb5nc6.ent.gz	290.8 KB	Display	PDB format
PDBx/mmJSON format	5nc6.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/nc/5nc6 ftp://data.pdbj.org/pub/pdb/validation_reports/nc/5nc6	HTTPS FTP

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Related structure data

Related structure data	5n1jC 5n1pC 5nc9C 5ncdC 5nekC 5nelC C: citing same article (ref.)
Similar structure data	5nek-d 5n1j-d 2p97-3 1oqm-d 2fyd-d 4o2f-d 2o54-2 3gj2-d 1u5i-d 5nel-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	#203 - Nov 2016 Aminopeptidase 1 and Autophagy similarity (1)

Deposited unit

A: Peptidoglycan N-acetylglucosamine deacetylase

B: Peptidoglycan N-acetylglucosamine deacetylase

C: Peptidoglycan N-acetylglucosamine deacetylase

D: Peptidoglycan N-acetylglucosamine deacetylase

hetero molecules

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

1

Idetical with deposited unit
defined by software
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	49.358, 118.012, 98.618
Angle α, β, γ (deg.)	90.00, 102.28, 90.00
Int Tables number	4
Space group name H-M	P12₁1

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Peptidoglycan N-acetylglucosamine ... , 2 types, 4 molecules ABCD

#1: Protein	Peptidoglycan N-acetylglucosamine deacetylase / Peptidoglycan-N-acetylglucosamine deacetylase / Polysaccharide deacetylase Mass: 23250.412 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Residues of the N-terminus were not detected / Source: (gene. exp.) Bacillus cereus (bacteria) Gene: AT268_30040, B4155_0776, TQ94_03800, TU58_19865, WR51_09920, WR52_09510 Production host: Escherichia coli (E. coli) / References: UniProt: A0A0A3VTA3, UniProt: Q81EJ6*PLUS
#2: Protein	Peptidoglycan N-acetylglucosamine deacetylase / Peptidoglycan-N-acetylglucosamine deacetylase / Polysaccharide deacetylase Mass: 30719.252 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus cereus (bacteria) Gene: AT268_30040, B4155_0776, TQ94_03800, TU58_19865, WR51_09920, WR52_09510 Production host: Escherichia coli (E. coli) / References: UniProt: A0A0A3VTA3, UniProt: Q81EJ6*PLUS

#1: Protein

Peptidoglycan N-acetylglucosamine deacetylase / Peptidoglycan-N-acetylglucosamine deacetylase / Polysaccharide deacetylase

Mass: 23250.412 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Residues of the N-terminus were not detected / Source: (gene. exp.)

Bacillus cereus (bacteria)
Gene: AT268_30040, B4155_0776, TQ94_03800, TU58_19865, WR51_09920, WR52_09510
Production host:

Escherichia coli (E. coli) / References: UniProt: A0A0A3VTA3, UniProt: Q81EJ6*PLUS

#2: Protein

Peptidoglycan N-acetylglucosamine deacetylase / Peptidoglycan-N-acetylglucosamine deacetylase / Polysaccharide deacetylase

Mass: 30719.252 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Bacillus cereus (bacteria)
Gene: AT268_30040, B4155_0776, TQ94_03800, TU58_19865, WR51_09920, WR52_09510
Production host:

Escherichia coli (E. coli) / References: UniProt: A0A0A3VTA3, UniProt: Q81EJ6*PLUS

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Non-polymers , 6 types, 98 molecules

#3: Chemical	ChemComp-ACT / ACETATE ION / Acetate Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂H₃O₂
#4: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Formula: Zn / Details: Residues of the N-terminus were not detected / Source: (gene. exp.) Bacillus cereus (bacteria) / Production host: Escherichia coli (E. coli)
#5: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂H₆O₂
#6: Chemical	ChemComp-8SQ / 3-naphthalen-1-yl-~{N}-oxidanyl-propanamide Mass: 215.248 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₁₃H₁₃NO₂
#7: Chemical	ChemComp-PGE / TRIETHYLENE GLYCOL / Polyethylene glycol Mass: 150.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₆H₁₄O₄
#8: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 88 / Source method: isolated from a natural source / Formula: H₂O

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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 Å³/Da / Density % sol: 58.95 %
Crystal grow	Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 5.6 / Details: 100 mM Na citrate, 10% ethanol, 30% PEG 4000

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
Detector	Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jun 14, 2015
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1 Å / Relative weight: 1
Reflection	Resolution: 2.8→47.35 Å / Num. obs: 52715 / % possible obs: 99.46 % / Redundancy: 4.6 % / B_iso Wilson estimate: 49.47 Å² / Net I/σ(I): 1.2
Reflection shell	Resolution: 2.8→2.9 Å / Redundancy: 4.2 % / Num. unique obs: 2630 / % possible all: 95.4

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Processing

Software

Name	Version	Classification
PHENIX	(1.11.1_2575: ???)	refinement
XDS		data reduction
XDS		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.8→47.346 Å / SU ML: 0.59 / Cross valid method: FREE R-VALUE / σ(F): 0.95 / Phase error: 33.85

	R_factor	Num. reflection	% reflection
R_free	0.2801	2633	4.99 %
R_work	0.22	-	-
obs	0.2234	52715	98.48 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 2.8→47.346 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	6585	0	54	88	6727

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.015	6844
X-RAY DIFFRACTION	f_angle_d	1.178	9233
X-RAY DIFFRACTION	f_dihedral_angle_d	4.769	4440
X-RAY DIFFRACTION	f_chiral_restr	0.056	956
X-RAY DIFFRACTION	f_plane_restr	0.008	1204

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 (%)
2.8003-2.8512	0.4271	127	0.3856	2302	X-RAY DIFFRACTION	86
2.8512-2.9061	0.3753	142	0.3506	2748	X-RAY DIFFRACTION	99
2.9061-2.9654	0.4128	137	0.3251	2562	X-RAY DIFFRACTION	99
2.9654-3.0298	0.3818	141	0.3182	2644	X-RAY DIFFRACTION	99
3.0298-3.1003	0.4198	142	0.3276	2717	X-RAY DIFFRACTION	100
3.1003-3.1778	0.3289	135	0.2967	2598	X-RAY DIFFRACTION	100
3.1778-3.2637	0.4088	141	0.2652	2681	X-RAY DIFFRACTION	100
3.2637-3.3597	0.3357	140	0.2517	2671	X-RAY DIFFRACTION	100
3.3597-3.4681	0.3295	141	0.236	2664	X-RAY DIFFRACTION	99
3.4681-3.592	0.2726	141	0.2253	2643	X-RAY DIFFRACTION	99
3.592-3.7358	0.3132	138	0.2099	2670	X-RAY DIFFRACTION	99
3.7358-3.9058	0.2655	136	0.1981	2632	X-RAY DIFFRACTION	99
3.9058-4.1116	0.2631	142	0.179	2705	X-RAY DIFFRACTION	99
4.1116-4.369	0.295	138	0.1674	2629	X-RAY DIFFRACTION	99
4.369-4.7061	0.2165	138	0.1659	2642	X-RAY DIFFRACTION	99
4.7061-5.1791	0.2387	137	0.1722	2619	X-RAY DIFFRACTION	98
5.1791-5.9273	0.2552	140	0.1813	2647	X-RAY DIFFRACTION	98
5.9273-7.4631	0.2184	137	0.2044	2636	X-RAY DIFFRACTION	100
7.4631-47.3528	0.2279	140	0.2009	2672	X-RAY DIFFRACTION	99

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	2.0466	-1.1542	-0.2796	4.8619	-2.4512	1.73	0.9066	-0.2442	-0.7238	-1.537	0.232	-0.0339	1.1897	0.5612	-0.5717	0.4907	0.0562	0.0641	0.733	-0.1446	0.3834	19.4993	-1.5565	88.7134
2	4.5665	-0.4014	-0.0749	5.759	-0.3034	5.7013	-0.0954	0.9146	-0.4922	-0.8738	0.465	-0.1031	1.604	0.8216	-0.187	0.6999	0.1325	-0.0684	0.5968	-0.1528	0.4938	19.5924	-6.8771	84.2576
3	1.2173	-0.201	-1.1373	1.1757	1.4026	2.9216	0.3638	0.1209	-0.3888	-0.5788	-0.013	0.3037	0.6069	-0.0277	0.32	1.0956	-0.0072	-0.2204	0.4299	-0.0499	0.6197	9.3788	-11.0024	89.4962
4	0.9209	0.8495	1.7822	1.6566	0.2664	5.8163	0.7276	-0.3736	-0.2445	-0.0848	0.0718	0.1901	1.8852	-0.0859	-0.5409	0.6007	-0.0206	-0.0575	0.3866	-0.0557	0.5152	11.8414	-4.628	101.6452
5	1.2396	0.1877	0.0955	1.6037	-0.6182	1.864	0.1792	0.0074	-0.0687	-0.571	0.151	0.1147	0.3762	0.1435	-0.2296	0.4812	0.0632	-0.0646	0.3479	-0.0605	0.4147	18.0615	5.309	100.0138
6	1.9858	-0.4528	1.4386	4.5788	-1.3515	4.3333	0.2513	0.2303	0.032	-0.9781	-0.1952	-0.3239	-0.6754	1.2662	-0.0604	0.615	-0.0928	0.1294	0.6837	-0.1176	0.4175	24.2383	6.6674	85.7616
7	2.4281	0.332	0.0403	0.9681	-0.263	1.5417	0.201	0.676	0.0179	-0.2933	0.1511	-1.1628	0.6778	1.3084	-0.2645	0.6308	0.0661	0.0949	1.0155	-0.3242	0.6997	27.6779	-2.0626	86.1499
8	0.8989	-0.411	-1.2107	2.0376	-0.7567	2.6199	0.2162	0.0487	-0.7057	0.2656	0.131	-0.5259	0.4602	1.3746	-0.3783	0.4624	0.1201	-0.1987	0.4891	-0.1244	0.687	26.6185	1.7145	106.7702
9	2.5093	2.3883	1.9052	2.4256	1.4876	3.6279	-0.2333	0.2817	0.1786	0.5818	0.2137	-0.5182	0.9504	0.8732	-0.0175	0.5327	0.1198	-0.1687	0.5239	-0.0248	0.5564	32.4012	5.065	129.0888
10	2.751	1.4335	-0.7717	2.6991	0.1959	3.1401	0.3261	-0.1032	-0.423	0.4377	-0.0826	0.2385	0.5392	0.0902	-0.271	0.6147	0.0111	-0.0953	0.3768	0.0807	0.415	21.3782	5.4493	136.086
11	0.1265	0.154	-0.0097	2.8011	-0.7464	0.2206	0.2341	-0.1124	-0.0186	0.9097	-0.0426	0.1755	-0.1271	0.0023	-0.0993	1.1738	-0.0256	-0.0946	0.4288	0.0645	0.5404	19.8571	6.0236	143.3602
12	4.6246	0.3651	0.5139	5.478	-0.9701	2.083	0.6343	-0.3653	0.339	0.3276	0.0106	1.7237	0.2723	-0.7541	-0.5956	0.7204	-0.1487	0.1229	0.456	-0.0248	0.5608	17.2522	21.3009	144.8039
13	2.4138	0.1268	-1.0163	2.3199	0.4275	1.9618	0.113	-0.1637	0.038	0.6091	-0.1246	-0.2158	0.3748	-0.298	-0.1534	0.4425	-0.0544	-0.0974	0.3059	0.0305	0.5477	25.2746	16.3854	128.8991
14	0.0954	0.46	0.4588	2.7389	-0.4165	3.678	0.1866	0.0133	0.2287	-0.168	-0.1187	-0.6039	-0.0102	0.5106	-0.042	0.2525	0.0188	-0.0123	0.4786	-0.0804	0.5495	34.3472	13.9649	124.0072
15	3.0027	2.014	-3.6998	3.4149	-2.1596	5.1415	0.357	-0.8291	-0.983	1.8112	-0.2719	-1.2302	-0.5885	0.8741	0.0692	0.6989	0.0199	-0.3056	0.7204	-0.0546	0.678	38.886	11.3104	138.7384
16	3.0289	0.3631	-0.4545	0.4143	-0.2567	3	0.504	-0.1831	0.6394	1.0896	-0.1979	-0.2532	0.0945	0.7842	-0.3615	0.9846	-0.0318	-0.174	0.4652	-0.1003	0.5305	27.3185	22.2891	144.7053
17	1.7072	-0.8098	-0.3884	2.7759	0.6581	3.7732	-0.4091	-0.2198	0.2656	0.593	0.2488	-0.4545	-0.7614	0.1441	0.1117	0.7018	0.0141	-0.0646	0.4504	-0.0542	0.4291	28.1322	45.6723	141.3872
18	2.3892	-1.0992	0.4067	0.491	-0.0645	1.4496	-0.2833	-0.2366	0.4008	0.6851	-0.1039	-0.0291	-0.8935	-0.211	0.4518	0.7642	0.0155	0.0209	0.3591	-0.0374	0.3072	23.5486	40.2159	128.0996
19	2.6621	-0.8992	1.704	2.1468	0.3187	4.2361	0.0012	0.0787	-0.1508	0.8142	0.1829	-0.6913	0.4969	0.7504	-0.2462	0.813	0.0782	-0.2584	0.5754	-0.0997	0.7295	39.0516	34.6004	142.3632
20	2.8481	0.3519	0.7245	2.6912	0.7174	2.607	-0.1028	0.1322	0.4235	-0.2688	0.4093	-0.7113	-0.552	0.8026	-0.1086	0.6732	-0.1017	0.0311	0.5455	-0.1384	0.5582	36.951	42.3128	128.1961
21	3.1997	-1.2511	-0.5795	2.5371	1.9518	2.5294	0.1619	0.5937	-0.3109	-1.4557	0.2316	-0.1648	-0.1663	-0.281	-0.0521	0.7202	-0.2294	0.1181	0.5024	0.0235	0.4116	22.8535	27.8865	96.7664
22	1.1246	-0.3201	1.1891	1.0964	0.5411	2.2819	-0.5478	0.1385	0.4596	-0.249	0.0951	-0.2572	-1.3391	0.6966	0.1253	0.8946	-0.2618	-0.0873	0.4971	0.0394	0.3522	23.1106	37.6903	102.166
23	2.6669	0.4169	-1.5665	0.7376	0.4455	2.0484	-0.1532	0.2386	0.2339	0.3208	-0.1158	0.194	-1.3787	-0.0168	0.1341	1.1523	0.0067	-0.196	0.4175	0.0532	0.5235	13.3608	42.754	102.5906
24	1.8193	0.3469	0.7337	3.6834	0.568	4.4783	0.0445	-0.3281	-0.6832	-0.667	-0.6295	0.8126	-1.3188	0.3807	-0.0219	-0.1473	0.0732	0.1552	0.4945	0.0597	0.532	6.171	28.8692	102.7597
25	0.0884	-0.0937	-0.01	3.3211	-0.389	0.1182	-0.3782	0.2809	0.291	-1.0078	0.0759	0.4402	-0.3454	-0.3255	0.1098	0.8045	0.0113	-0.1662	0.4092	0.0116	0.5414	5.736	33.9282	96.567
26	4.2448	-0.764	-0.1158	5.3946	-1.8138	7.5491	0.0639	-0.2425	-0.953	-0.4489	0.7843	0.9416	-0.4314	-0.3569	-0.5992	0.4517	-0.0418	-0.0568	0.3044	0.0307	0.5404	2.7635	18.7386	96.9426
27	1.7225	0.279	1.6284	1.354	0.1144	2.0282	0.1429	0.1246	-0.2623	-0.1373	0.1818	-0.0717	-0.3773	0.0812	-0.3232	0.336	-0.0965	0.1271	0.3785	0.0073	0.424	22.9448	23.8199	105.4076
28	0.3854	-0.5061	0.5522	2.5385	0.7824	4.9008	0.1716	0.4311	0.1325	-0.6999	0.3238	-0.1276	-1.4442	1.1118	-0.5119	0.6388	-0.1491	-0.0077	0.5457	-0.0066	0.511	27.6953	29.3571	96.9836
29	4.8301	1.4732	-0.6812	0.8575	0.9442	3.4518	-0.5599	0.3397	-0.3261	-0.9607	0.1516	-0.0162	-0.565	0.0847	0.4399	0.5963	-0.1128	-0.0328	0.4632	-0.065	0.38	11.344	17.695	91.402

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 69 through 82 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 83 through 102 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 103 through 118 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 119 through 166 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 167 through 204 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 205 through 233 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 234 through 261 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 262 through 273 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 68 through 93 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 94 through 140 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 141 through 166 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 167 through 183 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 184 through 204 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 205 through 249 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 250 through 261 )
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 262 through 273 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 68 through 156 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 157 through 183 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 184 through 249 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 250 through 273 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 68 through 78 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 79 through 102 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 103 through 118 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 119 through 140 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 141 through 166 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 167 through 183 )
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 184 through 233 )
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 234 through 261 )
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 262 through 273 )

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