PDB-38le: Crystal Structure of L-erythrulose-1-phosphate isomerase from Bru...

ID or keywords:

Entry

Database: PDB / ID: 38le

Title

Crystal Structure of L-erythrulose-1-phosphate isomerase from Brucella melitensis in complex with ETHYL DIHYDROGEN PHOSPHATE

Components

L-erythrulose-1-phosphate isomerase

Keywords

ISOMERASE / SSGCID / STRUCTURAL GENOMICS / SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE / L-erythrulose-1-phosphate isomerase / Brucella melitensis

Function / homology

Function and homology information

L-erythrulose-1-phosphate isomerase / triose-phosphate isomerase activity / glycerol catabolic process / glyceraldehyde-3-phosphate biosynthetic process / gluconeogenesis / glycolytic process / cytosol
Similarity search - Function

Biological species

Brucella abortus 2308 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.5 Å

Authors

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 L-erythrulose-1-phosphate isomerase from Brucella melitensis in complex with ETHYL DIHYDROGEN PHOSPHATE
Authors: Liu, L. / Lovell, S. / Battaile, K.P.

History

Deposition	Sep 1, 2026	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 16, 2026	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	38le.cif.gz	409.1 KB	Display	PDBx/mmCIF format
PDB format	pdb38le.ent.gz	332.9 KB	Display	PDB format
PDBx/mmJSON format	38le.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/8l/38le ftp://data.pdbj.org/pub/pdb/validation_reports/8l/38le	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	#50 - Feb 2004 Glycolytic Enzymes similarity (6)

Deposited unit

A: L-erythrulose-1-phosphate isomerase

B: L-erythrulose-1-phosphate isomerase

C: L-erythrulose-1-phosphate isomerase

D: L-erythrulose-1-phosphate isomerase

hetero molecules

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

1

A: L-erythrulose-1-phosphate isomerase

D: L-erythrulose-1-phosphate isomerase

hetero molecules

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

2

B: L-erythrulose-1-phosphate isomerase

C: L-erythrulose-1-phosphate isomerase

hetero molecules

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

Unit cell

Length a, b, c (Å)	45.318, 49.513, 116.429
Angle α, β, γ (deg.)	88.44, 83.14, 86.18
Int Tables number	1
Space group name H-M	P1

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Protein , 1 types, 4 molecules ABCD

#1: Protein	L-erythrulose-1-phosphate isomerase / D-3-tetrulose-4-phosphate isomerase Mass: 28744.627 Da / Num. of mol.: 4 / Fragment: K3-N256 / Mutation: A173D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Brucella abortus 2308 (bacteria) / Gene: eryH, tpiA-2, BAB2_0367 / Plasmid: BrabA.00276.a.B2 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: Q2YIQ6, L-erythrulose-1-phosphate isomerase

#1: Protein

L-erythrulose-1-phosphate isomerase / D-3-tetrulose-4-phosphate isomerase

Mass: 28744.627 Da / Num. of mol.: 4 / Fragment: K3-N256 / Mutation: A173D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Brucella abortus 2308 (bacteria) / Gene: eryH, tpiA-2, BAB2_0367 / Plasmid: BrabA.00276.a.B2 / Production host:

Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q2YIQ6, L-erythrulose-1-phosphate isomerase

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Non-polymers , 6 types, 1030 molecules

#2: Chemical	ChemComp-EFS / ETHYL DIHYDROGEN PHOSPHATE Mass: 126.048 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂H₇O₄P / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical	ChemComp-HEZ / HEXANE-1,6-DIOL Mass: 118.174 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₆H₁₄O₂
#4: Chemical	ChemComp-NA / SODIUM ION Mass: 22.990 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Na
#5: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#6: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₃H₈O₃
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1014 / 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: 2.25 Å³/Da / Density % sol: 45.34 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 70 mM MES pH 6.5, 70 mM CaCl2, 14% PEG 1500, 8.4% hexanediol. BrabA.00276.a.B2.PW39519 at 15.2 mg/mL. 20 hour soak in 10 mM glycerol 3-phosphate (D/L mixture), EFS fit best to the electron ...Details: 70 mM MES pH 6.5, 70 mM CaCl2, 14% PEG 1500, 8.4% hexanediol. BrabA.00276.a.B2.PW39519 at 15.2 mg/mL. 20 hour soak in 10 mM glycerol 3-phosphate (D/L mixture), EFS fit best to the electron density, plate Liu-S-202 E9-F10, Puck: PSL-0208, Cryo: 100 mM MES, pH 6.5, 100 mM CaCl2, 20% PEG 1500, 12% hexanediol

Crystal

Density Matthews: 2.25 Å³/Da / Density % sol: 45.34 %

Crystal grow

Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 70 mM MES pH 6.5, 70 mM CaCl2, 14% PEG 1500, 8.4% hexanediol. BrabA.00276.a.B2.PW39519 at 15.2 mg/mL. 20 hour soak in 10 mM glycerol 3-phosphate (D/L mixture), EFS fit best to the electron ...

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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: Feb 22, 2026
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: 1.5→45.74 Å / Num. obs: 152470 / % possible obs: 95 % / Redundancy: 3.6 % / CC_1/2: 0.997 / R_merge(I) obs: 0.076 / R_pim(I) all: 0.048 / R_rim(I) all: 0.09 / Χ²: 0.96 / Net I/σ(I): 10.1 / Num. measured all: 546898
Reflection shell	Resolution: 1.5→1.54 Å / % possible obs: 87.9 % / Redundancy: 3.3 % / R_merge(I) obs: 0.642 / Num. measured all: 34260 / Num. unique obs: 10484 / CC_1/2: 0.707 / R_pim(I) all: 0.414 / R_rim(I) all: 0.767 / Χ²: 0.78 / Net I/σ(I) obs: 1.7

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Processing

Software

Name	Version	Classification
PHENIX	(2.2_6151: ???)	refinement
Aimless		data scaling
XDS		data reduction
PHASER		phasing
PDB_EXTRACT		data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.5→45.74 Å / SU ML: 0.15 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 17.89 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1818	7874	5.17 %
R_work	0.1519	-	-
obs	0.1533	152427	94.93 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 1.5→45.74 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7549	0	55	1014	8618

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	7816
X-RAY DIFFRACTION	f_angle_d	0.877	10593
X-RAY DIFFRACTION	f_dihedral_angle_d	17.995	2863
X-RAY DIFFRACTION	f_chiral_restr	0.052	1187
X-RAY DIFFRACTION	f_plane_restr	0.012	1376

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 (%)
1.5-1.52	0.2867	261	0.2788	4389	X-RAY DIFFRACTION	87
1.52-1.53	0.2594	214	0.252	4525	X-RAY DIFFRACTION	88
1.53-1.55	0.2355	248	0.2343	4601	X-RAY DIFFRACTION	90
1.55-1.57	0.2337	257	0.2157	4699	X-RAY DIFFRACTION	93
1.57-1.59	0.2403	262	0.2043	4814	X-RAY DIFFRACTION	95
1.59-1.62	0.206	280	0.1979	4816	X-RAY DIFFRACTION	95
1.62-1.64	0.2308	255	0.1918	4774	X-RAY DIFFRACTION	95
1.64-1.66	0.2157	272	0.181	4919	X-RAY DIFFRACTION	95
1.66-1.69	0.2105	282	0.1801	4760	X-RAY DIFFRACTION	95
1.69-1.72	0.2171	279	0.1711	4818	X-RAY DIFFRACTION	96
1.72-1.75	0.188	253	0.1651	4879	X-RAY DIFFRACTION	96
1.75-1.78	0.2033	250	0.1662	4824	X-RAY DIFFRACTION	96
1.78-1.81	0.1946	270	0.1676	4909	X-RAY DIFFRACTION	96
1.81-1.85	0.183	288	0.1656	4837	X-RAY DIFFRACTION	96
1.85-1.89	0.2035	278	0.169	4894	X-RAY DIFFRACTION	96
1.89-1.93	0.1772	279	0.1558	4809	X-RAY DIFFRACTION	96
1.93-1.98	0.1731	271	0.1493	4890	X-RAY DIFFRACTION	96
1.98-2.04	0.1805	279	0.1503	4866	X-RAY DIFFRACTION	96
2.04-2.1	0.1755	257	0.1444	4875	X-RAY DIFFRACTION	96
2.1-2.16	0.2018	259	0.1487	4988	X-RAY DIFFRACTION	97
2.16-2.24	0.1751	266	0.1398	4853	X-RAY DIFFRACTION	96
2.24-2.33	0.1673	251	0.1366	4847	X-RAY DIFFRACTION	96
2.33-2.44	0.169	267	0.1333	4866	X-RAY DIFFRACTION	96
2.44-2.56	0.1596	256	0.1379	4923	X-RAY DIFFRACTION	96
2.56-2.73	0.172	262	0.142	4905	X-RAY DIFFRACTION	96
2.73-2.94	0.1839	275	0.1454	4855	X-RAY DIFFRACTION	96
2.94-3.23	0.1655	222	0.1423	4886	X-RAY DIFFRACTION	95
3.23-3.7	0.1706	273	0.1366	4798	X-RAY DIFFRACTION	95
3.7-4.66	0.1465	248	0.1263	4818	X-RAY DIFFRACTION	95
4.66-45.74	0.1923	260	0.1611	4916	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	0.7011	0.2907	0.545	4.4934	2.6085	3.7847	0.0555	0.0119	-0.0258	-0.1836	-0.0825	0.0941	0.0391	-0.0718	0.0419	0.1177	0.0027	-0.0031	0.1165	0.0248	0.1126	1.1845	6.4612	-4.0528
2	3.6179	2.6576	4.3069	4.1906	4.2721	6.0826	-0.1756	0.0919	0.1622	-0.4491	-0.0392	0.2458	-0.4053	-0.073	0.2338	0.1892	0.0058	-0.032	0.1228	0.0286	0.1205	-4.2664	16.4178	-9.2473
3	0.7041	-0.1993	0.1669	1.0807	0.1286	3.1867	0.0336	-0.0029	-0.0545	-0.0628	-0.0604	0.0994	0.0933	-0.1619	0.0324	0.0993	-0.0139	-0.0128	0.1006	0.0069	0.1251	-6.4521	6.7481	3.4276
4	0.9475	0.5275	0.6067	1.8543	0.129	1.8768	0.0842	-0.0216	-0.1444	0.0637	-0.0117	-0.299	0.1021	0.2034	-0.021	0.1444	0.0104	-0.019	0.1217	0.0267	0.1811	3.7614	-4.7021	8.5666
5	4.9082	0.5402	-2.2775	3.6064	1.1339	3.1752	0.035	-0.2128	-0.3509	-0.0053	0.0865	-0.3386	0.1777	0.2053	-0.1176	0.1412	0.0056	-0.0332	0.0828	0.047	0.1599	-0.1343	-14.1206	8.2876
6	5.7326	1.0705	-2.8013	3.4512	-0.4948	4.6994	-0.0807	-0.1315	-0.0535	-0.1331	-0.0091	-0.3783	-0.1009	0.4106	0.0704	0.1666	-0.0095	-0.0392	0.0883	0.0361	0.1535	1.8735	-7.6378	0.2563
7	1.839	2.417	-1.5833	5.1209	-2.7348	2.2215	-0.0753	0.063	-0.1914	-0.306	-0.0532	-0.2886	0.1091	0.0565	0.1375	0.1783	0.0075	-0.0001	0.1343	-0.0145	0.1575	3.86	-11.4397	-4.6699
8	1.9277	1.7541	-0.0322	2.2648	1.0209	3.3719	-0.1051	0.0811	-0.0845	-0.22	0.1099	-0.1156	0.1319	0.0805	-0.0553	0.1757	0.0221	0.0186	0.1275	0.0187	0.1305	6.0088	-1.3365	-10.2874
9	7.0292	-0.6492	-0.615	6.6464	4.1565	7.2758	0.0413	0.5339	-0.1804	-0.669	-0.0504	-0.0068	0.1014	0.0034	-0.044	0.2663	0.0065	0.0049	0.1671	0.0064	0.097	2.1592	3.7405	-17.4466
10	1.8153	2.4104	1.7168	6.6583	4.3672	5.675	0.0102	0.038	0.0472	0.158	0.0243	0.0258	0.1581	-0.0118	-0.0303	0.0804	0.0068	0.014	0.1216	0.0125	0.1222	-1.1717	5.0036	-45.3564
11	6.2521	6.0056	1.0649	9.0776	3.504	3.9184	0.3021	-0.3107	-0.0038	0.7905	-0.3221	0.2194	0.2093	-0.1688	0.0164	0.2008	-0.0433	0.0335	0.1788	0.0071	0.1494	-3.9221	2.1697	-33.3879
12	1.8137	-0.1132	-0.016	0.5325	-0.4013	2.961	-0.0216	0.0781	-0.1234	-0.0125	0.0377	0.0893	0.2829	-0.1746	-0.0089	0.0999	-0.0134	0.0086	0.0835	0.0031	0.1045	-1.8034	-2.3234	-43.6879
13	5.1499	3.4929	-0.9566	4.0259	-2.1683	2.0542	0.0715	-0.0785	-0.1972	0.122	-0.0508	-0.0916	0.0711	-0.0359	-0.0297	0.113	0.0102	0.0009	0.0799	-0.0059	0.0916	6.0967	0.44	-39.4804
14	0.791	0.1623	0.5372	1.2842	-0.05	1.5897	0.0129	0.0759	-0.0015	0.0221	-0.0035	-0.1	-0.0498	0.0753	-0.0053	0.0957	-0.0023	0.0023	0.1291	0.0075	0.1381	15.0337	8.2003	-48.3681
15	2.519	-3.0497	3.9177	4.5888	-4.8649	6.7469	-0.1912	-0.017	0.0847	0.122	-0.0153	-0.1018	-0.2599	-0.0219	0.2383	0.1133	-0.005	-0.0039	0.1539	-0.0103	0.1453	4.8636	12.2808	-60.9082
16	7.3963	-4.1185	3.6141	6.8575	-2.6809	5.7739	-0.135	0.3179	0.126	-0.3668	-0.0249	-0.1777	0.0521	0.1827	0.1571	0.0973	-0.006	0.0401	0.1665	0.0016	0.0775	13.4265	5.689	-64.4728
17	6.4611	-2.6092	1.7568	4.9789	-1.0619	4.1827	-0.0611	0.1174	0.2603	-0.0285	-0.0236	0.1375	-0.2396	-0.2202	0.0247	0.1124	-0.0268	0.0011	0.1275	-0.0107	0.0963	3.8994	4.9317	-59.0852
18	3.3478	-0.7801	-1.7083	1.6631	0.9625	4.594	0.0236	0.0987	-0.159	-0.1321	-0.029	0.1647	-0.0017	-0.125	0.0027	0.109	-0.0073	-0.0277	0.1029	-0.0145	0.1198	-0.2577	2.9843	-63.1571
19	1.7118	-0.3465	-0.8259	1.6664	1.8943	4.0152	-0.0324	0.1649	-0.02	-0.069	-0.1366	0.2395	-0.0596	-0.4218	0.1723	0.1014	0.0058	-0.0009	0.1664	0.0001	0.1438	-7.5684	3.4726	-54.7691
20	5.9581	2.2199	3.3473	5.9963	1.1853	7.6362	-0.1586	0.1331	-0.0176	-0.0802	-0.0361	0.381	0.0527	-0.6869	0.1794	0.0828	-0.0232	0.0317	0.2131	-0.0112	0.1923	-12.6596	-0.8782	-48.3303
21	2.1861	-0.2629	0.5663	0.6006	-0.5846	0.6314	-0.0505	-0.22	0.2271	0.3046	-0.0154	-0.0448	-0.0681	-0.0567	0.0721	0.1908	-0.0388	-0.023	0.1335	0.0097	0.1533	21.7266	20.1864	-28.2088
22	2.0756	1.4514	3.1684	3.6726	4.3274	7.0534	0.1836	-0.2677	-0.1111	0.4676	-0.1851	-0.1662	0.6916	-0.2274	0.0313	0.2421	-0.0258	-0.0577	0.1446	0.0424	0.1608	22.2857	5.5507	-23.9287
23	1.9205	0.0608	1.1137	0.9643	-0.0979	1.8903	0.0103	-0.1903	0.0896	0.2131	-0.0711	-0.006	-0.0626	-0.0863	0.0622	0.162	-0.0173	-0.0074	0.1048	-0.004	0.1093	14.1283	17.2132	-29.3185
24	2.8965	-1.9713	-2.8637	2.6152	1.8407	4.3367	0.0598	0.1239	0.0157	-0.0929	-0.0966	0.0114	-0.175	-0.1006	0.0279	0.1363	-0.0236	-0.0329	0.0897	0.015	0.1267	14.2591	26.1433	-42.1183
25	3.707	1.7799	-2.6255	2.3437	-1.2458	4.0344	0.0123	0.0962	-0.2877	-0.0788	-0.0561	-0.3402	-0.1059	0.2699	0.0467	0.1853	0.0062	-0.0075	0.1471	-0.0179	0.1868	23.3855	30.3843	-40.8891
26	4.2292	2.7844	-3.9681	2.4541	-2.4481	4.6918	0.0624	0.2932	-0.0534	-0.0116	0.0824	-0.1317	-0.1098	0.0051	-0.054	0.1926	-0.0274	-0.0161	0.1192	0.008	0.1975	21.7346	37.4644	-42.0433
27	8.628	-2.3529	-0.8276	2.1575	-0.4526	2.0575	0.0818	0.0844	-0.0494	0.1028	-0.0667	-0.0927	-0.0357	0.0499	-0.0128	0.2054	-0.0484	-0.0483	0.0559	-0.001	0.1344	17.8757	33.4532	-33.2517
28	1.9654	-1.1724	-0.11	3.2946	-0.0076	0.5637	0.0956	0.0611	-0.0012	0.1516	-0.1436	-0.2188	-0.1343	0.0942	0.0464	0.216	-0.0498	-0.0632	0.1404	0.0269	0.1909	28.1094	33.9818	-32.0985
29	1.6018	1.8521	0.2708	3.4428	0.9784	0.8203	-0.0499	0.0601	0.1095	0.169	-0.0533	-0.498	-0.1578	0.1117	0.0437	0.2028	-0.04	-0.0867	0.143	0.038	0.233	32.7744	23.5302	-29.1835
30	6.2296	4.8888	2.3022	4.755	3.7265	4.9422	-0.0568	-0.1832	0.1988	0.5309	-0.034	-0.5094	-0.1819	0.2604	-0.0349	0.2756	-0.0133	-0.1515	0.1704	0.0229	0.2541	34.5322	18.5096	-21.1472
31	1.875	-0.5955	0.3109	1.7162	0.0845	1.9131	-0.039	-0.0945	0.2119	0.1189	0.0196	0.0332	-0.171	-0.0046	0.0084	0.1028	-0.0072	0.0135	0.1205	0.0037	0.1175	-6.5826	24.7153	22.0527
32	0.2432	0.0665	0.1473	0.3491	0.0104	0.6619	0.0163	-0.0465	-0.0041	0.048	-0.0064	-0.0301	0.0421	0.0527	-0.014	0.1073	-0.0003	-0.0009	0.1385	0.0145	0.1227	7.034	16.0719	19.8758
33	2.3089	0.1362	0.1213	0.6725	-0.1088	1.5706	0.0501	-0.2851	0.0108	0.1517	-0.0222	0.0166	-0.0275	-0.064	-0.0321	0.1614	-0.0019	-0.0052	0.1425	-0.0021	0.1152	3.0509	21.4564	33.4911

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 3 through 15 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 16 through 32 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 33 through 96 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 97 through 139 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 140 through 158 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 159 through 182 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 183 through 217 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 218 through 238 )
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 239 through 254 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 3 through 15 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 16 through 28 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 29 through 47 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 48 through 68 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 69 through 119 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 120 through 139 )
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 140 through 158 )
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 159 through 182 )
18	X-RAY DIFFRACTION	18	chain 'B' and (resid 183 through 217 )
19	X-RAY DIFFRACTION	19	chain 'B' and (resid 218 through 238 )
20	X-RAY DIFFRACTION	20	chain 'B' and (resid 239 through 253 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid -3 through 15 )
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 16 through 28 )
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 29 through 96 )
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 97 through 119 )
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 120 through 139 )
26	X-RAY DIFFRACTION	26	chain 'C' and (resid 140 through 151 )
27	X-RAY DIFFRACTION	27	chain 'C' and (resid 152 through 182 )
28	X-RAY DIFFRACTION	28	chain 'C' and (resid 183 through 217 )
29	X-RAY DIFFRACTION	29	chain 'C' and (resid 218 through 238 )
30	X-RAY DIFFRACTION	30	chain 'C' and (resid 239 through 254 )
31	X-RAY DIFFRACTION	31	chain 'D' and (resid -3 through 47 )
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 48 through 151 )
33	X-RAY DIFFRACTION	33	chain 'D' and (resid 152 through 254 )

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