PDB-6huy: HmdII from Desulfurobacterium thermolithotrophum reconstitued wit...

ID or keywords:

Entry

Database: PDB / ID: 6huy

Title

HmdII from Desulfurobacterium thermolithotrophum reconstitued with Fe-guanylylpyridinol (FeGP) cofactor and co-crystallized with methenyl-tetrahydrofolate form A

Components

(Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related ...) x 2

Keywords

OXIDOREDUCTASE /

Hydrogenase / H2-activation / Lateral gene-transfer / cofactor biosynthesis /

tetrahydromethanopterin /

tetrahydrofolate /

paralog / sulfur-reducing bacteria /

metalloenzyme

Function / homology

Function and homology information

H(2)-forming methylenetetrahydromethanopterin dehydrogenase-related protein / H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase, C-terminal / HMD, C-terminal domain superfamily / H2-forming N5,N10-methylene-tetrahydromethanopterin dehydrogenase / 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily /

Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology

Biological species

Desulfurobacterium thermolithotrophum DSM 11699 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.25 Å

Authors

Watanabe, T. / Wagner, T. / Huang, G. / Kahnt, J. / Ataka, K. / Ermler, U. / Shima, S.

Funding support

Germany,

China, 2items

Citation

Journal: Angew. Chem. Int. Ed. Engl. / Year: 2019
Title: The Bacterial [Fe]-Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates.
Authors: Watanabe, T. / Wagner, T. / Huang, G. / Kahnt, J. / Ataka, K. / Ermler, U. / Shima, S.

History

Deposition	Oct 9, 2018	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jan 9, 2019	Provider: repository / Type: Initial release
Revision 1.1	Feb 6, 2019	Group: Data collection / Database references / Category: citation / citation_author / Item: _citation.title / _citation_author.identifier_ORCID
Revision 1.2	Mar 13, 2019	Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3	Jan 24, 2024	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 / struct_conn Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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 / _struct_conn.ptnr2_label_seq_id

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/hu/6huy ftp://data.pdbj.org/pub/pdb/validation_reports/hu/6huy	HTTPS FTP

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Related structure data

Related structure data	6huxC 6huzC 4yt4S S: Starting model for refinement C: citing same article (ref.)
Similar structure data	4yt5-d 4yt2-d 4yt8-d 6huz-1 3gnq-4 5e70-3 5kvq-d 6bit-2 4mw9-2 4gmg-2 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 - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#111 - Mar 2009 Hydrogenase similarity (5) #228 - Dec 2018 Directed Evolution of Enzymes similarity (1) #127 - Jul 2010 Crystallins similarity (1)

Deposited unit

A: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

B: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

C: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

D: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

hetero molecules

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

1

A: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

B: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

hetero molecules

defined by author&software
Evidence: gel filtration, The homolog in archaea has been shown to have a dimeric assembly (Fujishiro T. et al FEBS journal 282 (2015) 3412-3423).
84.2 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

D: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

hetero molecules

defined by author&software
84.1 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	99.769, 131.829, 168.263
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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Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related ... , 2 types, 4 molecules ACBD

#1: Protein	Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein Mass: 40994.000 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: synthetic gene Source: (gene. exp.) Desulfurobacterium thermolithotrophum DSM 11699 (bacteria) Tissue: / / Cell: / / Cell line: / / Gene: Dester_1504 / Organ: / / Details (production host): / / Cell (production host): / / Organ (production host): / / Production host: Escherichia coli BL21(DE3) (bacteria) / Tissue (production host): / References: UniProt: F0S2B6, 5,10-methenyltetrahydromethanopterin hydrogenase
#2: Protein	Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein Mass: 41010.000 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: synthetic gene Source: (gene. exp.) Desulfurobacterium thermolithotrophum DSM 11699 (bacteria) Tissue: / / Cell: / / Cell line: / / Gene: Dester_1504 / Organ: / / Details (production host): / / Cell (production host): / / Organ (production host): / / Production host: Escherichia coli BL21(DE3) (bacteria) / Tissue (production host): / / References: UniProt: F0S2B6

#1: Protein

Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

Mass: 40994.000 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: synthetic gene
Source: (gene. exp.)

Desulfurobacterium thermolithotrophum DSM 11699 (bacteria)
Tissue: / / Cell: / / Cell line: / / Gene: Dester_1504 / Organ: / / Details (production host): / / Cell (production host): / / Organ (production host): / / Production host:

Escherichia coli BL21(DE3) (bacteria) / Tissue (production host): /
References: UniProt: F0S2B6,

5,10-methenyltetrahydromethanopterin hydrogenase

#2: Protein

Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein

Mass: 41010.000 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: synthetic gene
Source: (gene. exp.)

Desulfurobacterium thermolithotrophum DSM 11699 (bacteria)
Tissue: / / Cell: / / Cell line: / / Gene: Dester_1504 / Organ: / / Details (production host): / / Cell (production host): / / Organ (production host): / / Production host:

Escherichia coli BL21(DE3) (bacteria) / Tissue (production host): / / References: UniProt: F0S2B6

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Non-polymers , 6 types, 627 molecules

#3: Chemical	ChemComp-FE9 / iron-guanylyl pyridinol cofactor Mass: 686.323 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂₁H₂₃FeN₆O₁₃PS
#4: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₃H₈O₃
#5: Chemical	ChemComp-GUE / 5,10-Methenyltetrahydrofolate / 5,10-Methenyltetrahydrofolate Mass: 456.432 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₂₀H₂₂N₇O₆
#6: Chemical	ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide Mass: 78.133 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C₂H₆OS / Comment: DMSO, precipitant*YM
#7: Chemical	ChemComp-PG4 / TETRAETHYLENE GLYCOL / Polyethylene glycol Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₈H₁₈O₅ / Comment: precipitant*YM
#8: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 609 / 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: 3.38 Å³/Da / Density % sol: 63.31 % / Description: plate shape
Crystal grow	Temperature: 281 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: dHmdII reconstituted with the Fe-guanylylpyridinol cofactor from Methanothermobacter marburgensis was cocrystallized with methenyl-tetrahydrofolate using the sitting drop vapor diffusion ...Details: dHmdII reconstituted with the Fe-guanylylpyridinol cofactor from Methanothermobacter marburgensis was cocrystallized with methenyl-tetrahydrofolate using the sitting drop vapor diffusion method at 281 K under N2/H2 (95%/5%) in red light condition. The reconstituted dHmdII holoenzyme was mixed with methenyl-tetrahydrofolate at the final concentrations of 1.6 mM. Methenyl-tetrahydrofolate was dissolved in 10% DMSO, and the final concentration of DMSO in the protein solution was 1.6%. 0.7 ul of dHmdII at 21 mg/ml (with Fe-guanylylpryridinol and methenyl-tetrahydrofolate) was spotted on a 96-well 2-drop MRC Crystallization Plates (Molecular Dimensions, Suffolk, UK) and 0.7 ul of reservoir solution was mixed. After 10 days, the crystals appeared in 20% PEG 3000 (w/v), 100 mM Tri-Sodium Citrate pH 5.5 (from the kit Wizard, Jean Bioscience). Crystals were cryoprotected by a soak of few seconds in 20% PEG 3000 (w/v), 100 mM Tri-Sodium Citrate pH 5.5 and 20% glycerol before a flash freeze in liquid nitrogen. Temp details: The temperature was fluctuating by +/- 1 degree

Crystal

Density Matthews: 3.38 Å³/Da / Density % sol: 63.31 % / Description: plate shape

Crystal grow

Temperature: 281 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: dHmdII reconstituted with the Fe-guanylylpyridinol cofactor from Methanothermobacter marburgensis was cocrystallized with methenyl-tetrahydrofolate using the sitting drop vapor diffusion ...
Temp details: The temperature was fluctuating by +/- 1 degree

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
Detector	Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 15, 2018
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1 Å / Relative weight: 1
Reflection	Resolution: 2.25→48.89 Å / Num. obs: 105630 / % possible obs: 99.9 % / Redundancy: 4.8 % / B_iso Wilson estimate: 42.3 Å² / CC_1/2: 0.998 / R_merge(I) obs: 0.096 / R_pim(I) all: 0.049 / R_rim(I) all: 0.108 / Net I/σ(I): 9.7
Reflection shell	Resolution: 2.25→2.37 Å / Redundancy: 4.9 % / R_merge(I) obs: 1.421 / Num. unique obs: 15270 / CC_1/2: 0.623 / R_pim(I) all: 0.714 / R_rim(I) all: 1.595 / % possible all: 100

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Processing

Software

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

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 4YT4

4yt4

Resolution: 2.25→24.983 Å / SU ML: 0.26 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 27.47
Details: For the last refinement cycle, the hydrogens have been generated in riding position. In the final deposited model, these hydrogens were omitted.

	R_factor	Num. reflection	% reflection
R_free	0.2122	5111	4.85 %
R_work	0.1869	-	-
obs	0.1881	105367	99.77 %

Solvent computation

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

Displacement parameters

B_iso mean: 55.2 Å²

Refinement step

Cycle: LAST / Resolution: 2.25→24.983 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	10949	0	270	609	11828

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	11439
X-RAY DIFFRACTION	f_angle_d	0.879	15526
X-RAY DIFFRACTION	f_dihedral_angle_d	17.128	6992
X-RAY DIFFRACTION	f_chiral_restr	0.046	1815
X-RAY DIFFRACTION	f_plane_restr	0.005	1958

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 (%)
2.25-2.2756	0.3144	152	0.3387	3316	X-RAY DIFFRACTION	100
2.2756-2.3023	0.3274	179	0.3234	3286	X-RAY DIFFRACTION	100
2.3023-2.3304	0.3122	150	0.3069	3348	X-RAY DIFFRACTION	100
2.3304-2.3598	0.3649	178	0.3105	3292	X-RAY DIFFRACTION	100
2.3598-2.3909	0.319	150	0.2857	3319	X-RAY DIFFRACTION	100
2.3909-2.4236	0.3155	163	0.2862	3292	X-RAY DIFFRACTION	100
2.4236-2.4582	0.3094	170	0.2783	3327	X-RAY DIFFRACTION	100
2.4582-2.4949	0.304	152	0.2594	3332	X-RAY DIFFRACTION	100
2.4949-2.5338	0.2755	184	0.2581	3273	X-RAY DIFFRACTION	100
2.5338-2.5753	0.3021	159	0.2568	3335	X-RAY DIFFRACTION	100
2.5753-2.6197	0.2938	194	0.2417	3295	X-RAY DIFFRACTION	100
2.6197-2.6672	0.2428	188	0.224	3282	X-RAY DIFFRACTION	100
2.6672-2.7185	0.2811	173	0.2199	3330	X-RAY DIFFRACTION	100
2.7185-2.7739	0.2402	163	0.2169	3351	X-RAY DIFFRACTION	100
2.7739-2.8341	0.2476	181	0.2144	3298	X-RAY DIFFRACTION	100
2.8341-2.9	0.2568	184	0.2115	3322	X-RAY DIFFRACTION	100
2.9-2.9724	0.2175	165	0.2084	3317	X-RAY DIFFRACTION	100
2.9724-3.0526	0.2632	153	0.2048	3365	X-RAY DIFFRACTION	100
3.0526-3.1423	0.2853	180	0.201	3334	X-RAY DIFFRACTION	100
3.1423-3.2435	0.2385	172	0.1968	3290	X-RAY DIFFRACTION	99
3.2435-3.3592	0.233	164	0.1965	3334	X-RAY DIFFRACTION	100
3.3592-3.4933	0.2161	169	0.1922	3342	X-RAY DIFFRACTION	100
3.4933-3.6518	0.2296	172	0.1649	3365	X-RAY DIFFRACTION	100
3.6518-3.8437	0.1832	151	0.1606	3390	X-RAY DIFFRACTION	100
3.8437-4.0836	0.1651	190	0.1497	3338	X-RAY DIFFRACTION	100
4.0836-4.3973	0.1617	178	0.1397	3362	X-RAY DIFFRACTION	100
4.3973-4.8369	0.1486	185	0.1325	3372	X-RAY DIFFRACTION	100
4.8369-5.5302	0.1651	178	0.1445	3419	X-RAY DIFFRACTION	100
5.5302-6.9426	0.1861	149	0.1679	3477	X-RAY DIFFRACTION	100
6.9426-24.9847	0.1723	185	0.17	3553	X-RAY DIFFRACTION	99

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	3.9704	-0.0452	-0.4131	4.4057	0.6548	3.0772	0.0895	0.0729	0.6556	0.4157	-0.1653	-0.9149	-0.5736	0.8041	0.0731	0.6461	-0.2088	-0.0294	0.6589	0.1734	0.9119	-91.466	-64.3319	59.5407
2	2.6934	-0.0205	-1.0632	3.5355	-0.3042	2.8466	0.0038	0.1434	0.8749	0.0689	-0.0339	-0.9901	-0.7548	0.5195	0.0839	0.675	-0.2003	0.0457	0.6478	0.2374	0.9326	-91.1665	-58.3326	55.2181
3	4.3819	0.0161	-1.5036	4.6806	0.6245	2.8916	0.2381	0.0855	0.9273	0.4685	-0.3366	-0.6414	-0.636	0.3626	-0.0873	0.5918	-0.137	0.0437	0.4156	0.0792	0.6603	-104.8629	-62.6388	63.5742
4	3.7026	-0.1504	-0.7113	3.4435	-0.3198	2.164	0.2443	0.3601	0.6098	0.087	-0.1334	-0.0931	-0.4092	0.0099	-0.0798	0.4521	-0.0663	0.0235	0.4097	0.1618	0.4383	-107.9387	-68.8713	59.1489
5	1.7707	-0.2782	-0.0841	3.0988	-0.4799	0.8281	0.057	0.4261	0.1247	-0.3168	-0.048	-0.1837	-0.0585	0.0161	-0.0134	0.3032	-0.0157	0.0163	0.509	0.0287	0.2792	-101.7995	-88.5004	54.7851
6	2.8602	0.5591	-0.3261	4.7129	-1.4766	2.5372	-0.1125	0.4804	-0.0208	-0.0703	-0.2028	-1.201	-0.0085	0.3367	0.1159	0.3325	0.0482	0.0368	0.6592	-0.0248	0.7952	-85.5757	-105.2874	57.8029
7	3.9442	0.6811	-0.5577	2.5383	-0.2488	1.332	0.0217	-0.2179	-0.3341	0.4692	-0.0195	-0.5418	-0.0635	0.3901	0.0295	0.4621	-0.0681	-0.099	0.4343	0.0222	0.3879	-100.038	-94.9794	72.0945
8	1.1989	1.4875	1.7273	1.8948	2.2946	2.8148	0.2146	-0.8692	0.6015	0.3229	-0.1089	-0.1907	-0.3971	0.1618	-0.0302	0.5496	-0.0808	-0.0212	0.5502	0.0168	0.5679	-107.6295	-80.2331	70.178
9	2.2396	-0.4372	0.0047	3.1184	-0.445	2.5963	0.1032	0.2699	-0.4106	-0.4483	-0.0175	-0.6065	0.3397	0.4594	-0.1149	0.5124	0.1291	-0.0209	0.5031	-0.2323	0.6	-95.1593	-125.5272	57.2302
10	2.9196	-0.0084	-0.7555	3.1731	0.3584	2.6856	0.0389	0.3174	-0.4895	-0.0291	-0.0174	-0.0628	0.3723	-0.0339	0.038	0.4147	0.0337	-0.1073	0.364	-0.0839	0.4501	-106.298	-124.2068	65.471
11	3.1182	0.2564	-0.2531	5.119	-0.6677	3.6923	0.1408	-0.1689	0.1704	0.5094	0.0472	-0.2803	0.1425	-0.0428	-0.3246	0.3791	0.049	-0.1317	0.385	0.0214	0.341	-102.0191	-110.5787	76.0454
12	1.4664	0.1139	0.0795	3.5423	-0.9482	1.295	0.0522	0.2005	0.0415	0.0341	-0.101	-0.7338	-0.0186	0.2813	0.0635	0.2725	0.0143	-0.0226	0.4751	-0.0253	0.4144	-93.7445	-96.0888	61.7077
13	3.3437	-0.9479	-1.5233	3.4675	-0.1856	4.3095	0.3077	0.3773	0.1703	-0.3191	0.0486	-0.0263	-0.3601	0.0787	-0.1313	0.3495	-0.0627	-0.056	0.424	-0.0346	0.3765	-108.4031	-92.541	55.7781
14	0.6279	-0.9108	-0.2968	3.3613	1.8856	1.3293	-0.3299	0.3953	-0.7813	-0.225	-0.1994	0.6969	0.3701	-0.4764	0.0883	0.4332	-0.0745	-0.0559	0.5761	-0.0272	0.6491	-115.7667	-104.1709	62.2448
15	2.7789	0.2105	-0.2474	3.1399	0.1388	2.0206	0.1795	-0.0777	0.6984	-0.0998	-0.0153	0.5433	-0.3082	-0.2103	0.0369	0.5982	0.1327	0.0625	0.4867	-0.1089	0.8652	-107.8958	-74.1117	108.4109
16	2.6248	-0.1428	-0.7581	2.3115	0.3448	2.2937	-0.0201	-0.0974	0.7575	-0.0914	0.0266	0.4878	-0.7217	-0.3689	-0.0546	0.6382	0.146	0.0591	0.4713	-0.1824	0.9197	-108.1927	-68.0558	112.7358
17	4.329	-0.0717	-1.366	3.8047	-0.6148	3.1658	0.0939	0.2214	0.9242	-0.2995	-0.0302	0.3899	-0.4635	-0.4474	-0.1792	0.5669	0.07	0.0506	0.3966	-0.0216	0.6256	-94.508	-72.4335	104.4386
18	1.6517	0.4326	-0.3112	2.395	0.0041	1.0908	0.1202	-0.3077	0.3584	0.2101	-0.0391	0.1138	-0.2203	0.0277	-0.0847	0.3349	0.0152	0.0097	0.3355	-0.0828	0.3112	-94.4779	-87.3734	114.1069
19	1.9981	-0.0243	-0.2564	1.9486	-0.1324	1.5055	0.093	-0.0026	-0.2801	-0.0361	-0.0284	0.3069	0.0153	-0.1912	-0.0533	0.337	0.0295	-0.0407	0.3585	0.0006	0.3995	-103.7196	-109.1304	102.3681
20	5.306	-2.2586	1.8165	1.0541	-0.7518	1.3392	0.1401	0.5188	0.345	-0.2283	0.0861	0.1333	-0.0049	0.0804	-0.1142	0.4588	0.0007	-0.0511	0.4643	0.0111	0.4615	-92.3853	-90.0235	97.5288
21	2.5096	0.1346	-0.251	3.185	-0.2386	2.8144	-0.0424	-0.2321	-0.7144	0.166	-0.009	0.6812	0.2744	-0.1322	0.0114	0.5561	-0.0155	-0.0298	0.405	0.1937	0.7799	-104.337	-135.2467	111.2613
22	2.5918	0.0405	-0.763	2.0827	0.1429	2.6759	-0.195	-0.2111	-0.9186	0.0773	-0.0794	0.2076	0.8279	0.1808	0.1977	0.6652	0.0547	-0.0706	0.4085	0.1125	0.7458	-94.1439	-139.4877	106.8096
23	3.2499	-1.2798	-0.7301	2.9833	-0.1671	2.3185	0.1487	0.213	-0.3139	-0.292	-0.1919	0.1929	0.1767	-0.0285	0.0587	0.4033	0.0284	-0.1148	0.3321	-0.0083	0.391	-96.3498	-126.121	96.5307
24	1.5422	0.2013	-0.2627	2.8739	0.0552	1.7835	0.0491	-0.148	0.0955	0.1358	-0.0107	0.4886	-0.1261	-0.2612	-0.0368	0.2849	0.0093	0.0155	0.3844	-0.0207	0.3716	-106.3811	-98.7815	110.5914
25	3.8704	1.0183	-0.8958	2.5445	-0.6392	4.2295	0.2033	-0.3661	0.0012	0.2571	0.014	-0.0693	0.0903	0.4698	-0.2667	0.3813	0.0909	-0.0716	0.2974	-0.024	0.3441	-91.0152	-102.2799	112.452
26	5.2096	0.9452	-2.3797	5.4898	-0.9112	3.7259	-0.4357	-0.165	-1.3118	-0.0933	-0.2419	-0.3806	0.6223	0.7133	0.6088	0.4186	0.1042	-0.084	0.4992	0.0428	0.7043	-83.3863	-113.7196	104.2247

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 1 through 19 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 20 through 74 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 75 through 104 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 105 through 157 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 158 through 262 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 263 through 292 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 293 through 332 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 333 through 350 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 1 through 41 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 42 through 157 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 158 through 173 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 174 through 292 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 293 through 332 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 333 through 357 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 1 through 19 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 20 through 74 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 75 through 104 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 105 through 231 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 232 through 332 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 333 through 351 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 1 through 41 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 42 through 103 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 104 through 204 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 205 through 292 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 293 through 332 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 333 through 355 )

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