PDB-10uh: Crystal structure of Formyl-coenzyme A transferase from Brucella ...

ID or keywords:

Entry

Database: PDB / ID: 10uh

Title

Crystal structure of Formyl-coenzyme A transferase from Brucella melitensis in complex with CoA

Components

Formyl-coenzyme a transferase

Keywords

TRANSFERASE / SSGCID / STRUCTURAL GENOMICS / SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE / Formyl-coenzyme A transferase

Function / homology

Function and homology information

Transferases; Transferring sulfur-containing groups; CoA-transferases / CoA-transferase activity
Similarity search - Function

Biological species

Brucella melitensis 16M1W (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.85 Å

Authors

Seattle Structural Genomics Center for Infectious Disease / Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Funding support

United States, 2items

Organization	Grant number	Country
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)	75N93022C00036	United States
National Institutes of Health/Office of the Director	S10OD030394	United States

Citation

Journal: To be published
Title: Crystal structure of Formyl-coenzyme A transferase from Brucella melitensis in complex with CoA
Authors: Liu, L. / Lovell, S. / Cooper, A. / Battaile, K.P.

History

Deposition	Feb 9, 2026	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Feb 18, 2026	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	10uh.cif.gz	486.8 KB	Display	PDBx/mmCIF format
PDB format	pdb10uh.ent.gz	400.5 KB	Display	PDB format
PDBx/mmJSON format	10uh.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/0u/10uh ftp://data.pdbj.org/pub/pdb/validation_reports/0u/10uh	HTTPS FTP

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Related structure data

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	#146 - Feb 2012 Aminoglycoside Antibiotics similarity (1) #93 - Sep 2007 Citrate Synthase similarity (1) #154 - Oct 2012 Citric Acid Cycle similarity (1) #216 - Dec 2017 Biodegradable Plastic similarity (1) #39 - Mar 2003 lac Repressor similarity (1)

Deposited unit

A: Formyl-coenzyme a transferase

B: Formyl-coenzyme a transferase

C: Formyl-coenzyme a transferase

hetero molecules

136 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Formyl-coenzyme a transferase

B: Formyl-coenzyme a transferase

hetero molecules

defined by author&software
Evidence: gel filtration
90.6 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Formyl-coenzyme a transferase

hetero molecules

C: Formyl-coenzyme a transferase

hetero molecules

defined by author&software
90.6 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	95.054, 176.355, 213.183
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	20
Space group name H-M	C222₁

Components on special symmetry positions

ID	Model	Components
1	1	A-791- HOH

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Protein , 1 types, 3 molecules ABC

#1: Protein	Formyl-coenzyme a transferase Mass: 44101.301 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Brucella melitensis 16M1W (bacteria) / Gene: BMEII0224 / Plasmid: BrmeA.18114.b.B2 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: Q8YDF2, Transferases; Transferring sulfur-containing groups; CoA-transferases

#1: Protein

Formyl-coenzyme a transferase

Mass: 44101.301 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Brucella melitensis 16M1W (bacteria) / Gene: BMEII0224 / Plasmid: BrmeA.18114.b.B2 / Production host:

Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q8YDF2, Transferases; Transferring sulfur-containing groups; CoA-transferases

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Non-polymers , 6 types, 716 molecules

#2: Chemical	ChemComp-PGE / TRIETHYLENE GLYCOL Mass: 150.173 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C₆H₁₄O₄
#3: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₃H₈O₃
#4: Chemical	ChemComp-ACT / ACETATE ION Mass: 59.044 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₂H₃O₂
#5: Chemical	ChemComp-COA / COENZYME A Mass: 767.534 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₂₁H₃₆N₇O₁₆P₃S / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical	ChemComp-PEG / DI(HYDROXYETHYL)ETHER Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₄H₁₀O₃
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 701 / 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: 3.38 Å³/Da / Density % sol: 63.57 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: Index G7: 0.20M Ammonium Acetate, 0.1M Bis-Tris pH 6.5, 20% PEG 3350. BrmeA.18114.b.B2.PW39356 at 20.7 mg/mL. Cocrystallization with 2mM CoA. plate 19820 G7 drop 2, Puck: PSL-1916, Cryo: 20% ...Details: Index G7: 0.20M Ammonium Acetate, 0.1M Bis-Tris pH 6.5, 20% PEG 3350. BrmeA.18114.b.B2.PW39356 at 20.7 mg/mL. Cocrystallization with 2mM CoA. plate 19820 G7 drop 2, Puck: PSL-1916, Cryo: 20% PEG 200 + 80% crystallant

Crystal

Density Matthews: 3.38 Å³/Da / Density % sol: 63.57 %

Crystal grow

Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: Index G7: 0.20M Ammonium Acetate, 0.1M Bis-Tris pH 6.5, 20% PEG 3350. BrmeA.18114.b.B2.PW39356 at 20.7 mg/mL. Cocrystallization with 2mM CoA. plate 19820 G7 drop 2, Puck: PSL-1916, Cryo: 20% ...

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: NSLS-II / Beamline: 19-ID / Wavelength: 0.9786 Å
Detector	Type: DECTRIS EIGER2 XE 9M / Detector: PIXEL / Date: Apr 5, 2025
Radiation	Monochromator: Double Crystal Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9786 Å / Relative weight: 1
Reflection	Resolution: 1.85→48.68 Å / Num. obs: 151962 / % possible obs: 99.9 % / Redundancy: 13.4 % / CC_1/2: 0.996 / R_merge(I) obs: 0.155 / R_pim(I) all: 0.044 / R_rim(I) all: 0.161 / Χ²: 1.43 / Net I/σ(I): 17.1 / Num. measured all: 2034117
Reflection shell	Resolution: 1.85→1.9 Å / % possible obs: 100 % / Redundancy: 14 % / R_merge(I) obs: 1.726 / Num. measured all: 156594 / Num. unique obs: 11162 / CC_1/2: 0.738 / R_pim(I) all: 0.476 / R_rim(I) all: 1.791 / Χ²: 0.94 / Net I/σ(I) obs: 1.7

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Processing

Software

Name	Version	Classification
PHENIX	(2.0_5936: ???)	refinement
Aimless		data scaling
XDS		data reduction
PHASER		phasing
PDB_EXTRACT		data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.85→48.68 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 20.32 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1912	7609	5.01 %
R_work	0.1746	-	-
obs	0.1754	151872	99.9 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 1.85→48.68 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9117	0	231	701	10049

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.003	9631
X-RAY DIFFRACTION	f_angle_d	0.594	13081
X-RAY DIFFRACTION	f_dihedral_angle_d	17.492	3711
X-RAY DIFFRACTION	f_chiral_restr	0.045	1456
X-RAY DIFFRACTION	f_plane_restr	0.006	1697

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 (%)
1.85-1.87	0.3748	281	0.3245	4723	X-RAY DIFFRACTION	100
1.87-1.89	0.332	280	0.2968	4763	X-RAY DIFFRACTION	100
1.89-1.92	0.2997	254	0.2669	4760	X-RAY DIFFRACTION	100
1.92-1.94	0.2593	260	0.2445	4765	X-RAY DIFFRACTION	100
1.94-1.97	0.2557	251	0.23	4791	X-RAY DIFFRACTION	100
1.97-1.99	0.2484	242	0.211	4777	X-RAY DIFFRACTION	100
1.99-2.02	0.2244	222	0.2074	4793	X-RAY DIFFRACTION	100
2.02-2.05	0.2361	207	0.2059	4825	X-RAY DIFFRACTION	100
2.05-2.08	0.243	247	0.2071	4799	X-RAY DIFFRACTION	100
2.08-2.12	0.2175	227	0.2028	4780	X-RAY DIFFRACTION	100
2.12-2.15	0.2236	275	0.2065	4726	X-RAY DIFFRACTION	100
2.15-2.19	0.2382	274	0.1975	4754	X-RAY DIFFRACTION	100
2.19-2.24	0.2303	239	0.1906	4829	X-RAY DIFFRACTION	100
2.24-2.28	0.2098	230	0.183	4811	X-RAY DIFFRACTION	100
2.28-2.33	0.211	266	0.1819	4807	X-RAY DIFFRACTION	100
2.33-2.39	0.219	222	0.1727	4813	X-RAY DIFFRACTION	100
2.39-2.44	0.1786	212	0.1704	4821	X-RAY DIFFRACTION	100
2.44-2.51	0.1945	244	0.1728	4825	X-RAY DIFFRACTION	100
2.51-2.58	0.1674	271	0.1733	4776	X-RAY DIFFRACTION	100
2.58-2.67	0.2027	248	0.1741	4792	X-RAY DIFFRACTION	100
2.67-2.76	0.1983	292	0.1882	4766	X-RAY DIFFRACTION	100
2.76-2.87	0.2066	241	0.1936	4841	X-RAY DIFFRACTION	100
2.87-3	0.213	250	0.195	4810	X-RAY DIFFRACTION	100
3-3.16	0.2184	282	0.1883	4815	X-RAY DIFFRACTION	100
3.16-3.36	0.2237	267	0.1861	4828	X-RAY DIFFRACTION	100
3.36-3.62	0.1797	261	0.1759	4832	X-RAY DIFFRACTION	100
3.62-3.99	0.1623	288	0.1469	4837	X-RAY DIFFRACTION	100
3.99-4.56	0.1399	232	0.1348	4895	X-RAY DIFFRACTION	100
4.56-5.74	0.1486	272	0.1453	4861	X-RAY DIFFRACTION	99
5.75-48.68	0.1604	272	0.1541	5048	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	4.4198	-0.3343	0.2732	3.4522	0.3399	2.1831	-0.0743	0.0228	0.2444	0.0826	-0.0044	-0.0385	-0.3083	-0.1437	0.0971	0.2456	0.0178	-0.0167	0.1848	-0.0035	0.1856	-42.8984	-10.1702	-15.0129
2	2.1617	0.4694	-0.9931	4.1088	-1.3981	1.0102	0.0189	0.1005	0.1242	-0.0793	-0.0217	0.2806	-0.0547	-0.1963	-0.0166	0.2724	0.045	-0.0074	0.2927	-0.0507	0.2614	-53.5503	-9.6474	-12.9609
3	4.868	0.4902	-0.2332	8.5238	-0.3039	3.4416	0.0891	0.2539	0.3841	-0.3643	-0.1385	-0.092	-0.4751	-0.0814	0.0692	0.2842	0.0546	0.0552	0.2562	0.0617	0.1741	-41.6546	-2.0823	-25.5531
4	0.6512	0.356	0.0464	4.7397	-0.5343	1.3667	0.1332	0.2102	0.0175	-0.4857	-0.0798	0.0689	-0.0182	-0.2175	-0.0442	0.3442	0.0547	-0.0044	0.3532	0.0393	0.2523	-42.2878	-11.2752	-31.9727
5	1.9288	-2.1975	-0.1824	5.1274	-0.1711	3.595	0.0785	0.0222	-0.265	-0.153	-0.1448	0.4865	0.2229	-0.2966	0.0553	0.1889	-0.0229	-0.0496	0.322	-0.0837	0.3171	-55.8403	-34.4924	-23.2003
6	1.1199	0.1855	-0.0044	1.4805	-0.2436	0.4931	-0.0185	0.0981	-0.0667	-0.1849	-0.087	0.0492	0.088	-0.031	0.0924	0.2255	0.0152	0.0085	0.2731	-0.0265	0.2264	-40.8375	-31.7793	-22.6308
7	7.1884	-2.8256	-4.0538	6.1746	0.4655	7.0197	-0.1775	-0.3785	-0.2785	0.0202	-0.0011	-0.5912	0.6538	0.4585	0.1603	0.2541	-0.0009	-0.0081	0.2972	0.0449	0.416	-43.2589	-55.8645	-4.3277
8	2.2323	0.4056	-1.1268	3.6616	0.401	6.6158	-0.1115	-0.1192	-0.4182	-0.2102	-0.0499	-0.1032	0.4896	0.0667	0.1618	0.2768	-0.0073	0.0563	0.2129	0.0409	0.4544	-46.9441	-56.6657	-6.7195
9	0.6028	-0.0711	0.4444	4.1341	-0.7177	0.3976	-0.0384	-0.2164	0.0477	0.7293	-0.0859	0.1403	-0.224	-0.1396	0.1305	0.3747	-0.0298	0.0536	0.3674	-0.026	0.2595	-47.6409	-29.3044	1.0821
10	1.6402	-1.9352	-1.1315	4.8061	0.5019	1.2677	-0.1996	-0.1287	0.2319	0.5337	0.0876	-0.142	-0.2104	0.0535	0.1156	0.3365	-0.0108	-0.042	0.2662	-0.0333	0.2164	-43.7668	-12.9412	-3.7876
11	5.003	-1.1819	0.2756	5.3364	-1.1263	1.8161	0.3513	-0.0903	0.6445	0.3838	-0.1237	-0.0634	-0.9057	-0.1449	-0.2197	0.5125	0.0455	0.0611	0.251	-0.0284	0.3501	-47.7821	8.2402	-13.9862
12	2.7349	0.9882	-0.8303	5.2761	-0.6389	1.7745	0.0109	-0.0754	-0.0955	-0.0695	-0.1172	-0.2566	0.2022	0.2151	0.1259	0.2015	0.06	0.0049	0.2859	0.0107	0.2426	-26.0649	-35.4667	-19.5559
13	0.7812	-0.4846	0.2529	0.5047	0.4462	1.0797	-0.0464	-0.0874	-0.1077	0.2215	0.0298	-0.2526	0.2843	0.1311	0.0135	0.2977	0.0383	-0.0303	0.2881	0.0311	0.3223	-25.2053	-38.6559	-10.3751
14	4.2996	-2.5024	-0.1892	3.9316	-0.0059	3.6819	-0.0131	0.1104	-0.2334	0.1854	-0.0426	0.3959	0.0883	-0.4425	0.0314	0.2198	-0.0577	0.0453	0.2838	-0.0355	0.2983	-53.4117	-38.2116	-11.7737
15	1.4771	0.0344	0.1442	1.0056	-0.037	0.4349	0.0035	0.0115	-0.0202	0.1001	-0.0815	0.0914	0.0409	-0.0397	0.0781	0.194	0.0009	-0.0026	0.2221	-0.022	0.1962	-45.0124	-25.2059	-11.8147
16	6.7971	-1.6968	2.0236	4.7083	3.1518	7.5989	-0.0419	0.1111	0.7762	-0.7479	0.0241	-0.0902	-0.7897	-0.2119	0.0159	0.3525	0.0249	-0.0372	0.3253	0.0107	0.3903	-68.665	-19.2587	-30.999
17	2.9339	0.0113	-0.4688	4.1757	2.1022	6.531	0.0024	-0.0972	0.2381	-0.3577	-0.1362	0.4163	-0.3055	-0.3728	0.1364	0.2067	0.0434	-0.0714	0.3005	-0.0383	0.3763	-70.4956	-21.9763	-28.641
18	4.0079	-1.6471	-1.0055	2.1608	-0.2478	0.4797	0.1964	0.6431	-0.1302	-0.4665	-0.2956	0.0523	0.1987	-0.003	0.0841	0.4449	0.0623	-0.0233	0.3957	-0.0815	0.2476	-41.7466	-34.8784	-35.375
19	2.5426	-1.6794	1.0152	3.5866	0.1602	1.596	0.2927	0.3952	-0.1057	-0.3731	-0.1708	-0.4056	0.3116	0.4086	-0.038	0.2941	0.0699	0.1028	0.4319	0.0135	0.3288	-18.8321	-40.1185	-24.909
20	4.2642	1.0512	-0.174	3.2884	0.3014	1.1703	-0.2911	-0.0576	0.3523	-0.0948	0.0147	0.2005	-0.1107	-0.2443	0.2882	0.3262	0.0304	-0.063	0.2685	-0.0241	0.2115	-15.2621	-47.1922	-52.0593
21	3.8905	-1.0245	0.9066	4.2369	-1.7249	1.7115	-0.3552	0.0799	-0.1049	0.0663	0.1322	0.1376	0.0652	-0.0504	0.2116	0.3359	-0.0164	0.0607	0.2922	-0.0643	0.2343	-21.832	-55.8015	-50.3723
22	8.4643	-4.0492	0.2503	5.5228	-1.9912	3.2045	-0.2062	0.266	-0.0053	-0.1205	0.0979	0.0937	0.0445	0.0306	0.1667	0.2976	-0.0317	-0.0819	0.2588	0.0672	0.2133	-20.966	-41.5512	-62.9495
23	2.925	-2.4252	0.2441	3.3078	-0.1364	0.7858	-0.1343	0.4317	-0.0488	-0.2016	-0.0432	0.276	0.1738	-0.1457	0.1926	0.4668	-0.1054	-0.1063	0.3807	0.0376	0.3007	-12.9584	-47.3317	-68.964
24	8.3149	-2.3141	-0.4444	2.9261	0.7202	3.8142	-0.389	0.0689	-0.5842	-0.0237	0.1982	-0.0024	0.2308	0.0613	0.1615	0.44	-0.0797	0.1211	0.2137	-0.045	0.2843	-1.7938	-71.5499	-59.1494
25	0.9466	-0.1879	0.1319	1.583	-0.3221	0.3917	-0.2106	0.0994	0.0434	-0.1858	0.0366	-0.1477	0.0875	-0.0072	0.1686	0.386	-0.0271	0.0111	0.2863	0.0175	0.2452	4.2097	-57.3225	-58.4931
26	2.2903	2.7781	-1.385	6.4696	-3.0109	6.1848	0.1227	-0.3045	0.0774	0.2797	-0.2086	-0.5225	0.0367	0.6325	0.0958	0.3124	0.0642	0.0403	0.307	0.0377	0.3712	21.2483	-72.9668	-38.1787
27	2.282	0.2732	-1.8262	3.6417	-1.5686	6.6923	-0.1138	-0.0522	-0.1546	-0.127	-0.2353	-0.417	0.2327	0.3682	0.3767	0.3222	0.0725	0.0567	0.2883	0.0842	0.4122	20.337	-76.2944	-40.6621
28	1.8452	-0.47	0.1672	0.8715	0.0043	-0.0207	-0.376	-0.496	0.0032	0.3469	0.1987	0.0274	-0.0114	-0.1049	0.1863	0.5212	0.1118	0.022	0.4243	-0.0159	0.2627	-8.9701	-55.5974	-37.9073
29	7.0432	0.0928	2.0223	7.7176	-0.2655	5.2264	-0.4131	-0.2221	0.0891	0.3183	0.6367	1.0264	-0.2876	-0.9336	-0.1987	0.3344	0.1269	-0.0234	0.4491	0.0331	0.427	-33.4131	-41.4101	-51.9812

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 48 through 94 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 95 through 124 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 125 through 148 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 149 through 187 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 188 through 214 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 215 through 288 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 289 through 317 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 318 through 358 )
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 359 through 388 )
10	X-RAY DIFFRACTION	10	chain 'A' and (resid 389 through 420 )
11	X-RAY DIFFRACTION	11	chain 'A' and (resid 421 through 450 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 48 through 95 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 96 through 187 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 188 through 214 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 215 through 287 )
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 288 through 317 )
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 318 through 358 )
18	X-RAY DIFFRACTION	18	chain 'B' and (resid 359 through 397 )
19	X-RAY DIFFRACTION	19	chain 'B' and (resid 398 through 450 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 48 through 94 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 95 through 124 )
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 125 through 148 )
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 149 through 187 )
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 188 through 214 )
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 215 through 287 )
26	X-RAY DIFFRACTION	26	chain 'C' and (resid 288 through 317 )
27	X-RAY DIFFRACTION	27	chain 'C' and (resid 318 through 358 )
28	X-RAY DIFFRACTION	28	chain 'C' and (resid 359 through 420 )
29	X-RAY DIFFRACTION	29	chain 'C' and (resid 421 through 450 )

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