PDB-6ok1: Ltp2-ChsH2(DUF35) aldolase

ID or keywords:

Entry

Database: PDB / ID: 6ok1

Title

Ltp2-ChsH2(DUF35) aldolase

Components

ChsH2(DUF35)
Lipid-transfer protein

Keywords

TRANSPORT PROTEIN / Aldolase / cholesterol degradation / thiolase superfamily / DUF35 domain

Function / homology

Function and homology information

Lyases; Carbon-carbon lyases; Oxo-acid-lyases / bile acid catabolic process / Lyases; Carbon-oxygen lyases; Hydro-lyases / acyltransferase activity, transferring groups other than amino-acyl groups / lipid catabolic process / lyase activity
Similarity search - Function

Biological species

Thermomonospora curvata (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

SAD / Resolution: 1.7 Å

Authors

Kimber, M.S. / Mallette, E. / Aggett, R. / Seah, S.Y.K.

Funding support

Canada, 2items

Citation

Journal: J.Biol.Chem. / Year: 2019
Title: The steroid side-chain-cleaving aldolase Ltp2-ChsH2DUF35is a thiolase superfamily member with a radically repurposed active site.
Authors: Aggett, R. / Mallette, E. / Gilbert, S.E. / Vachon, M.A. / Schroeter, K.L. / Kimber, M.S. / Seah, S.Y.K.

History

Deposition	Apr 12, 2019	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jun 26, 2019	Provider: repository / Type: Initial release
Revision 1.1	Jul 3, 2019	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed ..._citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2	Aug 14, 2019	Group: Data collection / Database references / Category: citation Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.3	Jan 8, 2020	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4	Mar 13, 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	6ok1.cif.gz	590.6 KB	Display	PDBx/mmCIF format
PDB format	pdb6ok1.ent.gz	493.3 KB	Display	PDB format
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Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ok/6ok1 ftp://data.pdbj.org/pub/pdb/validation_reports/ok/6ok1	HTTPS FTP

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Related structure data

Similar structure data	6e7v-1 5ewj-1 3quf-d 6k09-d 6k00-d 6e7r-1 6p3q-d 1lf8-d 1xu8-d 6e7w-1 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	#216 - Dec 2017 Biodegradable Plastic similarity (4) #90 - Jun 2007 Fatty Acid Synthase similarity (2)

Deposited unit

A: Lipid-transfer protein

B: ChsH2(DUF35)

C: Lipid-transfer protein

D: ChsH2(DUF35)

hetero molecules

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

1

Idetical with deposited unit
defined by author&software
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	91.680, 110.560, 120.140
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

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Protein , 2 types, 4 molecules ACBD

#1: Protein	Lipid-transfer protein Mass: 42997.156 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9) (bacteria) Strain: ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9 Gene: Tcur_3479 / Plasmid: pTIPQC2 / Production host: Rhodococcus jostii RHA1 (bacteria) / Strain (production host): Rha1 / References: UniProt: D1AB74
#2: Protein	ChsH2(DUF35) Mass: 14803.011 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9) (bacteria) Strain: ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9 Gene: Tcur_3482 / Plasmid: pTIPRT2 / Production host: Rhodococcus jostii RHA1 (bacteria) / References: UniProt: D1AB77

#1: Protein

Lipid-transfer protein

Mass: 42997.156 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9) (bacteria)
Strain: ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9
Gene: Tcur_3479 / Plasmid: pTIPQC2 / Production host:

Rhodococcus jostii RHA1 (bacteria) / Strain (production host): Rha1 / References: UniProt: D1AB74

#2: Protein

ChsH2(DUF35)

Mass: 14803.011 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9) (bacteria)
Strain: ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9
Gene: Tcur_3482 / Plasmid: pTIPRT2 / Production host:

Rhodococcus jostii RHA1 (bacteria) / References: UniProt: D1AB77

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Non-polymers , 6 types, 883 molecules

#3: Chemical	ChemComp-NA / SODIUM ION Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#4: Chemical	ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES Mass: 238.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₈H₁₈N₂O₄S / Comment: pH buffer*YM
#5: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Cl
#6: Chemical	ChemComp-PEG / DI(HYDROXYETHYL)ETHER Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₄H₁₀O₃
#7: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#8: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 867 / 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: 2.63 Å³/Da / Density % sol: 53.29 %
Crystal grow	Temperature: 283 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.2 M sodium thiocyanate, 20% PEG 3350, 16 mg/ml protein

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: CLSI / Beamline: 08B1-1 / Wavelength: 0.9786 Å
Detector	Type: RAYONIX MX300HE / Detector: CCD / Date: May 25, 2018
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9786 Å / Relative weight: 1
Reflection	Resolution: 1.7→50 Å / Num. obs: 134309 / % possible obs: 99.92 % / Redundancy: 5.2 % / B_iso Wilson estimate: 24.33 Å² / CC_1/2: 0.999 / R_merge(I) obs: 0.0485 / Net I/σ(I): 19.08
Reflection shell	Resolution: 1.7→1.761 Å / Redundancy: 5.2 % / Mean I/σ(I) obs: 2.23 / Num. unique obs: 11051 / CC_1/2: 0.734 / R_sym value: 0.724 / % possible all: 99.97

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Processing

Software

Name	Version	Classification
PHENIX	(1.12_2829: ???)	refinement
XDS		data reduction
XSCALE		data scaling
RESOLVE		phasing

Refinement

Method to determine structure:

SAD / Resolution: 1.7→42.828 Å / SU ML: 0.15 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 15.48

	R_factor	Num. reflection	% reflection
R_free	0.168	6714	5 %
R_work	0.1443	-	-
obs	0.1455	134294	99.93 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 1.7→42.828 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7707	0	70	867	8644

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	8204
X-RAY DIFFRACTION	f_angle_d	0.985	11226
X-RAY DIFFRACTION	f_dihedral_angle_d	13.346	4928
X-RAY DIFFRACTION	f_chiral_restr	0.059	1233
X-RAY DIFFRACTION	f_plane_restr	0.008	1491

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 (%)
1.7-1.7193	0.26	222	0.2266	4205	X-RAY DIFFRACTION	100
1.7193-1.7395	0.2357	221	0.213	4212	X-RAY DIFFRACTION	100
1.7395-1.7608	0.2692	221	0.2075	4199	X-RAY DIFFRACTION	100
1.7608-1.7831	0.2453	222	0.1998	4213	X-RAY DIFFRACTION	100
1.7831-1.8065	0.1963	219	0.1787	4168	X-RAY DIFFRACTION	100
1.8065-1.8313	0.2069	224	0.1775	4236	X-RAY DIFFRACTION	100
1.8313-1.8574	0.1981	221	0.1691	4215	X-RAY DIFFRACTION	100
1.8574-1.8851	0.1846	221	0.1665	4190	X-RAY DIFFRACTION	100
1.8851-1.9146	0.1971	225	0.1668	4267	X-RAY DIFFRACTION	100
1.9146-1.946	0.2065	221	0.1607	4204	X-RAY DIFFRACTION	100
1.946-1.9795	0.218	221	0.1577	4195	X-RAY DIFFRACTION	100
1.9795-2.0155	0.1994	224	0.1506	4259	X-RAY DIFFRACTION	100
2.0155-2.0543	0.1793	220	0.1439	4189	X-RAY DIFFRACTION	100
2.0543-2.0962	0.1564	224	0.1391	4246	X-RAY DIFFRACTION	100
2.0962-2.1418	0.1804	222	0.1378	4222	X-RAY DIFFRACTION	100
2.1418-2.1916	0.1909	224	0.1351	4251	X-RAY DIFFRACTION	100
2.1916-2.2464	0.1543	222	0.1296	4226	X-RAY DIFFRACTION	100
2.2464-2.3072	0.1751	224	0.13	4254	X-RAY DIFFRACTION	100
2.3072-2.3751	0.1573	221	0.1267	4209	X-RAY DIFFRACTION	100
2.3751-2.4517	0.1797	225	0.1279	4262	X-RAY DIFFRACTION	100
2.4517-2.5393	0.1584	223	0.1241	4244	X-RAY DIFFRACTION	100
2.5393-2.641	0.1673	225	0.1268	4279	X-RAY DIFFRACTION	100
2.641-2.7612	0.135	225	0.1294	4264	X-RAY DIFFRACTION	100
2.7612-2.9067	0.1599	224	0.1302	4258	X-RAY DIFFRACTION	100
2.9067-3.0888	0.1823	225	0.1451	4285	X-RAY DIFFRACTION	100
3.0888-3.3272	0.1431	226	0.1465	4280	X-RAY DIFFRACTION	100
3.3272-3.6619	0.1546	227	0.1407	4322	X-RAY DIFFRACTION	100
3.6619-4.1913	0.1605	228	0.1325	4331	X-RAY DIFFRACTION	100
4.1913-5.2791	0.1401	230	0.1285	4365	X-RAY DIFFRACTION	100
5.2791-42.8419	0.1766	237	0.1792	4530	X-RAY DIFFRACTION	100

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	0.266	-0.1211	0.1328	0.033	0.072	0.2414	-0.1142	0.0228	0.1131	-0.0305	0.0544	0.0314	-0.1774	0.0097	-0.001	0.2937	-0.0115	-0.0244	0.1568	-0.0245	0.2226	-25.4406	14.3079	-3.967
2	0.2849	0.1067	-0.1103	0.0861	-0.1251	0.1066	-0.1003	0.0625	0.0562	-0.0422	0.0664	0.0019	-0.0541	0.053	0	0.2967	0.0102	-0.012	0.2076	-0.044	0.2277	-25.8623	6.1449	-6.0106
3	0.4331	0.1248	0.1944	0.3434	0.1469	0.6452	-0.0788	-0.0169	0.0736	0.0089	0.0146	0.0599	-0.0728	-0.1963	0.0001	0.1399	0.0474	0.0093	0.1956	-0.0279	0.1907	-45.3555	2.1015	-6.8307
4	0.167	0.0962	0.1237	0.0286	0.0095	0.085	-0.1298	-0.0138	0.1135	0.0402	0.0052	0.1008	-0.1935	-0.1293	-0.1005	0.2548	0.1174	-0.0355	0.2115	-0.0478	0.2927	-45.1327	15.1752	-4.9799
5	0.0145	-0.016	0.0036	0.0105	0.0224	0.0011	0.1486	0.2302	-0.1798	-0.0637	0.0304	-0.2124	0.0616	0.1374	0.0001	0.2165	0.0076	0.0185	0.229	-0.0422	0.265	-28.2721	-27.0253	-4.4051
6	0.2368	0.1002	-0.0438	0.2	0.0597	0.0491	0.0769	-0.036	-0.1033	0.0553	-0.0393	-0.0085	0.1164	-0.0919	0	0.2059	-0.0414	0.0065	0.1909	0.0052	0.1819	-38.2713	-24.9262	4.5509
7	0.0681	-0.0382	0.0619	0.0681	0.0306	0.0493	0.1248	0.0439	-0.0202	-0.1635	-0.0402	0.099	0.0396	0.0199	0	0.257	-0.0218	0.0334	0.2839	-0.0145	0.2054	-42.7618	-20.2577	-13.6035
8	-0.0009	-0.0004	-0.0049	0.002	0.0069	0.0041	-0.0593	-0.0308	0.0723	-0.0513	0.0379	0.0363	0.0449	-0.0228	0	0.2425	-0.0569	-0.0061	0.3417	-0.0301	0.256	-53.4454	-22.9218	-15.3375
9	0.0064	-0.0042	0.0164	0.0041	0.0023	0.0214	0.0401	0.1073	-0.0315	-0.1081	0.1066	0.015	0.1407	-0.0554	0.0001	0.2687	-0.055	0.0461	0.2579	-0.0637	0.2834	-40.5354	-31.4276	-12.1385
10	0.0014	0.0081	-0.0003	0.02	0.0227	-0.0114	-0.0547	-0	-0.0243	-0.2392	0.0838	-0.1743	0.0521	-0.0105	0	0.2449	-0.0596	0.0062	0.2315	-0.0202	0.2889	-43.354	-30.6868	-14.0704
11	0.088	0.0482	0.0581	0.0132	0.0001	0.0911	0.0212	-0.1068	-0.0489	0.1012	-0.0194	-0.0448	-0.0056	-0.0293	-0	0.2495	0.0279	0.0029	0.2318	-0.0395	0.2073	-19.2913	-6.703	16.2218
12	0.0617	0.0062	0.1647	0.0856	0.0258	0.2016	-0.0199	-0.0742	-0.0302	0.0562	-0.0024	-0.0097	-0.0416	-0.0543	-0	0.1835	0.0144	0.0201	0.1829	-0.0362	0.1688	-27.3498	-4.6575	11.3926
13	0.1371	0.1513	0.1579	0.1043	0.03	0.1486	-0.0685	-0.1096	0.0068	-0.0168	0.0751	-0.0374	-0.0547	0.1064	0.0002	0.222	0.016	0.0191	0.1851	-0.0379	0.1848	-20.9572	-5.28	5.8501
14	0.486	0.1516	0.1122	0.4888	0.1401	0.3171	-0.0604	-0.0501	-0.0557	0.0665	0.0718	-0.1461	-0.0899	0.1126	-0	0.1713	-0.0049	-0.0096	0.2338	-0.0566	0.2261	-3.1251	-2.0755	10.6253
15	0.2034	-0.0555	0.0331	0.1547	-0.1205	0.0686	-0.0919	-0.0319	0.0808	-0.0128	0.0697	-0.0995	-0.2013	0.1105	-0.0039	0.2491	-0.0531	-0.0257	0.2226	-0.0749	0.2252	-4.1891	11.0476	11.0275
16	0.0282	-0.0151	-0.0053	0.0354	-0.018	0.0097	-0.0149	-0.0282	-0.0675	0.0154	0.0427	-0.0765	-0.0827	0.1162	-0	0.2462	-0.0121	-0.0326	0.2765	-0.048	0.216	-2.4551	-0.8072	20.2537
17	0.1083	0.0657	0.0653	0.0518	0.0362	0.0569	-0.0114	-0.0998	0.068	0.115	-0.0066	-0.0683	-0.1451	0.0426	0	0.2912	0.006	-0.0174	0.2666	-0.0605	0.212	-13.1714	2.2414	23.1215
18	0.0054	0.0054	0.0009	0.0071	-0.0027	0.0083	-0.0225	0.0325	-0.1143	-0.0434	0.0618	0.1031	0.0709	0.1033	0	0.2989	-0.0922	-0.0131	0.3476	-0.0329	0.2696	-11.6151	4.3279	-19.8025
19	0.0038	-0.0038	-0.0019	-0.0016	-0.0008	0.0059	0.0082	0.1058	0.0327	-0.0414	0.0712	0.052	-0.0091	0.0364	-0	0.3494	-0.1629	0.0498	0.5373	-0.0366	0.2278	-3.7851	8.1915	-24.5587
20	-0.0047	-0.0324	0.0225	0.0629	-0.0901	0.1194	-0.1722	0.208	0.2956	-0.1004	0.0754	-0.0156	-0.4407	0.2632	-0.0593	0.4125	-0.1963	-0.0175	0.3279	0.0577	0.2688	-6.6484	19.322	-18.3892
21	0.0702	-0.0016	-0.009	0.0309	0.0331	0.232	-0.1058	0.2886	-0.0243	-0.0645	0.147	0.0079	-0.0367	0.7911	0.02	0.2547	-0.1268	0.0308	0.4242	-0.1021	0.36	7.0722	3.5729	-9.4523
22	0.0135	-0.0277	0.0379	0.0894	-0.0945	0.2216	-0.0481	0.1856	-0.1019	0.0214	-0.0343	-0.0391	-0.1352	0.0811	-0.0035	0.2118	-0.1404	0.0662	0.5891	-0.1281	0.5006	16.8979	5.1172	-7.6662
23	0.0193	-0.0085	0.0027	0.0378	-0.0078	0.0105	-0.0536	0.0329	-0.1239	-0.0905	-0.1699	0.0087	0.0556	0.2534	-0.0728	0.1649	-0.3217	0.2235	0.8938	-0.074	0.3191	8.1153	4.8303	-20.9253

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	( CHAIN A AND RESID 3:98 )	A	3 - 98
2	X-RAY DIFFRACTION	2	( CHAIN A AND RESID 99:131 )	A	99 - 131
3	X-RAY DIFFRACTION	3	( CHAIN A AND RESID 132:321 )	A	132 - 321
4	X-RAY DIFFRACTION	4	( CHAIN A AND RESID 322:394 )	A	322 - 394
5	X-RAY DIFFRACTION	5	( CHAIN B AND RESID 187:204 )	B	187 - 204
6	X-RAY DIFFRACTION	6	( CHAIN B AND RESID 205:251 )	B	205 - 251
7	X-RAY DIFFRACTION	7	( CHAIN B AND RESID 252:279 )	B	252 - 279
8	X-RAY DIFFRACTION	8	( CHAIN B AND RESID 280:292 )	B	280 - 292
9	X-RAY DIFFRACTION	9	( CHAIN B AND RESID 293:302 )	B	293 - 302
10	X-RAY DIFFRACTION	10	( CHAIN B AND RESID 303:317 )	B	303 - 317
11	X-RAY DIFFRACTION	11	( CHAIN C AND RESID 2:25 )	C	2 - 25
12	X-RAY DIFFRACTION	12	( CHAIN C AND RESID 26:98 )	C	26 - 98
13	X-RAY DIFFRACTION	13	( CHAIN C AND RESID 99:131 )	C	99 - 131
14	X-RAY DIFFRACTION	14	( CHAIN C AND RESID 132:248 )	C	132 - 248
15	X-RAY DIFFRACTION	15	( CHAIN C AND RESID 249:321 )	C	249 - 321
16	X-RAY DIFFRACTION	16	( CHAIN C AND RESID 322:347 )	C	322 - 347
17	X-RAY DIFFRACTION	17	( CHAIN C AND RESID 348:393 )	C	348 - 393
18	X-RAY DIFFRACTION	18	( CHAIN D AND RESID 188:195 )	D	188 - 195
19	X-RAY DIFFRACTION	19	( CHAIN D AND RESID 196:204 )	D	196 - 204
20	X-RAY DIFFRACTION	20	( CHAIN D AND RESID 205:241 )	D	205 - 241
21	X-RAY DIFFRACTION	21	( CHAIN D AND RESID 242:279 )	D	242 - 279
22	X-RAY DIFFRACTION	22	( CHAIN D AND RESID 280:292 )	D	280 - 292
23	X-RAY DIFFRACTION	23	( CHAIN D AND RESID 293:314 )	D	293 - 314

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