PDB-5ux9: The crystal structure of chloramphenicol acetyltransferase from V...

ID or keywords:

Entry

Database: PDB / ID: 5ux9

Title

The crystal structure of chloramphenicol acetyltransferase from Vibrio fischeri ES114

Components

Chloramphenicol acetyltransferase

Keywords

TRANSFERASE /

Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID

Function / homology

Function and homology information

chloramphenicol O-acetyltransferase /

chloramphenicol O-acetyltransferase activity
Similarity search - Function

Biological species

Vibrio fischeri (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

SAD / Resolution: 2.7 Å

Authors

Tan, K. / Zhou, M. / Anderson, W.F. / Joachimiak, A. / Center for Structural Genomics of Infectious Diseases (CSGID)

Funding support

United States, 1items

Citation

Journal: To Be Published
Title: The crystal structure of chloramphenicol acetyltransferase from Vibrio fischeri ES114
Authors: Tan, K. / Zhou, M. / Anderson, W.F. / Joachimiak, A.

History

Deposition	Feb 22, 2017	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 8, 2017	Provider: repository / Type: Initial release
Revision 1.1	Sep 20, 2017	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2	Dec 11, 2019	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5ux9.cif.gz	351.6 KB	Display	PDBx/mmCIF format
PDB format	pdb5ux9.ent.gz	302 KB	Display	PDB format
PDBx/mmJSON format	5ux9.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/ux/5ux9 ftp://data.pdbj.org/pub/pdb/validation_reports/ux/5ux9	HTTPS FTP

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Related structure data

Similar structure data	6pxa-3 6pxa-1 6pxa-2 6mfk-2 6pxa-4 3hin-3 1k39-d 6pub-1 3a73-1 5ifo-d Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search
Other databases	TargetTrack: CSGID-IDP07301

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#39 - Mar 2003 lac Repressor similarity (5) #165 - Sep 2013 Designed Protein Cages similarity (3) #49 - Jan 2004 Carbonic Anhydrase similarity (3)

Deposited unit

A: Chloramphenicol acetyltransferase

B: Chloramphenicol acetyltransferase

C: Chloramphenicol acetyltransferase

D: Chloramphenicol acetyltransferase

hetero molecules

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

1

A: Chloramphenicol acetyltransferase

B: Chloramphenicol acetyltransferase

C: Chloramphenicol acetyltransferase

hetero molecules

defined by author&software
76.4 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: Chloramphenicol acetyltransferase

hetero molecules

D: Chloramphenicol acetyltransferase

hetero molecules

D: Chloramphenicol acetyltransferase

hetero molecules

defined by author&software
76.7 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	147.426, 147.426, 101.211
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	173
Space group name H-M	P6₃

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Protein , 1 types, 4 molecules ABCD

#1: Protein	Chloramphenicol acetyltransferase / Mass: 25027.289 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio fischeri (strain ATCC 700601 / ES114) (bacteria) Strain: ATCC 700601 / ES114 / Gene: VF_A0790 / Plasmid: pMCSG53 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)magic References: UniProt: Q5DZD6, chloramphenicol O-acetyltransferase

#1: Protein

Chloramphenicol acetyltransferase /

Mass: 25027.289 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Vibrio fischeri (strain ATCC 700601 / ES114) (bacteria)
Strain: ATCC 700601 / ES114 / Gene: VF_A0790 / Plasmid: pMCSG53 / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21(DE3)magic
References: UniProt: Q5DZD6,

chloramphenicol O-acetyltransferase

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Non-polymers , 6 types, 109 molecules

#2: Chemical	ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer) Mass: 195.237 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₆H₁₃NO₄S / Comment: pH buffer*YM
#3: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#4: Chemical	ChemComp-ACT / ACETATE ION / Acetate Mass: 59.044 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₂H₃O₂
#5: Chemical	ChemComp-CL / CHLORIDE ION / Chloride Mass: 35.453 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Cl
#6: Chemical	ChemComp-FMT / FORMIC ACID / Formic acid Mass: 46.025 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: CH₂O₂
#7: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 86 / 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: 3.21 Å³/Da / Density % sol: 61.65 %
Crystal grow	Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.2 M Magnesium Chloride, 0.1 M MES:NaOH, 10% (w/v) PEG4000

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97919 Å
Detector	Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Feb 8, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97919 Å / Relative weight: 1
Reflection	Resolution: 2.7→50 Å / Num. obs: 34158 / % possible obs: 99.1 % / Observed criterion σ(I): -3 / Redundancy: 4.2 % / B_iso Wilson estimate: 38.1 Å² / R_merge(I) obs: 0.055 / R_pim(I) all: 0.027 / Χ²: 0.672 / Net I/σ(I): 21.6
Reflection shell	Resolution: 2.7→2.75 Å / Redundancy: 4.1 % / R_merge(I) obs: 0.779 / Mean I/σ(I) obs: 2.5 / Num. unique obs: 1724 / CC_1/2: 0.705 / R_pim(I) all: 0.4 / Χ²: 0.82 / % possible all: 99.4

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Processing

Software

Name	Version	Classification
PHENIX	(1.11.1_2575)	refinement
HKL-3000		data reduction
HKL-3000		data scaling
HKL-3000		phasing

Refinement

Method to determine structure:

SAD / Resolution: 2.7→47.045 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 24.7

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2397	1625	4.82 %	random
R_work	0.2	-	-	-
obs	0.2018	33713	97.86 %	-

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 2.7→47.045 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	6715	0	109	86	6910

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.003	6982
X-RAY DIFFRACTION	f_angle_d	0.568	9455
X-RAY DIFFRACTION	f_dihedral_angle_d	6.963	3998
X-RAY DIFFRACTION	f_chiral_restr	0.05	990
X-RAY DIFFRACTION	f_plane_restr	0.005	1210

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 (%)
2.7003-2.7797	0.3545	112	0.2922	2349	X-RAY DIFFRACTION	86
2.7797-2.8694	0.34	161	0.291	2618	X-RAY DIFFRACTION	98
2.8694-2.972	0.3131	157	0.2792	2690	X-RAY DIFFRACTION	99
2.972-3.091	0.3793	143	0.275	2697	X-RAY DIFFRACTION	99
3.091-3.2316	0.2727	147	0.2535	2683	X-RAY DIFFRACTION	99
3.2316-3.4019	0.2783	137	0.2154	2709	X-RAY DIFFRACTION	100
3.4019-3.615	0.2559	123	0.2106	2736	X-RAY DIFFRACTION	99
3.615-3.894	0.2509	141	0.1966	2704	X-RAY DIFFRACTION	99
3.894-4.2856	0.2061	97	0.1706	2738	X-RAY DIFFRACTION	99
4.2856-4.9052	0.1652	125	0.1455	2702	X-RAY DIFFRACTION	98
4.9052-6.1778	0.1891	138	0.1639	2738	X-RAY DIFFRACTION	99
6.1778-47.0519	0.1711	144	0.1656	2724	X-RAY DIFFRACTION	97

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	4.0112	1.3741	-4.1036	0.5785	-1.8858	7.2775	0.2232	0.0847	0.4949	0.0884	0.0803	0.4934	-0.9635	0.0119	-0.1768	0.5065	0.0338	0.2638	0.2648	-0.0543	0.8236	63.932	87.0861	87.2209
2	3.0132	-1.4856	-0.4748	0.8981	0.55	2.002	0.2577	-0.1734	0.8897	-0.1365	0.0368	0.1016	-0.3032	0.5648	-0.2635	0.5093	-0.0574	0.214	0.363	-0.1807	0.7183	71.7609	85.7276	88.8758
3	7.3242	-0.4386	0.9667	2.1453	0.8329	1.6965	0.0356	0.6959	0.2128	-0.2817	0.1654	-0.4186	-0.6511	0.5567	-0.1936	0.4523	-0.0927	0.2033	0.5289	-0.1319	0.5493	74.8431	82.7286	78.8674
4	4.5812	-0.0176	0.8547	0.6023	-0.0468	0.6471	0.0931	0.1907	0.1609	-0.084	0.0184	-0.1203	-0.1536	0.2396	-0.1295	0.3098	-0.0289	0.1076	0.3148	-0.1382	0.4103	79.0358	73.0916	85.2993
5	7.2198	-4.9309	4.3864	6.0637	-5.0327	4.2702	0.9696	0.8255	-1.1526	-0.1148	0.4065	0.3613	0.4659	0.6181	-1.0646	0.3107	0.1562	0.0328	0.3711	-0.1905	0.4265	62.8883	60.5592	83.0292
6	3.4975	3.6629	-1.2822	6.4715	0.2675	4.3807	0.3278	0.6794	-0.1657	-0.5777	-0.126	0.1447	0.1361	0.6085	-0.1835	0.2699	0.1311	-0.0568	0.4856	-0.0793	0.3836	55.8838	70.0192	70.1803
7	3.582	-4.5413	0.3014	6.5083	-1.8417	6.653	0.1686	0.1611	-0.2562	-0.2494	0.3514	1.5686	-0.5313	-0.8285	-0.481	0.3662	0.1583	0.0114	0.4537	0.0342	0.6875	45.9694	75.5652	75.3706
8	6.5899	-3.7867	4.7761	7.55	-3.8802	8.3222	0.2081	0.3605	-0.2987	-0.2928	0.1611	1.0445	0.1066	-0.6086	-0.4407	0.4129	0.1677	-0.1038	0.5035	-0.0877	0.6455	46.4737	70.7086	66.4865
9	2.0163	-0.4226	2.1912	0.1433	-0.8566	2.7857	-0.5042	-0.0105	1.1595	0.3863	0.4143	-0.7133	-0.5267	0.795	0.0795	0.8465	-0.133	0.2014	0.7709	-0.4353	0.8413	89.549	85.2242	99.8557
10	0.0467	0.2369	0.1238	1.3931	-0.7956	4.4483	0.1727	-0.193	-0.1855	1.1503	-0.1459	-0.4266	0.1972	0.6531	-0.1626	0.621	-0.0876	0.0696	0.7752	-0.3676	0.5958	95.1552	76.9362	109.5793
11	7.0456	-1.426	0.6567	3.9228	-1.1697	0.2706	-0.4867	-0.7739	0.9672	0.6733	0.2987	-0.1594	-0.1282	0.0722	0.1242	0.5219	-0.0521	0.0572	0.5624	-0.2596	0.5094	83.3452	81.2159	102.2722
12	1.8288	0.0108	-0.7804	1.4512	1.1712	3.788	-0.1478	-1.5333	0.8324	1.0011	0.0427	0.1991	0.1537	0.0379	0.1566	0.8794	-0.0487	0.0739	0.9139	-0.3294	0.6124	84.7377	74.958	120.5246
13	0.7722	1.1243	-1.4437	1.4288	-1.0101	1.9488	0.3151	-0.5764	0.3206	0.6575	-0.0687	0.0277	-0.3439	0.2482	-0.2097	0.5519	-0.0254	0.0565	0.6739	-0.2152	0.3761	79.2798	66.3907	114.9634
14	4.9003	-0.2656	-5.8413	1.5237	-1.3937	9.0762	-0.0029	-0.8003	0.5354	0.9906	-0.3998	-0.4739	0.6452	0.2398	0.0106	0.6988	-0.1178	0.0747	0.981	-0.2387	0.3842	79.9778	61.8182	124.4598
15	1.9838	-0.1807	1.337	2.5086	-0.3676	3.5175	-0.3823	0.0538	-0.1446	0.1885	0.3198	-0.0087	0.3483	-0.2046	0.0656	0.431	-0.0803	0.0851	0.4553	-0.227	0.3453	86.819	67.9452	101.9377
16	4.5543	-1.209	-0.8104	2.1158	0.0276	2.4107	0.0951	0.1092	-0.1253	0.3781	-0.1435	0.033	0.2682	-0.1015	0.0233	0.2838	-0.0309	0.0214	0.3608	-0.1853	0.3396	87.7643	62.3462	98.7202
17	6.9242	1.1431	-0.2465	1.6195	-0.08	2.6973	-0.1583	0.1966	-0.5921	0.1052	0.1071	-0.3462	0.2793	0.4867	0.0377	0.2996	0.0611	0.0173	0.4216	-0.1802	0.4159	98.92	61.3779	93.9707
18	4.7234	0.8718	0.855	1.3816	-1.232	1.5772	-0.1469	0.3727	-0.3345	-0.0601	0.207	-0.6873	-0.7156	0.3447	0.0589	0.3346	-0.1792	0.0662	0.7188	-0.254	0.7037	107.2886	73.7662	88.5524
19	6.8536	2.1623	-1.3746	5.3321	-3.2036	2.5499	-0.3521	0.1488	-0.5927	-0.6995	0.292	-1.9266	0.6817	1.1425	0.3803	0.2291	-0.059	0.1195	0.9993	-0.3358	0.8968	113.2099	65.1497	89.5155
20	6.8432	-0.955	-1.3044	-0.0518	0.3297	0.3611	-0.3066	-1.1759	1.3175	0.305	0.1244	0.1539	-0.0349	0.1566	0.0947	0.6624	0.0184	0.2112	0.649	-0.2716	0.6663	61.7566	76.149	117.3172
21	1.8135	-0.4098	1.6015	0.0106	-0.1492	1.4366	-0.1024	-0.6142	0.7162	0.1622	0.1885	-0.0496	-0.087	0.0572	-0.0344	0.5228	0.0531	0.1783	0.4353	-0.1696	0.5732	59.6434	77.7948	109.7963
22	4.6774	-3.6725	5.8868	5.2777	-5.2157	8.3133	0.1745	-0.3502	-0.255	0.1696	0.4996	0.8092	0.0237	-0.2796	-0.6834	0.3903	0.0232	0.1751	0.3595	-0.0579	0.5273	51.026	70.6829	109.0127
23	0.2754	0.3459	1.2024	0.1816	-0.4064	2.1629	0.0793	-0.0709	-0.0587	0.1369	0.1757	0.1128	-0.2003	-0.1177	-0.1415	0.3076	0.0883	0.1124	0.3592	-0.094	0.544	56.7854	69.9833	96.2121
24	1.3061	-0.0819	1.1055	0.1661	0.2114	1.4466	0.2145	0.0837	0.2831	0.4567	0.1291	0.4253	-0.6256	-0.6755	-0.297	0.4765	0.1306	0.1546	0.4193	-0.1098	0.8365	47.8745	75.4562	87.7524
25	2.1387	0.5656	1.5741	2.8133	-1.018	1.523	0.1474	-0.2546	0.3064	0.2034	0.1742	0.2106	-0.003	0.2817	-0.3213	0.4114	0.042	0.1336	0.3533	-0.16	0.3168	63.416	60.957	107.5648
26	6.0802	1.0523	-2.3498	6.0362	-7.1503	8.7826	0.0143	-0.3593	-0.1803	-0.5869	-0.1774	0.069	1.2319	0.5408	0.1239	0.4429	0.0283	0.0753	0.3188	-0.115	0.2887	68.2018	51.7228	108.3643
27	6.3635	-5.5357	2.433	2.0942	-3.5671	1.251	0.0552	-0.4243	-0.1034	-0.8257	-0.1005	0.1165	-0.1601	-0.4303	0.0976	0.4986	0.0035	0.0281	0.441	0.0011	0.2896	59.3081	46.803	119.6331
28	3.2462	-0.3513	-2.7623	3.8243	4.2963	6.675	-0.032	-1.3197	-0.0643	1.222	-0.1461	0.275	-0.1237	-0.0607	0.1389	0.8243	-0.0114	0.1353	0.6992	-0.0188	0.3127	62.3366	56.6298	129.7546
29	5.5579	1.0645	-5.0718	4.4181	0.0331	8.4987	0.0793	-0.7349	-0.4353	0.5594	0.0193	0.169	0.3491	-0.3042	-0.0363	0.7468	-0.0311	0.1524	0.9683	-0.0817	0.3018	59.2691	47.8809	131.8197
30	2.3457	3.1681	1.6733	2.602	0.7837	0.9352	-0.4667	0.4945	0.1388	-1.2911	0.676	0.217	0.209	-0.3429	-0.1835	0.4733	0.0232	-0.0492	0.5257	-0.034	0.2698	56.272	40.963	46.9529
31	4.396	1.3233	-0.7312	2.1909	-1.3767	1.5326	0.0239	-0.1271	-0.212	0.0023	-0.0718	-0.0962	-0.2294	0.1704	0.009	0.3949	0.0431	-0.0413	0.3633	-0.0519	0.1144	59.5744	42.1886	50.1527
32	6.4893	3.3179	0.1553	5.0377	1.8337	6.0947	-0.55	1.2637	-0.7093	-1.1015	0.5479	0.1375	0.2736	0.2212	0.0428	0.4412	-0.0508	-0.0309	0.3732	-0.1005	0.3009	62.9449	25.45	47.9091
33	4.7948	-1.7686	-0.4157	7.3063	1.9361	5.334	-0.3054	0.1106	-0.8991	-0.2939	0.473	0.1931	0.8988	-0.1737	-0.0891	0.4459	-0.0908	0.0001	0.2873	-0.0008	0.2482	55.5713	27.5241	55.7429
34	1.0531	-1.667	1.3048	2.3282	-1.1477	1.2589	0.2612	0.0838	-0.2422	-0.4704	-0.091	0.0933	0.4186	-0.1438	-0.1617	0.3047	-0.0261	-0.0468	0.2102	-0.0507	0.2338	68.814	27.165	60.8104
35	1.8432	-1.8484	1.18	3.9603	-0.6395	0.7181	0.1	0.6172	-0.7343	-0.2336	0.0399	0.234	0.0448	-0.1025	-0.1349	0.4451	0.045	-0.0732	0.3663	-0.108	0.3148	73.8157	14.8274	58.0975
36	2.0726	0.1459	-0.8029	3.6583	0.3102	1.8062	-0.0472	-0.1782	-0.1158	0.1834	0.1334	-0.1769	-0.0691	-0.1779	-0.1273	0.2294	0.0149	-0.0568	0.2733	0.0073	0.1106	59.5832	39.0525	65.8748
37	3.8276	-1.0803	-0.7454	1.833	-0.1338	2.1557	-0.0555	-0.3828	-0.0958	0.2607	0.2695	0.2414	-0.126	-0.3893	-0.2016	0.2715	0.047	-0.0295	0.3154	0.0817	0.2084	44.7455	45.9977	68.1354
38	2.1548	-0.2484	3.8493	1.6241	0.8153	4.9165	0.3498	-0.8889	0.6394	0.7457	0.0453	0.8865	-0.0434	-1.8095	-0.2023	0.3291	0.1873	0.1754	0.7145	0.2594	0.502	33.3822	47.5389	69.7925

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 3 through 24 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 25 through 58 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 59 through 75 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 76 through 162 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 163 through 173 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 174 through 189 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 190 through 204 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 205 through 217 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 3 through 16 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 17 through 28 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 29 through 42 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 43 through 67 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 68 through 105 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 106 through 118 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 119 through 136 )
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 137 through 162 )
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 163 through 189 )
18	X-RAY DIFFRACTION	18	chain 'B' and (resid 190 through 204 )
19	X-RAY DIFFRACTION	19	chain 'B' and (resid 205 through 217 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 3 through 24 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 25 through 58 )
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 59 through 75 )
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 76 through 95 )
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 96 through 118 )
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 119 through 162 )
26	X-RAY DIFFRACTION	26	chain 'C' and (resid 163 through 173 )
27	X-RAY DIFFRACTION	27	chain 'C' and (resid 174 through 183 )
28	X-RAY DIFFRACTION	28	chain 'C' and (resid 184 through 204 )
29	X-RAY DIFFRACTION	29	chain 'C' and (resid 205 through 217 )
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 1 through 24 )
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 25 through 42 )
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 43 through 58 )
33	X-RAY DIFFRACTION	33	chain 'D' and (resid 59 through 75 )
34	X-RAY DIFFRACTION	34	chain 'D' and (resid 76 through 95 )
35	X-RAY DIFFRACTION	35	chain 'D' and (resid 96 through 118 )
36	X-RAY DIFFRACTION	36	chain 'D' and (resid 119 through 162 )
37	X-RAY DIFFRACTION	37	chain 'D' and (resid 163 through 204 )
38	X-RAY DIFFRACTION	38	chain 'D' and (resid 205 through 217 )

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