PDB-4u1t: The crystal structure of holo CalE6, a methionine gamma lyase fro...

ID or keywords:

Entry

Database: PDB / ID: 4u1t

Title

The crystal structure of holo CalE6, a methionine gamma lyase from Micromonospora echinospora

Components

CalE6

Keywords

LYASE

Function / homology

Function and homology information

carbon-sulfur lyase activity / transsulfuration / pyridoxal phosphate binding / cytoplasm
Similarity search - Function

Biological species

Micromonospora echinospora (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2 Å

Authors

Song, H.G. / Guo, Z.H.

Citation

Journal: Chembiochem / Year: 2015
Title: Identification and Characterization of a Methionine gamma-Lyase in the Calicheamicin Biosynthetic Cluster of Micromonospora echinospora
Authors: Song, H. / Xu, R. / Guo, Z.

History

Deposition	Jul 16, 2014	Deposition site: RCSB / Processing site: PDBJ
Revision 1.0	Jan 7, 2015	Provider: repository / Type: Initial release
Revision 2.0	Nov 8, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Non-polymer description / Refinement description / Source and taxonomy / Structure summary Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / entity_src_gen / pdbx_initial_refinement_model / pdbx_struct_oper_list Item: _chem_comp.formula / _chem_comp.formula_weight ..._chem_comp.formula / _chem_comp.formula_weight / _chem_comp.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.formula_weight / _entity_src_gen.pdbx_alt_source_flag / _pdbx_struct_oper_list.symmetry_operation
Revision 2.1	Nov 15, 2023	Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/u1/4u1t ftp://data.pdbj.org/pub/pdb/validation_reports/u1/4u1t	HTTPS FTP

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Related structure data

Related structure data	4u2hC 3qi6S C: citing same article (ref.) S: Starting model for refinement
Similar structure data	4u2h-2 4u2h-1 6khq-1 4l0o-3 3qi6-d 4l0o-2 4q31-2 3qhx-d 3jbf-d 6k1m-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

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: CalE6

B: CalE6

C: CalE6

D: CalE6

E: CalE6

F: CalE6

G: CalE6

H: CalE6

hetero molecules

337 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: CalE6

B: CalE6

C: CalE6

D: CalE6

hetero molecules

defined by author&software
168 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: CalE6

F: CalE6

G: CalE6

H: CalE6

hetero molecules

defined by author&software
168 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	146.170, 146.220, 348.091
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	23
Space group name H-M	I222

#1: Protein	CalE6 Mass: 41981.336 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Micromonospora echinospora (bacteria) / Gene: calE6 / Plasmid: PET28A / Production host: Escherichia coli (E. coli) / References: UniProt: Q8KNG3, methionine gamma-lyase
#2: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: SO₄
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 2437 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION

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Sample preparation

Crystal	Density Matthews: 2.77 Å³/Da / Density % sol: 55.58 %
Crystal grow	Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.2 M ammonium sulfate, 0.1 M Bis-Tris, 17% PEG 3350

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9793 Å
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 15, 2012
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9793 Å / Relative weight: 1
Reflection	Resolution: 2→47.7 Å / Num. obs: 294248 / % possible obs: 99.9 % / Redundancy: 2 % / Net I/σ(I): 17

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Processing

Software

Name	Version	Classification
PHENIX	(phenix.refine: 1.8.4_1496)	refinement
HKL-2000		data collection
iMOSFLM		data scaling
PHASER		phasing
Coot		model building

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 3QI6

3qi6

Resolution: 2→47.661 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 17.46 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1843	12473	5.02 %
R_work	0.1515	-	-
obs	0.1532	248603	99.62 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 2→47.661 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	21897	0	40	2437	24374

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	22436
X-RAY DIFFRACTION	f_angle_d	1.07	30641
X-RAY DIFFRACTION	f_dihedral_angle_d	12.736	8021
X-RAY DIFFRACTION	f_chiral_restr	0.047	3588
X-RAY DIFFRACTION	f_plane_restr	0.006	4017

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 (%)
2-2.0227	0.2353	422	0.1799	7813	X-RAY DIFFRACTION	99
2.0227-2.0465	0.2192	409	0.1717	7825	X-RAY DIFFRACTION	100
2.0465-2.0715	0.2126	405	0.1692	7757	X-RAY DIFFRACTION	100
2.0715-2.0977	0.2053	401	0.154	7837	X-RAY DIFFRACTION	100
2.0977-2.1253	0.1799	401	0.1511	7803	X-RAY DIFFRACTION	100
2.1253-2.1544	0.1983	436	0.1488	7850	X-RAY DIFFRACTION	100
2.1544-2.1852	0.2142	416	0.151	7740	X-RAY DIFFRACTION	100
2.1852-2.2178	0.1928	428	0.1577	7827	X-RAY DIFFRACTION	99
2.2178-2.2525	0.2687	409	0.2196	7859	X-RAY DIFFRACTION	100
2.2525-2.2894	0.2208	395	0.1997	7763	X-RAY DIFFRACTION	99
2.2894-2.3289	0.2131	440	0.1616	7810	X-RAY DIFFRACTION	99
2.3289-2.3712	0.185	417	0.1437	7822	X-RAY DIFFRACTION	100
2.3712-2.4168	0.1894	375	0.1463	7854	X-RAY DIFFRACTION	100
2.4168-2.4661	0.186	362	0.1476	7904	X-RAY DIFFRACTION	100
2.4661-2.5198	0.1952	397	0.1531	7890	X-RAY DIFFRACTION	100
2.5198-2.5784	0.1877	401	0.1462	7862	X-RAY DIFFRACTION	100
2.5784-2.6428	0.1859	409	0.1414	7885	X-RAY DIFFRACTION	100
2.6428-2.7143	0.1841	409	0.1459	7864	X-RAY DIFFRACTION	100
2.7143-2.7942	0.1772	445	0.142	7871	X-RAY DIFFRACTION	100
2.7942-2.8843	0.189	416	0.1467	7881	X-RAY DIFFRACTION	100
2.8843-2.9874	0.1865	412	0.1495	7881	X-RAY DIFFRACTION	100
2.9874-3.107	0.1923	451	0.1492	7869	X-RAY DIFFRACTION	100
3.107-3.2484	0.1724	429	0.1424	7892	X-RAY DIFFRACTION	100
3.2484-3.4196	0.1826	418	0.1485	7904	X-RAY DIFFRACTION	100
3.4196-3.6338	0.1672	444	0.1498	7895	X-RAY DIFFRACTION	100
3.6338-3.9142	0.1607	420	0.1347	7974	X-RAY DIFFRACTION	100
3.9142-4.3079	0.1551	445	0.1329	7951	X-RAY DIFFRACTION	100
4.3079-4.9307	0.1483	415	0.1296	7946	X-RAY DIFFRACTION	100
4.9307-6.21	0.1863	426	0.1617	8060	X-RAY DIFFRACTION	100
6.21-47.6748	0.1863	420	0.1743	8041	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	1.4344	-0.3051	0.1731	0.274	-0.1787	0.6826	0.0173	0.0137	0.3673	-0.0189	-0.0058	-0.0283	-0.1568	-0.0419	-0.0017	0.1712	-0.0133	0.0153	0.0822	0.0006	0.1813	-30.5076	-20.2662	-52.8221
2	0.0666	0.0384	-0.1847	1.2875	-0.0863	1.0479	0.0352	0.6515	-0.1272	-0.3949	-0.0011	-0.2846	0.1657	0.0995	-0.0153	0.2322	0.0204	0.0785	0.4204	-0.0418	0.1193	-24.0517	-35.3659	-76.0314
3	0.7702	0.4106	0.4035	0.5996	-0.1777	1.1441	0.2081	0.7747	0.0351	-0.4601	-0.1429	-0.3983	0.1795	-0.029	0.5326	0.3228	0.045	0.2437	0.4631	0.093	0.2198	-11.9483	-34.2857	-77.9241
4	0.7359	0.0328	-0.0529	0.6119	0.1449	0.3808	-0.0218	0.2651	0.1019	-0.2189	-0.0057	-0.122	-0.0186	-0.0255	0.0232	0.1321	-0.0092	0.0436	0.1655	0.0431	0.1082	-23.0044	-30.1754	-65.9224
5	0.5211	0.0351	0.1562	0.625	-0.1269	0.0473	-0.0229	0.0813	-0.0799	-0.0918	0.0069	-0.2625	-0.0004	0.04	0.0333	0.0857	-0.0111	0.066	0.1038	-0.0044	0.159	-10.2947	-45.8184	-57.844
6	2.1503	-0.5974	-0.6302	3.2139	1.0994	1.5226	-0.0579	0.0807	-0.1753	-0.2165	0.0844	-0.03	-0.0131	-0.0648	-0.028	0.0827	-0.0114	0.0273	0.0754	-0.0152	0.1397	-15.0547	-53.7457	-55.9482
7	1.6189	0.1709	0.1337	0.8583	0.129	0.7841	-0.0602	0.3985	-0.0656	-0.2003	0.0228	0.0515	0.0854	0.0464	-0.0062	0.1629	-0.0326	-0.013	0.1689	-0.018	0.0543	-49.6917	-40.0316	-68.2331
8	0.6749	0.0183	0.1459	1.3105	0.1849	0.549	-0.0714	0.1351	0.1999	-0.2219	0.0025	0.2244	-0.0642	-0.0895	0.0571	0.1052	-0.0219	-0.052	0.1157	0.0315	0.1503	-61.1486	-20.5135	-59.6216
9	1.4794	-0.2262	0.0106	0.7534	0.3234	0.8129	-0.0247	-0.4595	0.0156	0.1519	0.0073	0.0512	0.0251	-0.0171	0.0032	0.1202	-0.0151	0.0096	0.2218	-0.012	0.0848	-48.9745	-29.2855	-25.454
10	1.1601	0.5595	-0.04	0.8594	-0.031	0.3542	0.0025	-0.2195	-0.0458	0.0594	-0.0024	0.0842	0.0052	0.0074	0.015	0.0627	0.0062	0.0141	0.1119	0.009	0.079	-60.1764	-41.8498	-31.056
11	2.0951	0.1792	0.1126	0.6237	-0.0358	0.735	0.0399	-0.1332	-0.3574	-0.0123	-0.0145	0.0982	0.1911	-0.0834	-0.0123	0.1909	-0.0162	0.002	0.1091	0.0184	0.1504	-31.4899	-50.6125	-38.5459
12	0.337	-0.1891	0.5621	1.0179	-0.6485	2.0285	-0.1723	-0.7317	-0.0814	0.2833	0.1601	-0.2987	0.0036	0.1209	0.047	0.1462	0.0521	-0.0499	0.421	0.0218	-0.1352	-27.3936	-38.9924	-17.952
13	0.2051	0.0172	-0.266	0.7754	0.1984	0.8462	0.0394	-0.7956	0.0442	0.1943	-0.0637	-0.3132	-0.1488	0.1065	0.0059	0.1926	0.0468	-0.1036	0.5479	-0.0352	0.0695	-18.7758	-36.8127	-14.7222
14	0.785	-0.1587	-0.2691	0.8002	-0.0482	0.5609	-0.0014	-0.3214	0.0349	0.1029	0.0245	-0.1218	0.0613	0.0954	-0.0176	0.0707	-0.0085	-0.0199	0.1618	-0.0233	0.0759	-19.7355	-34.3396	-30.8875
15	0.7825	0.1123	0.3013	1.2716	0.0566	1.2757	-0.0486	-0.2763	0.2329	0.0764	0.1889	-0.0795	-0.2533	0.2019	0.0806	0.1073	-0.0406	0.007	0.1865	-0.117	0.2107	-13.4928	-19.3215	-32.2729
16	0.2431	-0.3713	0.0687	1.3908	-0.0407	0.5434	-0.0204	-0.0078	-0.0106	0.0216	0.0512	-0.4038	0.0537	0.163	-0.0148	0.0933	-0.0059	-0.0132	0.1612	0.0003	0.1837	-22.356	-41.477	-140.535
17	0.7057	0.3498	0.4388	0.652	0.4671	1.4975	0.0529	-0.2081	0.3022	0.8811	-0.0424	-0.063	0.0204	-0.1453	0.1548	0.3761	0.0029	-0.0295	0.1386	-0.0676	-0.0938	-35.015	-45.482	-161.21
18	0.6974	-0.2006	0.1903	0.8007	-0.0083	0.494	-0.0206	-0.2715	0.1508	0.4481	-0.0115	-0.0308	0.0377	-0.0333	0.0341	0.2737	-0.0203	-0.0221	0.1851	-0.044	0.0851	-35.806	-50.978	-160.562
19	1.1517	-0.1503	0.1258	0.7958	0.3246	0.5927	-0.0218	-0.1501	0.1614	0.1326	-0.052	0.1536	-0.04	-0.1146	0.0735	0.112	-0.0159	0.0227	0.0856	-0.0281	0.1262	-51.26	-59.901	-146.076
20	0.3399	-0.2915	0.0677	1.7079	0.0122	0.5766	-0.021	-0.0598	-0.0024	0.0998	0.0075	0.3201	-0.071	-0.1393	0.0323	0.098	-0.0073	0.0177	0.1623	-0.0035	0.1561	-52.144	-28.384	-140.679
21	1.3402	0.264	-0.4046	0.5303	-0.2901	1.7955	-0.0193	-0.3396	-0.1894	0.7445	-0.0433	-0.1062	0.0407	0.1222	-0.0527	0.3392	0.0054	-0.0083	0.1497	0.06	0.0594	-38.87	-23.1	-160.399
22	0.7677	0.0321	-0.1318	0.1722	0.3698	0.868	-0.1619	-0.7114	-0.2983	0.9607	-0.0867	-0.235	0.074	0.1565	-0.3049	0.675	0.1349	-0.2523	0.1428	0.4966	-0.364	-33.449	-17.015	-168.433
23	0.5853	-0.1278	-0.053	0.5222	0.1542	0.4165	-0.0443	-0.2719	-0.204	0.3074	-0.0155	0.097	0.0282	-0.012	0.0035	0.2018	-0.01	0.0439	0.1655	0.0682	0.1193	-40.348	-17.758	-154.918
24	0.5563	-0.0868	-0.0173	0.4764	0.1299	0.3346	-0.0302	-0.0975	-0.2445	0.113	0.0256	-0.0617	0.051	-0.0154	0.0205	0.0628	-0.0167	-0.0106	0.0563	0.0609	0.16	-26.223	-8.427	-144.164
25	2.2661	-0.3506	0.3765	1.8785	-0.596	1.81	-0.0199	-0.3636	-0.0137	0.2666	-0.0254	-0.1825	-0.1244	0.042	0.0099	0.0885	-0.0091	-0.034	0.1022	0.0194	0.1443	-17.926	-14.011	-145.622
26	0.4354	-0.1138	-0.1529	1.6162	-0.2167	0.5313	0.0175	-0.0267	-0.0274	0.0305	0.0041	-0.4795	0.0574	0.1094	-0.0309	0.0736	0.0056	-0.0184	0.1612	0.0044	0.1741	-22.0125	-27.5958	-127.9744
27	0.5424	0.6046	0.4323	1.0006	-0.058	1.8371	0.0981	-0.0897	-0.0365	0.439	-0.1462	-0.2681	0.0979	0.0504	0.0177	0.1944	-0.0226	-0.0277	0.1242	-0.0045	0.0548	-30.6545	-28.6359	-111.4002
28	0.7254	-0.0273	0.0125	0.9406	0.0139	0.6468	0.0448	-0.2711	0.0873	0.4343	-0.0833	0.0279	0.0381	-0.0331	0.0237	0.2387	-0.0416	0.0023	0.1817	-0.0369	0.0866	-36.3416	-20.0853	-105.2337
29	1.0793	-0.3195	-0.2106	0.4649	0.1459	0.6389	0.0263	-0.0687	0.0854	0.1034	-0.0068	0.174	-0.0285	-0.0688	-0.0172	0.0848	-0.0062	0.0359	0.0749	-0.0156	0.1433	-49.4242	-10.892	-119.2055
30	1.5409	-0.6135	-0.6668	0.7709	0.5015	0.6822	0.1524	0.238	0.252	-0.0216	-0.0632	0.1652	-0.3688	-0.2986	0.0518	0.0996	0.0573	0.0359	0.1031	0.0131	0.1807	-54.905	-8.695	-126.029
31	0.3792	-0.2826	0.0884	1.6916	0.4858	0.4109	0.0359	-0.0096	0.0157	0.0155	-0.1096	0.4635	-0.0415	-0.0708	0.0455	0.0885	0.0093	0.0266	0.1514	-0.0098	0.1733	-53.5545	-43.8608	-129.5637
32	0.6651	0.5751	-0.4924	0.9782	-0.2237	1.7337	0.0582	-0.0647	0.0042	0.5128	-0.1122	0.3106	0.0158	0.0145	-0.0495	0.2333	-0.0149	0.0316	0.1262	0.0061	0.0278	-46.0744	-44.228	-112.6075
33	1.166	-0.0655	0.2194	0.2472	0.1364	1.3111	-0.1367	-0.3019	-0.3821	0.8657	0.1236	-0.115	0.0537	0.1964	0.0827	0.5471	-0.005	0.0049	0.1892	0.1406	0.0623	-39.1375	-57.0338	-103.3614
34	0.8006	-0.0891	-0.0056	1.0677	0.1653	0.5336	0.015	-0.0883	-0.11	0.2249	0.0087	-0.1115	0.0441	0.0369	-0.0131	0.1179	-0.0008	-0.0224	0.0678	0.0228	0.0752	-33.2574	-57.0554	-119.0131
35	2.8418	-0.6254	0.8141	1.5516	-0.6864	1.9838	0.0801	-0.0952	0.0336	0.2023	-0.0666	-0.3011	0.0538	0.1437	0.0357	0.1152	0.0107	-0.0586	0.0814	-0.003	0.1831	-20.3909	-58.701	-123.3517

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 1 through 65 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 66 through 124 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 125 through 164 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 165 through 233 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 234 through 314 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 315 through 380 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 1 through 233 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 234 through 379 )
9	X-RAY DIFFRACTION	9	chain 'C' and (resid 1 through 143 )
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 144 through 378 )
11	X-RAY DIFFRACTION	11	chain 'D' and (resid 1 through 65 )
12	X-RAY DIFFRACTION	12	chain 'D' and (resid 66 through 100 )
13	X-RAY DIFFRACTION	13	chain 'D' and (resid 101 through 194 )
14	X-RAY DIFFRACTION	14	chain 'D' and (resid 195 through 284 )
15	X-RAY DIFFRACTION	15	chain 'D' and (resid 285 through 378 )
16	X-RAY DIFFRACTION	16	chain 'E' and (resid 1 through 65 )
17	X-RAY DIFFRACTION	17	chain 'E' and (resid 66 through 100 )
18	X-RAY DIFFRACTION	18	chain 'E' and (resid 101 through 233 )
19	X-RAY DIFFRACTION	19	chain 'E' and (resid 234 through 379 )
20	X-RAY DIFFRACTION	20	chain 'F' and (resid 1 through 65 )
21	X-RAY DIFFRACTION	21	chain 'F' and (resid 66 through 100 )
22	X-RAY DIFFRACTION	22	chain 'F' and (resid 101 through 143 )
23	X-RAY DIFFRACTION	23	chain 'F' and (resid 144 through 233 )
24	X-RAY DIFFRACTION	24	chain 'F' and (resid 234 through 314 )
25	X-RAY DIFFRACTION	25	chain 'F' and (resid 315 through 379 )
26	X-RAY DIFFRACTION	26	chain 'G' and (resid 1 through 38 )
27	X-RAY DIFFRACTION	27	chain 'G' and (resid 39 through 100 )
28	X-RAY DIFFRACTION	28	chain 'G' and (resid 101 through 233 )
29	X-RAY DIFFRACTION	29	chain 'G' and (resid 234 through 355 )
30	X-RAY DIFFRACTION	30	chain 'G' and (resid 356 through 378 )
31	X-RAY DIFFRACTION	31	chain 'H' and (resid 1 through 38 )
32	X-RAY DIFFRACTION	32	chain 'H' and (resid 39 through 100 )
33	X-RAY DIFFRACTION	33	chain 'H' and (resid 101 through 194 )
34	X-RAY DIFFRACTION	34	chain 'H' and (resid 195 through 314 )
35	X-RAY DIFFRACTION	35	chain 'H' and (resid 315 through 379 )

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