PDB-4l63: Apo form of AB5 holotoxin

ID or keywords:

Entry

Database: PDB / ID: 4l63

Title

Apo form of AB5 holotoxin

Components

ECXA
ECXB

Keywords

HYDROLASE /

MATRIX METALLOPROTEASE /

AB5 TOXIN / OB FOLD / CHOLERA-LIKE TOXIN /

PENTAMER /

TOXIN /

PROTEASE /

GM1 / TOXILYSIN

Function / homology

Function and homology information

metallopeptidase activity / extracellular region /

metal ion binding
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.8 Å

Authors

Littler, D.R. / Ng, N.M. / Rossjohn, J. / Beddoe, T.

Citation

Journal: Structure / Year: 2013
Title: EcxAB Is a Founding Member of a New Family of Metalloprotease AB5 Toxins with a Hybrid Cholera-like B Subunit.
Authors: Ng, N.M. / Littler, D.R. / Paton, A.W. / Le Nours, J. / Rossjohn, J. / Paton, J.C. / Beddoe, T.

History

Deposition	Jun 11, 2013	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Nov 27, 2013	Provider: repository / Type: Initial release
Revision 1.1	Sep 20, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4l63.cif.gz	331.4 KB	Display	PDBx/mmCIF format
PDB format	pdb4l63.ent.gz	272.9 KB	Display	PDB format
PDBx/mmJSON format	4l63.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/l6/4l63 ftp://data.pdbj.org/pub/pdb/validation_reports/l6/4l63	HTTPS FTP

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Related structure data

Related structure data	4l6tC 2wv6S S: Starting model for refinement C: citing same article (ref.)
Similar structure data	7khs-1 3hxm-d 2as0-d 5g2e-4 6tm4-d 2nvv-1 2nvv-3 5g2e-5 1ko7-d 6s2b-d 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	#69 - Sep 2005 Cholera Toxin similarity (3) #28 - Apr 2002 Anthrax Toxin similarity (1) #237 - Sep 2019 Nanodiscs and HDL similarity (1) #44 - Aug 2003 Calmodulin similarity (1)

Deposited unit

A: ECXA

B: ECXB

C: ECXB

D: ECXB

E: ECXB

F: ECXB

hetero molecules

94.6 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	120.530, 120.530, 273.510
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	179
Space group name H-M	P6₅22

#1: Protein	ECXA Mass: 29492.879 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: 176 / Gene: ecxA / Plasmid: pBAD / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) References: UniProt: Q8GAV4, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases
#2: Protein	ECXB Mass: 12775.468 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: 176 / Gene: ecxB / Plasmid: pBAD / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: Q8GAV3
#3: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#4: Chemical	ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES / HEPES Mass: 238.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C₈H₁₈N₂O₄S / Comment: pH buffer*YM
#5: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 435 / 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: 3.09 Å³/Da / Density % sol: 60.15 %
Crystal grow	Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: 0.1M HEPES and 0.6M Na/K/PO4, VAPOR DIFFUSION, HANGING DROP, temperature 295K, pH 4.5

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.953699 Å
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: 2011 / Details: MONOCHROMATOR
Radiation	Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.953699 Å / Relative weight: 1
Reflection	Resolution: 1.8→39.5 Å / Num. obs: 109241 / % possible obs: 99.9 % / Observed criterion σ(I): 1.4 / Redundancy: 11.9 % / R_merge(I) obs: 0.072 / Net I/σ(I): 8.2

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Processing

Software

Name	Version	Classification
ADSC	Quantum	data collection
PHASER		phasing
PHENIX	(phenix.refine: 1.8.1_1168)	refinement
MOSFLM		data reduction
SCALA		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2WV6

2wv6

Resolution: 1.8→45.211 Å / SU ML: 0.19 / Isotropic thermal model: ISOTROPIC / σ(F): 1.33 / Phase error: 18.57 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1973	5289	5.02 %
R_work	0.1771	-	-
obs	0.1781	105445	96.86 %

Solvent computation

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

Displacement parameters

B_iso mean: 10.1 Å²

Refinement step

Cycle: LAST / Resolution: 1.8→45.211 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	6036	0	76	435	6547

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	6251
X-RAY DIFFRACTION	f_angle_d	1.093	8450
X-RAY DIFFRACTION	f_dihedral_angle_d	15.268	2373
X-RAY DIFFRACTION	f_chiral_restr	0.048	953
X-RAY DIFFRACTION	f_plane_restr	0.006	1077

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 (%)
1.8-1.8205	0.3404	160	0.2964	3323	X-RAY DIFFRACTION	99
1.8205-1.8419	0.3007	179	0.2772	3350	X-RAY DIFFRACTION	99
1.8419-1.8643	0.2925	179	0.2597	3329	X-RAY DIFFRACTION	98
1.8643-1.8879	0.2671	200	0.2503	3319	X-RAY DIFFRACTION	98
1.8879-1.9128	0.279	168	0.2358	3365	X-RAY DIFFRACTION	98
1.9128-1.939	0.2344	191	0.2158	3318	X-RAY DIFFRACTION	98
1.939-1.9667	0.2382	153	0.2106	3360	X-RAY DIFFRACTION	98
1.9667-1.996	0.2207	175	0.2098	3322	X-RAY DIFFRACTION	98
1.996-2.0272	0.2279	175	0.2169	3334	X-RAY DIFFRACTION	98
2.0272-2.0605	0.2123	182	0.201	3350	X-RAY DIFFRACTION	98
2.0605-2.096	0.2153	173	0.1821	3337	X-RAY DIFFRACTION	98
2.096-2.1341	0.2034	186	0.1835	3306	X-RAY DIFFRACTION	98
2.1341-2.1752	0.2108	183	0.1797	3334	X-RAY DIFFRACTION	98
2.1752-2.2196	0.198	160	0.1755	3351	X-RAY DIFFRACTION	98
2.2196-2.2678	0.2012	164	0.1742	3356	X-RAY DIFFRACTION	98
2.2678-2.3206	0.2001	171	0.173	3352	X-RAY DIFFRACTION	97
2.3206-2.3786	0.1857	169	0.1747	3316	X-RAY DIFFRACTION	97
2.3786-2.4429	0.1936	190	0.1691	3320	X-RAY DIFFRACTION	97
2.4429-2.5148	0.1953	183	0.1782	3341	X-RAY DIFFRACTION	97
2.5148-2.5959	0.2128	176	0.1774	3302	X-RAY DIFFRACTION	97
2.5959-2.6887	0.2032	175	0.1815	3354	X-RAY DIFFRACTION	97
2.6887-2.7964	0.2134	184	0.1816	3319	X-RAY DIFFRACTION	96
2.7964-2.9236	0.2111	174	0.1803	3319	X-RAY DIFFRACTION	96
2.9236-3.0777	0.2069	176	0.1867	3335	X-RAY DIFFRACTION	96
3.0777-3.2705	0.1971	168	0.1788	3320	X-RAY DIFFRACTION	95
3.2705-3.5229	0.1801	159	0.1618	3320	X-RAY DIFFRACTION	95
3.5229-3.8773	0.1604	194	0.1513	3329	X-RAY DIFFRACTION	95
3.8773-4.4379	0.1554	179	0.1407	3333	X-RAY DIFFRACTION	94
4.4379-5.5896	0.1753	173	0.1451	3378	X-RAY DIFFRACTION	94
5.5896-45.2256	0.2016	190	0.1942	3464	X-RAY DIFFRACTION	91

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	1.5392	0.2791	0.2393	3.4038	-0.208	3.0572	0.1349	0.2812	-0.5648	-0.2204	0.1969	0.2229	1.3022	0.3954	0.3133	0.8058	0.2343	-0.2136	0.4727	-0.1482	0.4569	19.8682	21.922	5.0933
2	0.7682	-0.5533	0.5655	0.4242	-0.6038	1.5447	-0.1769	-0.5279	-0.9675	-0.0395	0.7538	0.4892	1.0889	-0.7696	-0.1712	1.2615	-0.2639	-0.2582	0.7939	0.3078	1.5223	7.0742	7.2454	19.4874
3	1.857	0.2568	-0.2473	1.4813	1.1806	1.0547	0.439	0.0231	-1.1176	-0.1847	0.1192	0.3114	1.6652	0.2101	0.1867	1.4013	0.095	-0.2783	0.4838	-0.0669	0.9743	18.423	9.7513	10.8908
4	1.9722	-0.7151	0.3916	3.807	3.097	3.0274	0.0168	-0.6449	-0.8013	0.1804	0.6289	0.3927	0.9928	-0.0077	0.0824	1.2643	0.0881	-0.1404	0.8948	0.2516	0.6828	15.2576	12.5729	26.0463
5	2.6633	1.9021	4.5402	4.4267	1.2921	8.9807	-0.2293	-0.6925	-0.2321	0.2938	0.3947	1.0299	-0.1723	-0.372	-0.2338	0.9436	-0.0418	0.3554	1.511	0.5934	1.0733	1.2273	24.8667	29.83
6	3.6004	-0.8943	0.7088	3.0329	-0.9624	3.2301	0.1417	-0.4675	-0.7113	0.3786	0.2841	0.4039	0.7511	-0.2478	-0.1347	0.5736	0.0551	-0.0629	0.4286	0.0402	0.487	14.6951	24.9137	14.3876
7	8.3475	-1.0736	-1.4431	4.4284	0.2099	4.4541	0.009	-0.283	-0.6056	0.04	0.3374	1.0218	0.9408	-0.5435	-0.0135	0.5376	-0.0744	-0.0991	0.4584	0.0744	0.6338	8.642	24.7804	7.7571
8	5.0968	-1.9739	-0.4451	5.3919	-0.5481	4.3768	0.0141	0.3161	-0.1564	0.0043	0.1577	-0.3986	0.3756	0.3577	-0.0524	0.3146	0.0303	-0.0665	0.4748	-0.1245	0.3446	18.5486	35.6968	-3.5661
9	6.7821	-2.7355	0.783	1.1848	-0.4399	0.2761	-0.0154	0.3284	-0.072	-0.1422	0.0859	0.2257	-0.0634	-0.1739	0.2782	0.0941	-0.1973	-0.1377	1.0512	0.0414	0.3421	-14.7749	49.2094	-13.5328
10	0.6689	0.5992	-0.2088	1.8472	0.8315	0.8585	-0.0259	0.6372	0.1171	-0.5522	-0.1039	0.4257	-0.085	-0.4636	-0.0034	0.3517	-0.1958	-0.2231	1.1101	-0.026	0.2638	-10.9572	44.6279	-22.9864
11	8.5054	4.1829	-3.5254	2.7712	-2.1625	2.0517	0.1423	-0.2551	-0.6544	-0.0365	-0.223	0.0827	0.3046	-0.0244	0.0907	0.3392	-0.1752	-0.0162	0.6384	-0.2447	0.3646	0.5709	33.2974	-15.8285
12	2.1975	-0.2988	-0.0848	0.2346	0.3142	1.2504	-0.0728	1.1704	0.102	-0.3852	0.1093	0.1421	0.0321	-0.2226	-0.1485	0.2943	-0.1904	-0.0655	0.8308	-0.1129	0.2212	5.6087	46.3881	-24.8724
13	3.9872	-1.3419	0.1131	2.3366	-0.7746	1.4489	0.0075	0.6621	0.323	-0.0912	0.1452	0.0544	-0.2032	-0.2092	-0.0029	0.1009	-0.1036	-0.0953	0.6114	-0.096	0.1386	5.2317	49.8183	-14.8699
14	2.8345	-0.0148	0.6424	0.1862	0.2267	0.8921	-0.2851	0.8788	-0.0319	-0.2106	0.1751	0.0313	0.0234	-0.1511	-0.803	0.2472	-0.232	-0.0752	0.8977	-0.0856	0.2441	-3.6262	42.021	-21.2427
15	0.2002	-0.5265	0.0844	1.5228	0.2111	1.7605	-0.0652	0.2658	-0.2856	0.0343	0.1732	0.3151	0.2803	-0.1764	-0.2378	0.1694	-0.0675	-0.0445	0.5689	-0.0549	0.2684	-4.1477	41.6456	-11.8193
16	0.0062	0.1064	0.0573	4.0228	1.1166	0.6691	-0.113	-0.1176	0.6906	0.0024	0.0265	0.5475	0.0833	-0.1858	0.0271	0.2061	0.043	-0.0203	0.4317	-0.1072	0.3818	-2.7131	62.753	14.2992
17	2.3687	0.8818	-0.2453	1.1827	-0.529	1.503	-0.109	-0.2418	0.4851	0.0622	-0.0162	0.2263	-0.2521	-0.5384	-0.2632	0.0823	0.1003	-0.0435	0.5464	-0.1033	0.3838	-11.3654	58.3073	8.801
18	4.2193	-0.2307	-1.1987	3.2938	3.1762	5.3292	0.1231	-0.4353	-0.303	0.3631	-0.1006	0.0685	0.466	-0.067	0.1552	0.1521	-0.0068	0.0094	0.4068	-0.0379	0.3046	-5.3161	42.3316	5.5458
19	1.1452	-0.1567	0.2801	0.7856	0.669	0.9373	-0.1198	0.3431	0.3097	-0.2722	0.1077	0.1925	-0.2165	-0.2298	-0.1177	0.1175	-0.004	-0.0513	0.5019	0.0296	0.2993	-7.4863	53.1345	-6.8022
20	1.9726	-0.8448	-0.0558	5.4149	0.7176	0.9491	0	0.4065	0.1897	-0.2113	0.0258	0.0346	-0.0919	-0.0325	0.0058	0.0927	-0.0193	-0.0422	0.4174	-0.0429	0.1977	2.435	54.6498	-3.5653
21	2.3393	0.1465	0.3418	1.287	0.2559	0.9988	-0.1167	0.0923	0.1856	0.1381	-0.0083	0.0351	0.071	-0.1572	-0.0035	0.1015	0.0076	-0.0103	0.3972	-0.0403	0.2315	-5.9067	52.4353	5.3966
22	2.6206	2.142	-0.2793	2.2582	-0.2877	0.2363	-0.0073	0.1505	0.1239	0.1324	0.3261	-0.2982	-0.1176	0.4154	0.2031	0.1823	0.0078	-0.0679	0.4317	-0.126	0.3106	30.1411	63.9016	11.3262
23	4.6981	0.0304	-0.5736	2.4033	-2.3006	6.2308	0.2383	-0.1857	0.4775	0.7824	-0.0993	-0.0499	-0.5506	0.2274	0.1852	0.2185	-0.0183	-0.0427	0.2502	-0.117	0.2015	20.9629	65.4745	17.483
24	5.1776	0.8379	5.6293	3.3242	0.4337	6.2345	0.1936	-0.3701	-0.5122	0.5165	0.0871	-0.2791	0.3161	0.146	-0.1665	0.1894	0.0319	-0.0624	0.2758	-0.066	0.1779	14.586	48.7844	16.4039
25	2.1352	0.5534	-0.163	0.7603	0.3216	0.5889	-0.0043	0.1632	0.3928	0.033	0.0353	0.1774	-0.1029	-0.0329	-0.0675	0.136	0.0258	-0.0385	0.2613	-0.052	0.2445	6.8485	61.729	9.408
26	2.9032	2.8058	-0.6901	5.4995	-0.6905	0.8003	-0.1261	0.2537	0.2739	-0.0612	0.1123	-0.0741	-0.1145	-0.0297	-0.0581	0.1077	0.01	-0.0383	0.3101	-0.0486	0.1981	13.2842	58.0092	1.9229
27	2.1293	1.0178	0.5804	2.3004	0.684	1.7897	-0.022	-0.04	0.2952	0.2901	-0.0064	0.0585	-0.0506	-0.0592	0.0625	0.1577	0.0255	-0.0531	0.2501	-0.0801	0.1941	15.7599	59.8779	14.8586
28	0.9767	0.2369	0.5059	0.2525	-0.6056	3.2594	-0.0215	-0.0191	-0.1411	0.2349	-0.0598	-0.2867	0.3628	0.1906	0.0904	0.1423	0.0164	-0.0535	0.2594	-0.0745	0.2448	21.5138	54.1568	11.1196
29	1.1625	1.032	-0.391	3.4971	-1.7826	1.0715	-0.3386	0.5129	-0.0676	-0.4197	-0.0986	-0.2186	-0.0581	0.2713	-0.1355	0.2303	-0.0444	0.0534	0.6509	-0.0489	0.3436	38.4743	51.0779	-17.0503
30	5.5806	-1.0581	1.7057	1.8451	0.0711	2.3934	-0.3083	0.5417	0.4732	-0.1028	-0.0712	-0.2051	-0.3009	0.3701	0.0217	0.1341	-0.0583	-0.0056	0.608	-0.0047	0.2944	41.6005	55.4649	-7.8225
31	4.3728	-4.8085	-4.4261	6.7541	4.2173	5.4292	-0.273	-0.0372	-0.7666	0.0691	0.0198	-0.1673	0.4047	0.6063	0.0973	0.1174	0.0544	-0.0121	0.3908	-0.046	0.36	32.6782	43.827	2.2592
32	1.831	0.2878	-0.7734	0.9099	0.7884	1.2438	-0.0106	0.2696	0.2679	0.1085	0.051	-0.3976	-0.1609	0.2667	0.21	0.1224	-0.0165	-0.0458	0.3529	-0.0414	0.3009	28.5278	59.704	1.6388
33	2.4217	1.6381	-1.7782	3.1964	-2.1693	3.6917	-0.1219	0.4917	0.2869	-0.135	0.1468	0.0229	-0.0383	-0.1904	-0.1633	0.1137	-0.0141	-0.0255	0.4126	-0.0485	0.2755	22.7409	55.2355	-5.9844
34	5.6958	4.551	-5.9401	5.5132	-3.2627	7.3729	-0.0051	-0.0161	-0.3639	0.1058	-0.1914	-0.1458	0.2243	0.0409	0.0744	0.1605	-0.0323	0.0388	0.4055	-0.1241	0.3474	29.7587	42.2657	-2.0541
35	3.9123	0.806	0.0419	1.5686	0.1584	1.734	-0.1392	0.05	0.4627	-0.0208	0.0014	0.0179	-0.0769	0.2324	-0.1449	0.0818	-0.0323	-0.028	0.4563	-0.0244	0.3387	37.8397	57.8292	-3.464
36	3.2367	-2.6935	-1.6922	2.6147	0.9327	2.6	-0.1388	0.1779	-0.5231	0.0214	-0.1614	0.0306	0.2622	0.1923	-0.1959	0.086	0.008	0.0193	0.4545	-0.0536	0.2868	32.0041	46.4909	-7.766
37	0.8943	-0.0578	-0.3855	2.4306	-0.8195	3.4661	-0.0412	0.714	-0.0385	-0.4962	-0.1702	0.3022	0.2042	-0.11	0.0686	0.4883	-0.2003	-0.006	1.0066	-0.2232	0.295	11.4093	42.0657	-32.9956
38	2.8341	-1.2068	0.835	1.4456	0.7663	2.1722	-0.0353	1.0151	0.0125	-0.3297	-0.1297	-0.069	0.0128	0.1439	-0.2608	0.4256	-0.1145	0.1379	1.0381	-0.2248	0.2106	21.9052	42.7761	-33.1172
39	3.8909	4.2837	3.5929	6.6316	4.4744	6.0863	0.1	0.3566	-0.7093	-0.0503	-0.194	-0.0458	1.0338	0.181	-0.1185	0.4081	0.0489	0.0786	0.5778	-0.2949	0.4961	24.2775	34.2051	-17.9169
40	2.4681	1.0351	0.3513	1.3417	0.0507	2.49	-0.1068	0.6779	-0.1676	-0.2089	0.0313	-0.1079	0.0129	0.239	-0.0853	0.1667	-0.0205	0.0569	0.5876	-0.096	0.2873	29.4567	47.9726	-17.566
41	2.1978	-0.787	1.045	3.2123	-2.17	3.6235	-0.1736	0.6962	0.2386	-0.3429	0.0428	-0.2542	-0.1123	-0.0025	0.0828	0.1977	-0.0651	0.0051	0.5857	-0.0511	0.2479	19.0959	52.2274	-18.8477
42	1.1574	-0.3316	0.1512	0.5471	0.9376	3.928	-0.0627	0.6743	-0.1961	-0.2165	0.0224	-0.3053	0.2123	0.2539	0.1041	0.2753	-0.1001	0.0893	0.8119	-0.1959	0.302	23.7449	42.3818	-25.4193
43	1.7125	-0.2682	0.5716	1.0967	-0.2903	6.1189	-0.0313	0.4059	-0.2003	-0.2083	0.0228	0.0812	0.5475	-0.0681	0.0665	0.2173	-0.1333	-0.0499	0.815	-0.268	0.1718	16.6365	40.0118	-22.5029

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 21 through 56 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 57 through 89 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 90 through 133 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 134 through 149 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 150 through 164 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 165 through 234 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 235 through 258 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 259 through 278 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 0 through 11 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 12 through 19 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 20 through 25 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 26 through 58 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 59 through 78 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 79 through 94 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 95 through 104 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 0 through 11 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 12 through 19 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 20 through 25 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 26 through 58 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 59 through 78 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 79 through 104 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 0 through 11 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 12 through 19 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 20 through 25 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 26 through 58 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 59 through 78 )
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 79 through 94 )
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 95 through 104 )
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 1 through 11 )
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 12 through 19 )
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 20 through 25 )
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 26 through 58 )
33	X-RAY DIFFRACTION	33	chain 'E' and (resid 59 through 78 )
34	X-RAY DIFFRACTION	34	chain 'E' and (resid 79 through 83 )
35	X-RAY DIFFRACTION	35	chain 'E' and (resid 84 through 94 )
36	X-RAY DIFFRACTION	36	chain 'E' and (resid 95 through 104 )
37	X-RAY DIFFRACTION	37	chain 'F' and (resid 1 through 11 )
38	X-RAY DIFFRACTION	38	chain 'F' and (resid 12 through 19 )
39	X-RAY DIFFRACTION	39	chain 'F' and (resid 20 through 25 )
40	X-RAY DIFFRACTION	40	chain 'F' and (resid 26 through 50 )
41	X-RAY DIFFRACTION	41	chain 'F' and (resid 51 through 78 )
42	X-RAY DIFFRACTION	42	chain 'F' and (resid 79 through 94 )
43	X-RAY DIFFRACTION	43	chain 'F' and (resid 95 through 103 )

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