PDB-3mle: Crystal structure of dethiobiotin synthetase (BioD) from Helicoba...

ID or keywords:

Entry

Database: PDB / ID: 3mle

Title

Crystal structure of dethiobiotin synthetase (BioD) from Helicobacter pylori cocrystallized with ATP

Components

Dethiobiotin synthetase

Keywords

LIGASE / DTBS / dethiobiotin synthetase /

Structural Genomics / PSI-2 /

Protein Structure Initiative / Midwest Center for Structural Genomics / MCSG

Function / homology

Function and homology information

dethiobiotin synthase /

dethiobiotin synthase activity / biotin biosynthetic process / magnesium ion binding /

ATP binding /

cytosol
Similarity search - Function

Biological species

Helicobacter pylori (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.8 Å

Authors

Nicholls, R. / Porebski, P.J. / Klimecka, M.M. / Chruszcz, M. / Murzyn, K. / Joachimiak, A. / Murshudov, G. / Minor, W. / Midwest Center for Structural Genomics (MCSG)

Citation

Journal: Febs J. / Year: 2012
Title: Structural characterization of Helicobacter pylori dethiobiotin synthetase reveals differences between family members.
Authors: Porebski, P.J. / Klimecka, M. / Chruszcz, M. / Nicholls, R.A. / Murzyn, K. / Cuff, M.E. / Xu, X. / Cymborowski, M. / Murshudov, G.N. / Savchenko, A. / Edwards, A. / Minor, W.

History

Deposition	Apr 16, 2010	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	May 19, 2010	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Version format compliance
Revision 1.2	Mar 28, 2012	Group: Database references
Revision 1.3	Mar 27, 2013	Group: Database references
Revision 1.4	Apr 13, 2022	Group: Database references / Derived calculations / Structure summary Category: audit_author / citation_author ...audit_author / citation_author / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site Item: _audit_author.identifier_ORCID / _citation_author.identifier_ORCID ..._audit_author.identifier_ORCID / _citation_author.identifier_ORCID / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr2_label_alt_id / _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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5	Sep 6, 2023	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	3mle.cif.gz	282.3 KB	Display	PDBx/mmCIF format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ml/3mle ftp://data.pdbj.org/pub/pdb/validation_reports/ml/3mle	HTTPS FTP

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Related structure data

Related structure data	2qmoSC 3qxcC 3qxhC 3qxjC 3qxsC 3qxxC 3qy0C S: Starting model for refinement C: citing same article (ref.)
Similar structure data	3qy0-1 3qxx-1 3qxj-1 2qmo-1 3qxc-1 3qxs-1 1zkp-1 1xv2-1 3aqa-d 1dts-1 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	TargetDB: APC5858

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Dethiobiotin synthetase

B: Dethiobiotin synthetase

C: Dethiobiotin synthetase

D: Dethiobiotin synthetase

E: Dethiobiotin synthetase

F: Dethiobiotin synthetase

hetero molecules

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

1

A: Dethiobiotin synthetase

C: Dethiobiotin synthetase

hetero molecules

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

2

B: Dethiobiotin synthetase

D: Dethiobiotin synthetase

hetero molecules

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

3

E: Dethiobiotin synthetase

F: Dethiobiotin synthetase

hetero molecules

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

Unit cell

Length a, b, c (Å)	79.773, 131.905, 133.099
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	ILE	ILE	GLU	GLU	2	A	A	4 - 38	26 - 60
2	1	1	ILE	ILE	GLU	GLU	2	B	B	4 - 38	26 - 60
3	1	1	ILE	ILE	GLU	GLU	2	C	C	4 - 38	26 - 60
4	1	1	ILE	ILE	GLU	GLU	2	D	D	4 - 38	26 - 60
5	1	1	ILE	ILE	GLU	GLU	2	E	E	4 - 38	26 - 60
6	1	1	ILE	ILE	GLU	GLU	2	F	F	4 - 38	26 - 60
1	1	2	ARG	ARG	ASP	ASP	2	A	A	59 - 97	81 - 119
2	1	2	ARG	ARG	ASP	ASP	2	B	B	59 - 97	81 - 119
3	1	2	ARG	ARG	ASP	ASP	2	C	C	59 - 97	81 - 119
4	1	2	ARG	ARG	ASP	ASP	2	D	D	59 - 97	81 - 119
5	1	2	ARG	ARG	ASP	ASP	2	E	E	59 - 97	81 - 119
6	1	2	ARG	ARG	ASP	ASP	2	F	F	59 - 97	81 - 119
1	2	2	LEU	LEU	GLN	GLN	2	A	A	99 - 101	121 - 123
2	2	2	LEU	LEU	GLN	GLN	2	B	B	99 - 101	121 - 123
3	2	2	LEU	LEU	GLN	GLN	2	C	C	99 - 101	121 - 123
4	2	2	LEU	LEU	GLN	GLN	2	D	D	99 - 101	121 - 123
5	2	2	LEU	LEU	GLN	GLN	2	E	E	99 - 101	121 - 123
6	2	2	LEU	LEU	GLN	GLN	2	F	F	99 - 101	121 - 123
1	3	2	LEU	LEU	SER	SER	2	A	A	103 - 165	125 - 187
2	3	2	LEU	LEU	SER	SER	2	B	B	103 - 165	125 - 187
3	3	2	LEU	LEU	SER	SER	2	C	C	103 - 165	125 - 187
4	3	2	LEU	LEU	SER	SER	2	D	D	103 - 165	125 - 187
5	3	2	LEU	LEU	SER	SER	2	E	E	103 - 165	125 - 187
6	3	2	LEU	LEU	SER	SER	2	F	F	103 - 165	125 - 187
1	1	3	SER	SER	GLN	GLN	5	A	A	165 - 207	187 - 229
2	1	3	SER	SER	GLN	GLN	5	B	B	165 - 207	187 - 229
3	1	3	SER	SER	GLN	GLN	5	C	C	165 - 207	187 - 229
4	1	3	SER	SER	GLN	GLN	5	D	D	165 - 207	187 - 229
5	1	3	SER	SER	GLN	GLN	5	E	E	165 - 207	187 - 229
6	1	3	SER	SER	GLN	GLN	5	F	F	165 - 207	187 - 229

NCS ensembles :

ID
1
2
3

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Protein , 1 types, 6 molecules ABCDEF

#1: Protein	Dethiobiotin synthetase / Dethiobiotin synthase / DTB synthetase / DTBS Mass: 27148.088 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Helicobacter pylori (bacteria) / Strain: 26695 / Gene: bioD, HP0029, HP_0029 / Plasmid: p11 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-Gold(DE3) Magic / References: UniProt: O24872, dethiobiotin synthase

#1: Protein

Dethiobiotin synthetase / Dethiobiotin synthase / DTB synthetase / DTBS

Mass: 27148.088 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Helicobacter pylori (bacteria) / Strain: 26695 / Gene: bioD, HP0029, HP_0029 / Plasmid: p11 / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21-Gold(DE3) Magic / References: UniProt: O24872,

dethiobiotin synthase

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Non-polymers , 7 types, 128 molecules

#2: Chemical	ChemComp-PO4 / PHOSPHATE ION / Phosphate Mass: 94.971 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: PO₄
#3: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#4: Chemical	ChemComp-NO3 / NITRATE ION / Nitrate Mass: 62.005 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: NO₃
#5: Chemical	ChemComp-CL / CHLORIDE ION / Chloride Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#6: Chemical	ChemComp-8AC / 8-aminooctanoic acid / 8-aminocaprylic acid Mass: 159.226 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₈H₁₇NO₂
#7: Chemical	ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₁₀H₁₅N₅O₁₀P₂ / Comment: ADP, energy-carrying molecule*YM
#8: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 96 / 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: 2.15 Å³/Da / Density % sol: 42.78 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 20% PEG3350; 100 MM NH4NO3; 100 MM, BIS-TRIS; 10 MM ATP; 10 MM MGCL2; 10 MM 8-AMINOOCTANOIC ACID; IN SITU PROTEOLYSIS - CHYMOTRYPSIN, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.9793 / Wavelength: 0.9793 Å
Detector	Detector: CCD / Date: Jul 9, 2008 / Details: MIRROR
Radiation	Monochromator: SI-111 CHANNEL / Protocol: MOLECULAR REPLACEMENT / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9793 Å / Relative weight: 1
Reflection	Resolution: 2.8→50 Å / Num. all: 35576 / Num. obs: 35576 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 7.7 % / B_iso Wilson estimate: 81.3 Å² / R_merge(I) obs: 0.099 / R_sym value: 0.099 / Net I/σ(I): 21.615
Reflection shell	Resolution: 2.8→2.85 Å / Redundancy: 7.9 % / R_merge(I) obs: 0.846 / Mean I/σ(I) obs: 2 / Num. unique all: 1765 / R_sym value: 0.846 / % possible all: 100

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Processing

Software

Name	Version	Classification
HKL-3000		data collection
MOLREP		phasing
REFMAC	5.5.0109	refinement
Coot		model building
HKL-3000		phasing
HKL-2000		data reduction
HKL-2000		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2QMO

2qmo

Resolution: 2.8→50 Å / Cor.coef. F_o:F_c: 0.949 / Cor.coef. F_o:F_c free: 0.917 / SU B: 30.546 / SU ML: 0.309 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R Free: 0.399 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.246	1765	5 %	RANDOM
R_work	0.201	-	-	-
all	0.204	35281	-	-
obs	0.204	35281	99.92 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 59.69 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-1.37 Å²	0 Å²	0 Å²
2-	-	2.76 Å²	0 Å²
3-	-	-	-1.39 Å²

Refinement step

Cycle: LAST / Resolution: 2.8→50 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	10345	0	289	96	10730

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.014	0.022	10919
X-RAY DIFFRACTION	r_bond_other_d	0.006	0.02	6996
X-RAY DIFFRACTION	r_angle_refined_deg	1.356	1.99	14822
X-RAY DIFFRACTION	r_angle_other_deg	1.149	3.001	17143
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.231	5	1351
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	34.917	25.399	476
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.069	15	1828
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	22.741	15	35
X-RAY DIFFRACTION	r_chiral_restr	0.063	0.2	1753
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.02	11922
X-RAY DIFFRACTION	r_gen_planes_other	0.002	0.02	2035
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	1.368	1.5	6699
X-RAY DIFFRACTION	r_mcbond_other	0.27	1.5	2695
X-RAY DIFFRACTION	r_mcangle_it	2.107	2	10806
X-RAY DIFFRACTION	r_scbond_it	2.714	3	4220
X-RAY DIFFRACTION	r_scangle_it	3.98	4.5	4007
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	207	tight positional	0.03	0.05
1	1	B	207	tight positional	0.03	0.05
1	1	C	207	tight positional	0.03	0.05
1	1	D	207	tight positional	0.03	0.05
1	1	E	207	tight positional	0.03	0.05
1	1	F	207	tight positional	0.03	0.05
2	2	A	614	tight positional	0.03	0.05
2	2	B	614	tight positional	0.03	0.05
2	2	C	614	tight positional	0.03	0.05
2	2	D	614	tight positional	0.03	0.05
2	2	E	614	tight positional	0.03	0.05
2	2	F	614	tight positional	0.03	0.05
1	1	A	203	medium positional	0.04	0.5
1	1	B	203	medium positional	0.03	0.5
1	1	C	203	medium positional	0.03	0.5
1	1	D	203	medium positional	0.05	0.5
1	1	E	203	medium positional	0.04	0.5
1	1	F	203	medium positional	0.03	0.5
2	2	A	700	medium positional	0.04	0.5
2	2	B	700	medium positional	0.05	0.5
2	2	C	700	medium positional	0.03	0.5
2	2	D	700	medium positional	0.04	0.5
2	2	E	700	medium positional	0.04	0.5
2	2	F	700	medium positional	0.03	0.5
3	3	A	243	medium positional	0.09	0.5
3	3	B	243	medium positional	0.14	0.5
3	3	C	243	medium positional	0.08	0.5
3	3	D	243	medium positional	0.09	0.5
3	3	E	243	medium positional	0.17	0.5
3	3	F	243	medium positional	0.08	0.5
3	3	A	267	loose positional	0.26	5
3	3	B	267	loose positional	0.38	5
3	3	C	267	loose positional	0.34	5
3	3	D	267	loose positional	0.25	5
3	3	E	267	loose positional	0.37	5
3	3	F	267	loose positional	0.36	5
1	1	A	207	tight thermal	0.77	0.5
1	1	B	207	tight thermal	0.66	0.5
1	1	C	207	tight thermal	0.34	0.5
1	1	D	207	tight thermal	0.23	0.5
1	1	E	207	tight thermal	0.71	0.5
1	1	F	207	tight thermal	0.76	0.5
2	2	A	614	tight thermal	0.63	0.5
2	2	B	614	tight thermal	0.73	0.5
2	2	C	614	tight thermal	0.49	0.5
2	2	D	614	tight thermal	0.42	0.5
2	2	E	614	tight thermal	0.77	0.5
2	2	F	614	tight thermal	0.76	0.5
1	1	A	203	medium thermal	0.87	2
1	1	B	203	medium thermal	0.8	2
1	1	C	203	medium thermal	0.42	2
1	1	D	203	medium thermal	0.34	2
1	1	E	203	medium thermal	0.72	2
1	1	F	203	medium thermal	0.93	2
2	2	A	700	medium thermal	0.84	2
2	2	B	700	medium thermal	0.89	2
2	2	C	700	medium thermal	0.64	2
2	2	D	700	medium thermal	0.7	2
2	2	E	700	medium thermal	0.96	2
2	2	F	700	medium thermal	1.05	2
3	3	A	243	medium thermal	2.21	2
3	3	B	243	medium thermal	4.22	2
3	3	C	243	medium thermal	2.08	2
3	3	D	243	medium thermal	1.31	2
3	3	E	243	medium thermal	1.21	2
3	3	F	243	medium thermal	3.05	2
3	3	A	267	loose thermal	1.64	10
3	3	B	267	loose thermal	2.79	10
3	3	C	267	loose thermal	2.18	10
3	3	D	267	loose thermal	1.05	10
3	3	E	267	loose thermal	1.27	10
3	3	F	267	loose thermal	3.18	10

LS refinement shell

Resolution: 2.8→2.87 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.434	112	-
R_work	0.371	2467	-
obs	-	-	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	1.0412	-0.087	0.6755	1.6477	-0.0639	1.1239	-0.0894	-0.0476	0.0746	0.0242	0.1443	-0.0118	-0.0599	0.0055	-0.0549	0.4449	0.0358	0.0291	0.0739	-0.0525	0.6002	-16.061	27.758	-38.05
2	1.32	-0.5887	-0.2877	1.8367	-0.4131	0.457	-0.1686	-0.2861	0.0771	0.449	0.2096	0.0718	0.007	0.0108	-0.041	0.5355	0.0618	0.0026	0.0846	-0.0677	0.5125	-13.14	20.495	-27.156
3	4.5696	-3.554	-0.6613	4.1464	-0.1269	0.4766	0.1107	0.0915	-0.4062	-0.1572	0.0077	0.655	0.1867	-0.104	-0.1185	0.5115	-0.0507	-0.008	0.0725	-0.0442	0.7109	-21.918	5.702	-38.011
4	1.5412	-0.4042	-0.4555	1.6792	-0.9621	1.8147	0.1527	0.0369	-0.1178	-0.1745	-0.2036	-0.0756	0.1021	0.1232	0.0509	0.4545	0.1018	0.0678	0.1527	-0.0161	0.5325	-21.342	31.3	-57.446
5	1.454	-0.9404	0.0416	1.893	0.5056	0.7601	0.2837	0.293	-0.0992	-0.3657	-0.2337	0.0182	-0.0543	-0.0784	-0.05	0.5151	0.1386	0.0161	0.2076	-0.0222	0.484	-29.187	37.609	-66.517
6	1.4795	-0.9408	-0.7894	3.7735	0.2965	1.1065	0.0372	0.0425	-0.3854	0.2135	-0.1356	0.3578	-0.1586	-0.2879	0.0985	0.4095	0.0589	-0.0187	0.2018	-0.0824	0.582	-43.548	37.302	-52.621
7	2.8165	-0.4016	-0.4258	1.4897	0.7919	0.4947	-0.3307	-0.144	-0.0775	-0.0469	0.1271	-0.0045	0.0821	0.1002	0.2035	0.5976	0.1119	0.0538	0.0427	0.0991	0.5975	9.037	-10.248	-37.205
8	1.979	-1.3762	-0.5023	1.8881	-0.1224	0.6886	-0.4088	-0.4813	-0.1807	0.1541	0.2106	0.1902	0.1527	0.0862	0.1982	0.5578	0.1385	0.0384	0.1784	0.0547	0.487	-0.686	-6.511	-29.122
9	7.0089	-5.2826	1.3547	10.4016	-2.3181	0.5656	-0.9405	-1.079	1.8019	0.8625	0.6067	-1.6506	-0.1174	-0.0904	0.3338	0.4684	0.3115	-0.3417	0.3079	-0.4146	0.7116	10.285	9.942	-25.388
10	1.077	0.8158	0.3184	3.4879	-0.6456	0.534	0.0191	-0.13	0.0301	-0.1617	-0.125	0.5052	-0.0607	0.0037	0.1058	0.5652	0.2111	0.0075	0.228	-0.0021	0.5523	-43.514	72.027	-57.342
11	0.1397	-0.47	-0.2525	4.0742	0.037	0.9474	0.0235	0.0389	-0.1537	-0.6395	-0.1002	0.6442	-0.0875	-0.1741	0.0767	0.5445	0.2074	-0.0963	0.2015	0.0066	0.5055	-45.911	60.787	-64.004
12	1.3505	-1.7628	-0.6254	5.6483	0.2126	0.4095	0.11	0.0566	-0.0589	-1.0225	-0.3256	-0.6064	0.0691	0.0071	0.2156	0.7798	0.1883	0.1978	0.097	0.0439	0.5359	-27.405	62.707	-71.724
13	3.7814	-1.8945	-2.5606	1.0272	1.2042	3.5252	0.5098	0.3231	0.5335	-0.0696	-0.0128	-0.2053	-0.1091	-0.3604	-0.497	0.5003	0.1995	0.0201	0.182	0.2565	0.7064	25.866	-6.358	-48.689
14	1.8632	-1.0188	-0.4073	2.3212	0.9621	1.2632	0.1892	0.2174	0.5421	-0.0611	0.1215	-0.5079	-0.1308	0.2402	-0.3107	0.4384	0.0509	0.0007	0.1412	0.1477	0.7504	38.628	-8.781	-51.924
15	2.9695	-3.5428	-0.6569	4.2924	1.1193	2.2883	-0.3808	-0.458	0.4786	0.5357	0.5661	-0.5649	0.183	0.21	-0.1853	0.4953	0.1082	-0.1896	0.0839	-0.114	0.749	40.677	-15.989	-33.453
16	0.1987	0.1074	0.7369	2.0645	0.4705	2.8562	0.017	-0.0032	0.0524	-0.1084	-0.046	-0.1842	0.3356	0.1078	0.029	0.5684	0.2946	-0.042	0.2033	0.0054	0.488	49.107	-45.81	-49.245
17	1.4006	-1.2098	-0.3033	2.4397	-0.3386	1.3918	-0.2162	-0.1148	0.404	0.0357	0.0091	-0.5054	0.0392	0.3983	0.2072	0.43	0.1652	-0.1091	0.2305	0.011	0.5907	53.43	-33.267	-47.887
18	2.7949	-2.8746	-1.2765	3.1127	1.1233	2.3677	0.3553	0.282	0.2538	-0.6888	-0.3488	-0.2851	-0.0805	-0.2271	-0.0065	0.716	0.1611	0.0489	0.1074	0.1264	0.4674	44.678	-29.765	-66.001

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	-1 - 80
2	X-RAY DIFFRACTION	2	A	81 - 168
3	X-RAY DIFFRACTION	3	A	169 - 219
4	X-RAY DIFFRACTION	4	B	-3 - 79
5	X-RAY DIFFRACTION	5	B	80 - 176
6	X-RAY DIFFRACTION	6	B	177 - 220
7	X-RAY DIFFRACTION	7	C	-3 - 79
8	X-RAY DIFFRACTION	8	C	80 - 176
9	X-RAY DIFFRACTION	9	C	177 - 219
10	X-RAY DIFFRACTION	10	D	-3 - 79
11	X-RAY DIFFRACTION	11	D	80 - 176
12	X-RAY DIFFRACTION	12	D	177 - 219
13	X-RAY DIFFRACTION	13	E	-1 - 79
14	X-RAY DIFFRACTION	14	E	80 - 176
15	X-RAY DIFFRACTION	15	E	177 - 219
16	X-RAY DIFFRACTION	16	F	-3 - 79
17	X-RAY DIFFRACTION	17	F	80 - 175
18	X-RAY DIFFRACTION	18	F	176 - 219

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