PDB-6mn4: Crystal structure of aminoglycoside acetyltransferase AAC(3)-IVa,...

ID or keywords:

Entry

Database: PDB / ID: 6mn4

Title

Crystal structure of aminoglycoside acetyltransferase AAC(3)-IVa, H154A mutant, in complex with apramycin

Components

Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

Keywords

TRANSFERASE/ANTIBIOTIC / ANTIBIOTIC_NAT FAMILY / ACETYLTRANSFERASE / AMINOGLYCOSIDE / ANTIBIOTIC RESISTANCE / COENZYME A / APRAMYCIN / AAC(3)-IVA / CSGID / TRANSFERASE / CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES / National Institute of Allergy and Infectious Diseases / NIAID / TRANSFERASE-ANTIBIOTIC complex

Function / homology

Function and homology information

aminoglycoside 3-N-acetyltransferase activity / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / response to antibiotic / metal ion binding
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.8 Å

Authors

Stogios, P.J. / Evdokimova, E. / Michalska, K. / Di Leo, R. / Savchenko, A. / Joachimiak, A. / Satchell, K.J. / Center for Structural Genomics of Infectious Diseases (CSGID)

Funding support

United States, 2items

Organization	Grant number	Country
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)	HHSN272201700060C	United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)	HHSN272201200026C	United States

Citation

Journal: Commun Biol / Year: 2022
Title: Structural and molecular rationale for the diversification of resistance mediated by the Antibiotic_NAT family.
Authors: Stogios, P.J. / Bordeleau, E. / Xu, Z. / Skarina, T. / Evdokimova, E. / Chou, S. / Diorio-Toth, L. / D'Souza, A.W. / Patel, S. / Dantas, G. / Wright, G.D. / Savchenko, A.

History

Deposition	Oct 1, 2018	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Oct 24, 2018	Provider: repository / Type: Initial release
Revision 1.1	Dec 18, 2019	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2	Apr 6, 2022	Group: Database references / Structure summary Category: chem_comp / citation ...chem_comp / citation / citation_author / database_2 Item: _chem_comp.pdbx_synonyms / _citation.country ..._chem_comp.pdbx_synonyms / _citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.3	Oct 11, 2023	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	6mn4_validation.pdf.gz	2 MB	Display	wwPDB validaton report
Full document	6mn4_full_validation.pdf.gz	2.1 MB	Display
Data in XML	6mn4_validation.xml.gz	67.5 KB	Display
Data in CIF	6mn4_validation.cif.gz	87.1 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/mn/6mn4 ftp://data.pdbj.org/pub/pdb/validation_reports/mn/6mn4	HTTPS FTP

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Related structure data

Related structure data	5ht0C 6mmzC 6mn0C 6mn3C 6mn5C 7kesC 7laoC 7lapC 3smaS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	6mn5-4 6mn5-5 6mn3-1 6mn5-2 6mn5-3 5ex2-2 6mn3-2 3u9q-d 4k8o-d 6bc4-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) Search similar-shape structures by Omokage search (details) 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
Other databases	TargetTrack: IDP96427

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

B: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

C: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

D: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

E: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

F: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

hetero molecules

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

1

A: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

hetero molecules

defined by author&software
29.2 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

hetero molecules

defined by author&software
29.1 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

hetero molecules

defined by author&software
29 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

hetero molecules

defined by author&software
29.1 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

5

E: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

hetero molecules

defined by author&software
29.1 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

6

F: Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

hetero molecules

defined by author&software
28.9 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	77.550, 130.507, 264.919
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 , 1 types, 6 molecules ABCDEF

#1: Protein	Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa Mass: 28057.070 Da / Num. of mol.: 6 / Mutation: H154A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: aacC4, aac(3), aac(3)-IV, aac(3)IV, B9T59_28975, BEN53_26235, BJJ90_27515, BK373_27930, BK400_28640, BVL39_27730, BZL31_07055, BZL69_29365, C5P01_27985, C7235_00480, CR538_26885, CWS33_26775, ...Gene: aacC4, aac(3), aac(3)-IV, aac(3)IV, B9T59_28975, BEN53_26235, BJJ90_27515, BK373_27930, BK400_28640, BVL39_27730, BZL31_07055, BZL69_29365, C5P01_27985, C7235_00480, CR538_26885, CWS33_26775, CXB56_01995, DK267_24825, DK268_23980, DK278_24785, DK279_23955, DK288_24810, DK289_23980, pEC012_00026 Plasmid: pET19bTEV / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)Gold References: UniProt: Q306W4, aminoglycoside 3-N-acetyltransferase

#1: Protein

Aminoglycoside N(3)-acetyltransferase, AAC(3)-IVa

Mass: 28057.070 Da / Num. of mol.: 6 / Mutation: H154A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli)
Gene: aacC4, aac(3), aac(3)-IV, aac(3)IV, B9T59_28975, BEN53_26235, BJJ90_27515, BK373_27930, BK400_28640, BVL39_27730, BZL31_07055, BZL69_29365, C5P01_27985, C7235_00480, CR538_26885, CWS33_26775, ...
Plasmid: pET19bTEV / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21(DE3)Gold
References: UniProt: Q306W4, aminoglycoside 3-N-acetyltransferase

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Non-polymers , 7 types, 369 molecules

#2: Chemical	ChemComp-AM2 / APRAMYCIN / NEBRAMYCIN II / 4-O-(3ALPHA-AMINO-6ALPHA-((4-AMINO-4-DEOXY-ALPHA-D-GLUCOPYRANOSYL)OXY)-2,3,4,5ABETA,6,7,8,8AALPHA-OCTAHYDRO-8BETA-HYDROXY-7BETA-(METHYLAMINO)PYRANO(3,2-B)PYRAN-2ALPHA-YL)-2-DEOXY-D-STREPTAMINE Mass: 539.577 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₂₁H₄₁N₅O₁₁
#3: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#4: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₂H₆O₂
#5: Chemical	ChemComp-PO4 / PHOSPHATE ION Mass: 94.971 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: PO₄
#6: Chemical	ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES Mass: 238.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₈H₁₈N₂O₄S / Comment: pH buffer*YM
#7: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₃H₈O₃
#8: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 339 / 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: 3.99 Å³/Da / Density % sol: 69.18 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1 M HEPES pH 7, 30% (w/v) PEG1k, 2.5 mM apramycin

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.97933 Å
Detector	Type: ADSC QUANTUM 210r / Detector: CCD / Date: Dec 6, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97933 Å / Relative weight: 1
Reflection	Resolution: 2.8→30 Å / Num. obs: 66374 / % possible obs: 95.2 % / Redundancy: 9 % / R_merge(I) obs: 0.183 / R_pim(I) all: 0.063 / Net I/σ(I): 12.77
Reflection shell	Resolution: 2.8→2.85 Å / Redundancy: 8.9 % / R_merge(I) obs: 1.771 / Mean I/σ(I) obs: 1.4 / Num. unique all: 3328 / CC_1/2: 0.776 / R_pim(I) all: 0.613 / % possible all: 97.1

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Processing

Software

Name	Version	Classification
PHENIX	(dev_3092: ???)	refinement
HKL-3000		data reduction
HKL-3000		data scaling
PHENIX		phasing
PHENIX		model building
PHENIX		model building

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 3SMA

3sma

Resolution: 2.8→29.327 Å / SU ML: 0.45 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 32.91

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.3043	3627	3 %	RANDOM
R_work	0.247	-	-	-
obs	0.2487	120976	94.66 %	-

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 2.8→29.327 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	11627	0	382	339	12348

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.005	12308
X-RAY DIFFRACTION	f_angle_d	0.975	16810
X-RAY DIFFRACTION	f_dihedral_angle_d	23.066	4477
X-RAY DIFFRACTION	f_chiral_restr	0.052	1923
X-RAY DIFFRACTION	f_plane_restr	0.006	2160

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 (%)
2.8-2.8368	0.3953	144	0.3483	4573	X-RAY DIFFRACTION	96
2.8368-2.8756	0.3506	145	0.3391	4573	X-RAY DIFFRACTION	95
2.8756-2.9167	0.425	135	0.3175	4556	X-RAY DIFFRACTION	97
2.9167-2.9602	0.3306	143	0.3166	4586	X-RAY DIFFRACTION	95
2.9602-3.0064	0.3594	134	0.3135	4481	X-RAY DIFFRACTION	95
3.0064-3.0556	0.36	142	0.3194	4557	X-RAY DIFFRACTION	96
3.0556-3.1083	0.3901	143	0.3064	4566	X-RAY DIFFRACTION	94
3.1083-3.1647	0.3697	145	0.3165	4500	X-RAY DIFFRACTION	96
3.1647-3.2255	0.3355	136	0.2961	4481	X-RAY DIFFRACTION	94
3.2255-3.2913	0.3663	142	0.2942	4522	X-RAY DIFFRACTION	95
3.2913-3.3627	0.3836	139	0.2864	4497	X-RAY DIFFRACTION	93
3.3627-3.4408	0.3955	136	0.2902	4473	X-RAY DIFFRACTION	94
3.4408-3.5268	0.366	141	0.2836	4431	X-RAY DIFFRACTION	92
3.5268-3.6219	0.3229	133	0.2745	4449	X-RAY DIFFRACTION	94
3.6219-3.7283	0.2995	136	0.2597	4412	X-RAY DIFFRACTION	92
3.7283-3.8484	0.2833	139	0.2415	4355	X-RAY DIFFRACTION	92
3.8484-3.9856	0.3512	137	0.2457	4396	X-RAY DIFFRACTION	92
3.9856-4.1448	0.2847	134	0.2382	4299	X-RAY DIFFRACTION	91
4.1448-4.3329	0.2853	142	0.2276	4390	X-RAY DIFFRACTION	91
4.3329-4.5605	0.2738	136	0.2148	4370	X-RAY DIFFRACTION	92
4.5605-4.845	0.2804	133	0.2071	4480	X-RAY DIFFRACTION	94
4.845-5.2172	0.2638	136	0.202	4565	X-RAY DIFFRACTION	96
5.2172-5.7387	0.2667	151	0.2203	4671	X-RAY DIFFRACTION	99
5.7387-6.561	0.2583	146	0.2279	4788	X-RAY DIFFRACTION	99
6.561-8.2357	0.2405	137	0.2128	4743	X-RAY DIFFRACTION	100
8.2357-29.3288	0.2621	142	0.2047	4635	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	2.4255	1.0974	-0.8292	3.0185	-1.1006	2.595	-0.0179	0.005	-0.2218	0.0317	0.0136	0.0696	-0.1895	0.1687	0.0382	0.2065	-0.0226	-0.0114	0.6827	-0.0278	0.41	-28.9273	24.0962	-16.3654
2	4.7814	-2.6831	0.1021	5.3958	-2.0934	1.2971	0.0929	-0.9053	-0.2429	0.0938	-0.2537	-0.1505	0.0344	0.0153	0.1318	0.2659	-0.0284	-0.0227	0.8862	0.0264	0.435	-27.9705	19.125	-3.8317
3	5.5938	-1.9417	2.5979	3.6336	0.7439	2.13	0.2297	-1.2243	-0.3572	0.8709	0.2032	0.4725	0.2078	-0.9825	-0.3339	0.287	0.0236	0.1727	0.8763	0.0483	0.4951	-40.7051	20.2457	-2.6168
4	3.4098	-0.5115	1.528	5.5697	-2.4802	2.959	-0.3531	-0.2534	-0.8584	0.4828	-0.0293	0.0318	-0.2032	-0.0626	0.3671	0.2881	0.0052	0.0077	0.7347	0.0266	0.6554	-44.4536	9.9079	-6.1022
5	1.839	0.7575	-0.9743	4.4427	0.9988	5.3941	0.2302	-0.9065	-0.4484	0.6388	-0.0511	-0.1902	-0.719	-0.5311	0.041	0.5961	0.1501	0.0809	0.7864	0.2248	0.8638	-37.3929	4.0378	2.7614
6	3.4212	3.3646	-2.8105	7.2152	-3.7618	2.5314	-0.0683	0.1821	0.4021	-0.4038	0.1633	1.3455	-0.029	-0.2163	-0.0732	0.3029	-0.0574	-0.0735	0.7989	-0.0835	0.4853	-46.7347	19.3273	-21.6199
7	8.0584	2.0665	-1.6202	6.6759	-2.5177	3.1057	0.0333	-0.0115	-0.6024	-0.1003	0.0485	0.6538	0.3051	-0.1631	-0.0327	0.2179	0.0201	-0.0129	0.5134	0.0207	0.4634	-50.4406	9.9447	-13.4798
8	3.2639	1.6758	1.6491	4.1967	-0.4044	6.5173	-0.0544	-0.1806	0.2734	0.3498	0.3149	0.3249	-0.4126	-0.6143	-0.2344	0.2635	0.0569	0.0033	0.7315	0.0432	0.4151	-7.0375	21.4187	3.6412
9	7.3061	0.1993	4.3553	3.0143	-0.076	3.2315	0.1076	0.6242	-0.4525	-0.1712	-0.0225	-0.3646	0.0436	0.1953	-0.0712	0.2517	0.0284	0.0244	0.5813	-0.0476	0.3994	-6.3	14.2992	-14.3121
10	4.7961	1.4899	-0.8358	3.1205	2.6141	3.7151	-0.202	0.245	-0.7549	-0.3321	-0.2202	0.2026	0.135	-0.3928	0.4211	0.3455	0.1059	-0.05	0.5039	-0.0234	0.719	-2.1249	0.7843	-17.0012
11	2.6942	-1.3683	0.0497	6.2345	3.3372	4.7645	-0.0403	-0.4733	-1.0245	0.4225	0.1557	-0.2397	0.5343	0.4719	-0.1338	0.3404	0.0155	-0.0174	0.4981	0.1429	0.7728	7.3318	1.7778	-2.7128
12	5.323	-3.0973	-3.0831	6.7032	3.9787	8.2572	0.2332	0.0944	0.1861	-0.3371	0.2377	0.0195	0.1807	-0.5796	-0.4429	0.2729	-0.0352	-0.0651	0.7319	0.1836	0.3717	-3.3401	17.3687	22.5243
13	2.3885	1.1735	-1.2396	6.4899	-2.2751	5.2313	0.0701	-0.304	0.1236	0.3776	0.0831	0.4705	0.2027	-0.1884	-0.158	0.4057	0.117	-0.0099	0.8339	0.0974	0.3877	-6.102	11.8651	39.0644
14	7.3341	1.4436	-3.6226	4.5571	-0.7978	2.3707	0.3446	-0.191	0.4915	0.4889	-0.0319	0.6258	-0.7381	-1.0847	-0.3377	0.5131	0.1008	0.1684	0.9803	0.1031	0.5889	-14.8554	22.418	41.2338
15	7.8681	-0.9631	-1.7352	3.2938	1.57	2.7122	-0.0729	0.2861	-1.1663	0.3238	-0.2249	0.7198	0.1997	-0.5584	0.331	0.7665	0.0355	0.4653	1.4935	0.2931	0.8855	-24.5883	12.0863	48.9999
16	6.5731	-0.598	-4.0248	4.9171	0.7276	2.4541	0.3596	0.3795	1.3461	-0.3175	0.277	0.8529	-0.3252	-0.8024	-0.5567	0.5611	0.2719	0.1352	1.2774	0.2632	0.8097	-17.9652	28.8042	29.0704
17	5.2479	3.912	2.2957	4.3929	-0.0535	4.2508	0.4678	0.2151	-0.9158	0.111	0.2009	-0.1571	-0.2389	-0.6297	-0.6661	0.5193	0.0943	0.1099	1.6803	0.3758	1.3679	-35.5412	21.6179	36.8698
18	0.9166	0.0462	0.3235	8.6933	-0.6076	4.6258	0.1618	0.3058	-0.076	-0.026	-0.1557	-0.0061	0.0486	-0.5301	-0.0343	0.3392	-0.0512	0.0188	0.8443	-0.0698	0.3404	-33.0785	26.408	-41.4738
19	3.3764	-0.0069	-2.0107	3.1104	2.7844	6.1364	-0.2415	0.8223	-0.3327	-0.8561	0.2772	-0.3605	-0.5955	0.2638	-0.0057	0.5923	-0.1478	0.1141	0.8755	-0.1175	0.4429	-25.6038	23.5362	-58.9902
20	1.9929	1.0324	0.4848	0.8265	-0.3547	1.4098	-0.2575	0.1548	-0.9015	-0.5562	0.5769	-0.9698	0.6525	1.2086	0.0488	0.8514	-0.2367	0.3982	1.5185	-0.5078	1.0698	-11.7014	20.193	-60.9312
21	1.6833	-0.3319	-1.385	3.9989	0.111	1.1417	-0.5002	0.0332	-0.117	0.3316	0.5924	-1.4869	0.0412	0.4285	-0.2925	0.475	-0.1581	0.0053	1.2864	-0.155	0.69	-13.8867	31.5573	-40.7848
22	6.8147	-0.2928	-3.0154	0.5751	1.1883	3.3862	0.0554	0.2851	-0.1772	-0.2875	0.8142	-1.1334	-0.1088	1.5553	-0.7793	0.6685	-0.181	0.1603	1.4013	-0.4826	1.0681	-5.6082	26.8348	-49.4536
23	2.1463	0.455	-0.4804	3.3876	3.0644	6.1231	-0.2497	0.2746	-0.175	0.1624	-0.7428	0.5692	0.856	-1.6784	0.5855	0.8415	-0.262	0.2496	1.1598	-0.487	0.7777	-44.316	8.7917	-57.2996
24	1.7361	0.5715	1.0814	1.8319	0.6242	1.5025	0.1694	-0.0023	-0.925	0.8426	-0.3646	0.3117	1.9507	-1.0701	0.1598	2.1974	-0.6483	0.4679	1.2231	-0.4035	1.2106	-46.1342	-9.9129	-54.1263
25	2.7346	-1.94	-0.0343	7.5386	-3.3705	8.0237	0.1431	0.2103	-0.2233	-1.348	-1.3564	-0.769	1.9733	2.3574	0.497	1.0391	0.262	0.1996	1.1624	0.4648	0.7684	2.1344	-5.3817	37.5297
26	1.6123	0.0855	0.1105	2.2465	-0.0595	0.2326	0.2049	0.0952	-1.4603	-1.593	-0.5196	0.5715	2.5586	0.2707	0.0855	3.2321	0.369	0.0079	1.1434	0.2895	1.397	-4.1342	-21.7253	33.9281

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 0 through 71 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 72 through 114 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 115 through 143 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 144 through 172 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 173 through 190 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 191 through 213 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 214 through 257 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 0 through 52 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 53 through 143 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 144 through 190 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 191 through 257 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 0 through 39 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 40 through 114 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 115 through 159 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 160 through 190 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 191 through 232 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 233 through 257 )
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 0 through 52 )
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 53 through 143 )
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 144 through 190 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 191 through 213 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 214 through 257 )
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 0 through 114 )
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 115 through 257 )
25	X-RAY DIFFRACTION	25	chain 'F' and (resid 0 through 103 )
26	X-RAY DIFFRACTION	26	chain 'F' and (resid 104 through 250 )

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