PDB-6hr8: HMG-CoA reductase from Methanothermococcus thermolithotrophicus i...

ID or keywords:

Entry

Database: PDB / ID: 6hr8

Title

HMG-CoA reductase from Methanothermococcus thermolithotrophicus in complex with NADPH at 2.9 A resolution

Components

(HMG-CoA reductase) x 2

Keywords

OXIDOREDUCTASE / HMG-CoA / Mevalonate biosynthesis / statins / cholesterol biosynthesis / isoprenoids / NADPH / structural rearrangement.

Function / homology

Function and homology information

hydroxymethylglutaryl-CoA reductase (NADPH) / hydroxymethylglutaryl-CoA reductase (NADPH) activity / coenzyme A metabolic process / isoprenoid biosynthetic process
Similarity search - Function

Biological species

Methanothermococcus thermolithotrophicus DSM 2095 (archaea)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.9 Å

Authors

Wagner, T. / Voegeli, B. / Erb, T.J. / Shima, S.

Funding support

Germany, 1items

Citation

Journal: Febs Lett. / Year: 2019
Title: Crystal structure of archaeal HMG-CoA reductase: insights into structural changes of the C-terminal helix of the class-I enzyme.
Authors: Vogeli, B. / Shima, S. / Erb, T.J. / Wagner, T.

History

Deposition	Sep 26, 2018	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Feb 13, 2019	Provider: repository / Type: Initial release
Revision 1.1	Mar 20, 2019	Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc Item: _citation.journal_abbrev / _citation.journal_id_ISSN ..._citation.journal_abbrev / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.name
Revision 1.2	Jan 24, 2024	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	6hr8.cif.gz	912.1 KB	Display	PDBx/mmCIF format
PDB format	pdb6hr8.ent.gz	773.4 KB	Display	PDB format
PDBx/mmJSON format	6hr8.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	6hr8_validation.pdf.gz	2.4 MB	Display	wwPDB validaton report
Full document	6hr8_full_validation.pdf.gz	2.4 MB	Display
Data in XML	6hr8_validation.xml.gz	79.4 KB	Display
Data in CIF	6hr8_validation.cif.gz	104.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/hr/6hr8 ftp://data.pdbj.org/pub/pdb/validation_reports/hr/6hr8	HTTPS FTP

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Related structure data

Related structure data	6hr7SC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	6hr7-1 1hwi-d 1hw8-d 6m4o-d 7k0q-d 1dqa-d 6p4f-1 7cqi-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
Related items in Molecule of the Month	#96 - Dec 2007 Oxidosqualene Cyclase similarity (12)

Deposited unit

A: HMG-CoA reductase

B: HMG-CoA reductase

C: HMG-CoA reductase

D: HMG-CoA reductase

E: HMG-CoA reductase

F: HMG-CoA reductase

hetero molecules

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

1

A: HMG-CoA reductase

B: HMG-CoA reductase

C: HMG-CoA reductase

D: HMG-CoA reductase

hetero molecules

defined by author&software
Evidence: gel filtration, Other archaeal and human homologs are tetrameric
191 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: HMG-CoA reductase

F: HMG-CoA reductase

hetero molecules

E: HMG-CoA reductase

F: HMG-CoA reductase

hetero molecules

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

Unit cell

Length a, b, c (Å)	231.790, 231.790, 98.714
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	90
Space group name H-M	P42₁2

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Protein , 2 types, 6 molecules ABCDEF

#1: Protein	HMG-CoA reductase Mass: 46653.793 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The residue 233 is an oxidized cysteine. The N-terminal contains the poly-histidine tag. The C-terminal was too flexible to be modelled. Side chain of K87 was truncated because of an absence of electron density. Source: (gene. exp.) Methanothermococcus thermolithotrophicus DSM 2095 (archaea) Gene: HMGR / Plasmid: pET-28b / Production host: Escherichia coli BL21 (bacteria) / Variant (production host): BL21 AI References: UniProt: A0A4V8GZY0*PLUS, hydroxymethylglutaryl-CoA reductase (NADPH)
#2: Protein	HMG-CoA reductase Mass: 46637.793 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Details: The N-terminal contains the poly-histidine tag. The C-terminal was too flexible to be modelled. Side chain of D24 was truncated because of an absence of electron density. Source: (gene. exp.) Methanothermococcus thermolithotrophicus DSM 2095 (archaea) Gene: HMGR / Plasmid: pET-28b / Production host: Escherichia coli BL21 (bacteria) / Variant (production host): BL21 AI References: UniProt: A0A4V8GZY0*PLUS, hydroxymethylglutaryl-CoA reductase (NADPH)

#1: Protein

HMG-CoA reductase

Mass: 46653.793 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The residue 233 is an oxidized cysteine. The N-terminal contains the poly-histidine tag. The C-terminal was too flexible to be modelled. Side chain of K87 was truncated because of an absence of electron density.
Source: (gene. exp.)

Methanothermococcus thermolithotrophicus DSM 2095 (archaea)
Gene: HMGR / Plasmid: pET-28b / Production host:

Escherichia coli BL21 (bacteria) / Variant (production host): BL21 AI
References: UniProt: A0A4V8GZY0*PLUS, hydroxymethylglutaryl-CoA reductase (NADPH)

#2: Protein

HMG-CoA reductase

Mass: 46637.793 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Details: The N-terminal contains the poly-histidine tag. The C-terminal was too flexible to be modelled. Side chain of D24 was truncated because of an absence of electron density.
Source: (gene. exp.)

Methanothermococcus thermolithotrophicus DSM 2095 (archaea)
Gene: HMGR / Plasmid: pET-28b / Production host:

Escherichia coli BL21 (bacteria) / Variant (production host): BL21 AI
References: UniProt: A0A4V8GZY0*PLUS, hydroxymethylglutaryl-CoA reductase (NADPH)

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Non-polymers , 4 types, 22 molecules

#3: Chemical	ChemComp-NAP / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE Mass: 743.405 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₂₁H₂₈N₇O₁₇P₃
#4: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO₄
#5: Chemical	ChemComp-PEG / DI(HYDROXYETHYL)ETHER Mass: 106.120 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C₄H₁₀O₃
#6: Chemical	ChemComp-NA / SODIUM ION Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 2.37 Å³/Da / Density % sol: 48.19 % / Description: Prism shape
Crystal grow	Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: HMGR at 10 mg/ml was supplemented with a final concentration of 2 mM NADPH. The sample was centrifuged for 5 minute at 13.000 RPM to remove any aggregates and dust. 0.7 ul of protein sample ...Details: HMGR at 10 mg/ml was supplemented with a final concentration of 2 mM NADPH. The sample was centrifuged for 5 minute at 13.000 RPM to remove any aggregates and dust. 0.7 ul of protein sample was spotted on a 96-well 2-drop MRC Crystallization Plates (Molecular Dimensions, Suffolk, UK) and 0.7 ul of reservoir solution was mixed. The best crystals were obtained after several month using a solution containing 40% v/v PEG 400, 100 mM Tris PH 8.5 and 200 mM Li2SO4. Temp details: The temperature was fluctuating of +/- 3 degree

Crystal

Density Matthews: 2.37 Å³/Da / Density % sol: 48.19 % / Description: Prism shape

Crystal grow

Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: HMGR at 10 mg/ml was supplemented with a final concentration of 2 mM NADPH. The sample was centrifuged for 5 minute at 13.000 RPM to remove any aggregates and dust. 0.7 ul of protein sample ...
Temp details: The temperature was fluctuating of +/- 3 degree

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.97662 Å
Detector	Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 12, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97662 Å / Relative weight: 1
Reflection	Resolution: 2.9→25 Å / Num. obs: 59867 / % possible obs: 99.8 % / Redundancy: 7.3 % / B_iso Wilson estimate: 93.25 Å² / CC_1/2: 0.999 / R_merge(I) obs: 0.095 / R_pim(I) all: 0.037 / R_rim(I) all: 0.102 / Net I/σ(I): 13.3
Reflection shell	Resolution: 2.9→3.06 Å / Redundancy: 7.7 % / R_merge(I) obs: 1.285 / Mean I/σ(I) obs: 1.6 / Num. unique obs: 8592 / CC_1/2: 0.427 / R_pim(I) all: 0.491 / R_rim(I) all: 1.377 / % possible all: 100

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Processing

Software

Name	Version	Classification
PHENIX	(1.10.1_2155: ???)	refinement
XDS	3.3.22	data reduction
SCALA		data scaling
PHASER	2.6.0	phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 6HR7

6hr7

Resolution: 2.9→24.987 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.26
Details: For the last round of refinement, many side chains have been truncated were the electron density was absent. The last round of refinement has been done with hydrogens in riding position. ...

	R_factor	Num. reflection	% reflection
R_free	0.2426	2998	5.01 %
R_work	0.2111	-	-
obs	0.2127	59830	99.96 %

Solvent computation

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

Displacement parameters

B_iso mean: 113 Å²

Refinement step

Cycle: LAST / Resolution: 2.9→24.987 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	17794	0	279	0	18073

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.003	18318
X-RAY DIFFRACTION	f_angle_d	0.653	24793
X-RAY DIFFRACTION	f_dihedral_angle_d	17.28	11011
X-RAY DIFFRACTION	f_chiral_restr	0.047	2939
X-RAY DIFFRACTION	f_plane_restr	0.003	3126

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 (%)
2.9-2.9475	0.3884	124	0.3405	2635	X-RAY DIFFRACTION	100
2.9475-2.9982	0.3594	135	0.3344	2697	X-RAY DIFFRACTION	100
2.9982-3.0527	0.3465	142	0.3324	2644	X-RAY DIFFRACTION	100
3.0527-3.1113	0.3423	144	0.321	2685	X-RAY DIFFRACTION	100
3.1113-3.1746	0.3559	160	0.3177	2649	X-RAY DIFFRACTION	100
3.1746-3.2435	0.3306	144	0.2941	2658	X-RAY DIFFRACTION	100
3.2435-3.3188	0.2889	142	0.2957	2685	X-RAY DIFFRACTION	100
3.3188-3.4016	0.2583	149	0.2713	2661	X-RAY DIFFRACTION	100
3.4016-3.4934	0.3415	140	0.2632	2688	X-RAY DIFFRACTION	100
3.4934-3.5959	0.2612	129	0.2606	2689	X-RAY DIFFRACTION	100
3.5959-3.7116	0.2689	156	0.2422	2668	X-RAY DIFFRACTION	100
3.7116-3.8438	0.2582	129	0.2279	2707	X-RAY DIFFRACTION	100
3.8438-3.9971	0.2417	140	0.218	2711	X-RAY DIFFRACTION	100
3.9971-4.1782	0.2161	130	0.2075	2705	X-RAY DIFFRACTION	100
4.1782-4.3974	0.2221	147	0.1968	2701	X-RAY DIFFRACTION	100
4.3974-4.6712	0.2285	154	0.1834	2720	X-RAY DIFFRACTION	100
4.6712-5.0291	0.203	131	0.1795	2731	X-RAY DIFFRACTION	100
5.0291-5.5303	0.2354	138	0.1944	2747	X-RAY DIFFRACTION	100
5.5303-6.3192	0.2679	139	0.2047	2760	X-RAY DIFFRACTION	100
6.3192-7.9192	0.1963	180	0.1906	2752	X-RAY DIFFRACTION	100
7.9192-24.9876	0.2088	145	0.1578	2939	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	1.7196	-0.2397	0.8026	2.113	1.4763	2.0623	0.9335	-0.0295	-1.5654	-0.6504	0.2688	-1.5877	0.7417	0.4131	-0.413	1.6117	-0.0188	-0.1101	1.0695	-0.4538	1.8459	266.4507	43.6486	93.8133
2	0.8933	-0.0235	-0.6266	5.094	-0.1752	1.4948	-0.1787	1.0787	-0.6151	-1.4064	-0.0795	-0.4201	-0.6745	-0.2084	0.0644	1.4419	-0.221	0.1504	1.55	-0.6274	1.1992	259.3668	55.655	92.3634
3	1.6593	0.0388	0.0265	2.4555	0.7122	1.3597	0.046	0.7048	-0.4219	-0.7731	-0.0468	-0.4437	-0.1124	0.0681	0.0069	0.7146	-0.0254	0.078	0.8073	-0.1579	0.6227	259.8683	77.5622	111.7611
4	2.093	0.8109	0.392	4.1124	-0.8375	2.547	0.114	-0.4274	-0.6002	0.558	-0.1974	-1.2594	-0.1973	0.5897	0.1099	0.609	0.0576	-0.156	0.769	0.0829	1.2336	274.6221	63.3937	134.9505
5	1.5798	-0.2583	-0.7184	2.4136	0.4148	1.9739	0.0589	-0.2867	-1.0913	-0.1916	0.0542	-0.4103	0.3447	0.488	0.0212	0.6651	0.0133	-0.1214	0.616	-0.043	1.3068	273.6919	57.0287	130.8046
6	3.5034	-0.2737	-0.2429	2.6801	-0.7753	2.5153	0.0335	0.4547	-0.3888	-0.3244	0.0345	-0.0077	-0.145	0.2723	-0.1033	0.5673	-0.0355	-0.0946	0.555	-0.1255	0.5042	253.63	80.9905	120.2437
7	5.474	0.7236	-0.2269	2.0835	-0.4682	4.1104	0.1487	0.973	0.574	-0.1701	0.0759	-0.0032	-0.5553	-0.6122	-0.2355	0.6418	0.0467	0.0043	0.6477	-0.1039	0.3269	247.09	85.7269	118.0375
8	4.4027	-0.1149	-1.8789	2.8253	-0.6808	4.8784	0.4888	1.4355	1.1908	0.1792	0.5128	-0.2373	1.1285	-0.7408	-0.593	1.6123	-0.0225	0.0807	1.5214	-0.0563	1.0472	251.8049	94.0092	93.2708
9	1.8055	-1.1485	0.0604	1.8282	-0.5829	1.3405	0.0217	2.6139	1.1028	-0.3418	-0.7707	-0.6078	0.1538	0.1549	0.0121	1.502	-0.1306	0.1306	1.4681	-0.2219	0.7675	258.8743	81.8973	93.7927
10	1.3853	0.1074	-1.0868	0.5745	-0.2428	1.2093	-0.2563	0.3314	-0.5503	-0.7602	0.26	-0.1728	0.2014	-0.0519	0.0064	0.8545	-0.0924	0.0377	0.9089	-0.3077	0.8496	249.8367	57.5675	108.0907
11	4.0131	-0.7695	0.1665	3.6328	1.3121	4.5334	0.0424	0.8245	-1.0425	-0.2204	-0.2108	0.4342	0.2732	-0.6851	0.0618	0.5125	0.0493	-0.1746	0.7526	-0.1878	0.7891	225.6814	69.5132	122.4543
12	2.1567	0.3736	-1.2978	3.3127	0.8706	3.8408	0.0071	0.6206	-0.3256	-0.6634	0.043	-0.0622	-0.4273	-0.6218	-0.0663	0.6108	0.0759	-0.0994	0.6765	-0.1421	0.5628	228.3494	76.3847	120.0886
13	1.7909	0.3846	0.7283	1.7305	-0.2222	3.4097	-0.4405	0.0142	-1.1252	0.2184	0.1825	-0.0113	0.2818	0.3963	0.2576	0.6263	0.0699	0.0286	0.576	-0.1519	1.3288	255.0506	48.8934	125.4095
14	1.7089	0.5161	-0.2925	3.3057	-0.9363	3.7266	-0.5385	-0.1841	-0.2912	-1.0501	0.4266	-0.6877	0.6088	-0.3989	0.2463	0.7071	0.0161	0.0588	0.8188	-0.2994	0.9739	251.5908	54.1405	118.7946
15	2.1834	-0.1205	0.1304	2.9437	0.1823	2.8839	-0.1516	0.6903	-0.6089	-0.5129	-0.0233	-0.2771	0.2118	0.1379	0.1947	0.7927	-0.0624	0.1203	0.8653	-0.4145	1.0704	250.9401	54.3898	110.1454
16	1.9456	0.6652	-1.9705	3.2977	-1.1477	4.1331	0.4609	0.2817	0.4897	-0.6327	-0.1762	0.006	0.3741	1.006	-0.7287	1.4556	-0.0101	0.1498	1.4257	-0.1474	0.9982	229.7276	87.5379	173.8788
17	1.1256	-1.0809	0.6014	1.9087	0.2796	2.0298	-0.0598	-0.961	-0.2651	0.7251	-0.0788	-0.0819	0.0171	0.1568	0.128	1.0552	-0.1471	-0.1602	1.2454	0.3419	0.7802	245.6854	62.8956	165.786
18	3.0617	0.5563	0.4064	3.3842	-1.4847	3.9567	0.2504	-0.8191	-0.3384	0.6458	-0.228	-0.5609	-0.4147	0.2822	0.0001	0.6961	-0.1485	-0.1901	0.7653	0.0729	0.5989	263.6717	85.0376	146.6003
19	0.711	-0.09	0.3869	4.652	-0.3658	0.9974	-0.0597	-0.5295	-0.3068	0.1512	-0.0725	-0.5522	-0.0689	-0.0174	0.0153	0.6461	-0.1073	-0.0819	0.7996	0.1786	0.6812	256.4228	74.204	145.4475
20	1.8735	0.9004	0.1284	2.8208	-0.5948	3.5422	0.1927	-0.5833	-1.0777	0.1693	-0.0509	-0.7705	0.5267	0.5353	0.0869	0.7639	0.0657	-0.2225	0.7391	0.3752	1.1215	250.5374	50.6982	147.5201
21	4.8757	-2.8457	-4.4123	1.7693	2.7127	4.4314	-0.8849	-0.1598	-1.199	-0.0959	0.597	0.0858	0.3728	1.0734	0.1389	0.8346	0.1424	-0.1268	0.9313	0.3092	1.1467	258.6594	47.3158	143.9528
22	2.8064	-0.4722	-0.0344	2.4481	0.0217	2.2396	0.2661	-0.7143	-0.114	0.8846	-0.2942	-0.3939	0.38	0.4281	0.0682	1.0093	-0.0454	-0.132	1.0654	0.2662	0.7276	253.2537	55.8195	158.7492
23	1.4322	-0.3355	1.5457	3.0725	-0.2704	2.0812	0.6359	-0.4356	-0.606	0.9853	0.0063	-0.1257	-0.1072	-0.3082	-0.6059	1.6478	-0.1639	-0.2201	1.5152	0.5279	1.0259	246.6029	46.8389	176.2472
24	2.1541	-0.0567	-0.0062	1.4415	-0.5034	1.17	0.1031	-0.8582	-0.4978	0.6832	0.0069	0.2272	-0.1115	-0.303	-0.042	0.8329	-0.0996	-0.0195	1.0539	0.2682	0.5467	232.3889	69.0873	156.4368
25	2.4411	-1.5282	-0.9899	4.1351	0.6655	3.7413	-0.02	-0.1275	-0.9791	-0.0543	0.0105	0.4772	0.6111	-0.2694	-0.0209	0.6445	-0.1317	-0.0589	0.6181	0.1125	1.1769	231.5439	46.2969	135.926
26	3.6005	-0.0481	-0.9441	1.9218	0.1142	2.2226	0.3151	-0.8023	-0.3758	0.3027	-0.3027	0.0983	-0.1266	0.091	0.0551	0.6811	-0.0752	-0.1429	0.7304	0.1112	0.4289	235.9658	76.7097	148.1161
27	1.3861	0.2566	-0.3284	0.7833	0.6394	0.63	-0.7609	0.3941	0.2439	-0.6868	0.9954	0.7231	0.6326	0.7635	0.2843	1.1003	-0.3305	0.2189	2.1703	-0.3201	1.2914	179.1932	28.0242	136.8648
28	0.0452	0.2867	-0.0726	1.2717	0.6213	0.8746	-0.113	-0.5483	0.689	0.2514	-0.0139	0.4124	-0.0496	-0.3385	-0.0016	0.9232	-0.1668	-0.1445	1.3134	-0.3674	1.6709	207.6884	37.819	117.8326
29	1.47	0.5805	1.7083	2.7216	0.9065	2.7376	0.1922	-0.4827	0.0929	0.5618	-0.5892	0.2317	0.393	-0.5796	0.3554	0.8962	-0.2982	0.0401	1.1207	-0.0942	1.2853	212.6543	17.708	115.0413
30	1.1787	1.1082	0.3083	3.6926	1.5102	4.247	0.9654	0.0967	0.396	1.4252	-0.4023	-0.424	1.5007	-2.5516	-0.4581	1.7138	-0.3742	-0.1432	1.5178	0.1489	1.0366	207.9908	7.5193	138.6594
31	1.5115	0.129	0.5309	-0.1906	0.2271	1.8762	0.0919	-0.9184	0.1463	0.5602	-0.3451	0.7098	0.2507	-0.9073	0.266	0.9797	-0.3677	0.1733	1.6456	-0.3798	2.0257	186.6455	22.4692	119.1613
32	5.1571	0.8773	-1.4198	2.7169	0.0364	3.467	0.1139	-0.55	0.2835	-0.168	-0.1121	0.3935	0.431	-0.2895	-0.0607	0.992	-0.1724	-0.1047	0.88	-0.0881	1.0732	195.6939	1.9937	96.9338
33	2.2122	-1.8107	-0.3946	1.762	0.8825	1.6695	0.3479	-0.1688	0.8517	0.2471	-0.6893	-0.4245	0.0894	-0.6016	0.3522	0.8062	-0.2356	-0.0682	1.1298	-0.3414	1.5376	192.4382	20.5153	103.6228
34	4.5828	-1.8646	-2.9995	0.5074	1.0104	3.713	1.0766	-1.1544	2.2651	0.1088	-0.3698	-1.128	-0.7338	-0.4042	0.1963	1.0028	-0.1402	-0.1905	1.0173	-0.73	2.5486	191.2753	41.3356	106.4605
35	1.9848	-0.1127	-0.5509	-0.0385	-0.135	1.0115	-0.1706	-0.9613	0.9594	0.3297	-0.3605	0.3718	-0.2609	-0.1892	0.507	0.7936	-0.2197	0.0847	1.4142	-0.5715	1.7169	188.2105	29.4227	111.085
36	1.53	0.0379	-1.5398	0.3494	-0.8992	2.0723	0.2998	-0.527	0.415	1.4058	-1.0118	0.6701	-0.2159	-0.6299	0.6029	0.9843	-0.3274	-0.0111	1.7091	-0.5346	1.7919	184.7658	25.6488	117.4605

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 5 through 27 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 28 through 56 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 57 through 137 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 138 through 197 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 198 through 239 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 240 through 369 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 370 through 401 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 5 through 27 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 28 through 56 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 57 through 137 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 138 through 197 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 198 through 239 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 240 through 296 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 297 through 338 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 339 through 400 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 6 through 27 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 28 through 133 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 134 through 219 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 220 through 255 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 256 through 319 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 320 through 338 )
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 339 through 401 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 6 through 56 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 57 through 137 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 138 through 239 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 240 through 401 )
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 6 through 56 )
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 57 through 239 )
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 240 through 401 )
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 6 through 56 )
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 57 through 137 )
32	X-RAY DIFFRACTION	32	chain 'F' and (resid 138 through 219 )
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 220 through 264 )
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 265 through 296 )
35	X-RAY DIFFRACTION	35	chain 'F' and (resid 297 through 338 )
36	X-RAY DIFFRACTION	36	chain 'F' and (resid 339 through 401 )

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