PDB-6hk6: Human RIOK2 bound to inhibitor

ID or keywords:

Entry

Database: PDB / ID: 6hk6

Title

Human RIOK2 bound to inhibitor

Components

Serine/threonine-protein kinase RIO2

Keywords

TRANSFERASE / Kinase / Structural Genomics Consortium / SGC

Function / homology

Function and homology information

positive regulation of ribosomal small subunit export from nucleus / positive regulation of rRNA processing / regulation of mitotic metaphase/anaphase transition / preribosome, small subunit precursor / Major pathway of rRNA processing in the nucleolus and cytosol / maturation of SSU-rRNA / protein autophosphorylation / ribosomal small subunit biogenesis / non-specific serine/threonine protein kinase / protein kinase activity ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.35 Å

Authors

Wang, J. / Krojer, T. / Bountra, C. / Edwards, A.M. / Arrowsmith, C. / Knapp, S. / Elkins, J.M.

Citation

Journal: Open Biology / Year: 2019
Title: Crystal structure of human RIOK2 bound to a specific inhibitor.
Authors: Wang, J. / Varin, T. / Vieth, M. / Elkins, J.M.

History

Deposition	Sep 5, 2018	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Oct 24, 2018	Provider: repository / Type: Initial release
Revision 1.1	Apr 3, 2019	Group: Data collection / Source and taxonomy / Category: entity_src_gen Item: _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name
Revision 1.2	Apr 24, 2019	Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc Item: _citation.country / _citation.journal_abbrev ..._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
Revision 1.3	Oct 2, 2019	Group: Data collection / Derived calculations Category: pdbx_struct_assembly / pdbx_struct_assembly_gen ...pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list
Revision 1.4	Jan 17, 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 / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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	6hk6.cif.gz	1.1 MB	Display	PDBx/mmCIF format
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Validation report

Summary document	6hk6_validation.pdf.gz	559.9 KB	Display	wwPDB validaton report
Full document	6hk6_full_validation.pdf.gz	598 KB	Display
Data in XML	6hk6_validation.xml.gz	100 KB	Display
Data in CIF	6hk6_validation.cif.gz	134.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/hk/6hk6 ftp://data.pdbj.org/pub/pdb/validation_reports/hk/6hk6	HTTPS FTP

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Related structure data

Related structure data	4gyiS S: Starting model for refinement
Similar structure data	3luy-1 6bkg-d 2nuf-d 5e7p-2 6fdm-2 3wgi-1 3tbc-d 4naj-1 6p0c-d 6fdo-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) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

Related structure data

4gyiS

S: Starting model for refinement

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#60 - Dec 2004 Ubiquitin similarity (1) #260 - Aug 2021 Ribonuclease P similarity (1) #234 - Jun 2019 MDM2 and Cancer similarity (1) #86 - Feb 2007 Exosomes similarity (1)

Deposited unit

A: Serine/threonine-protein kinase RIO2

B: Serine/threonine-protein kinase RIO2

C: Serine/threonine-protein kinase RIO2

D: Serine/threonine-protein kinase RIO2

E: Serine/threonine-protein kinase RIO2

F: Serine/threonine-protein kinase RIO2

G: Serine/threonine-protein kinase RIO2

H: Serine/threonine-protein kinase RIO2

I: Serine/threonine-protein kinase RIO2

J: Serine/threonine-protein kinase RIO2

hetero molecules

387 kDa, 10 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Serine/threonine-protein kinase RIO2

B: Serine/threonine-protein kinase RIO2

hetero molecules

defined by software
Evidence: gel filtration
77.7 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Serine/threonine-protein kinase RIO2

F: Serine/threonine-protein kinase RIO2

hetero molecules

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

3

D: Serine/threonine-protein kinase RIO2

E: Serine/threonine-protein kinase RIO2

hetero molecules

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

4

G: Serine/threonine-protein kinase RIO2

J: Serine/threonine-protein kinase RIO2

hetero molecules

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

5

H: Serine/threonine-protein kinase RIO2

hetero molecules

I: Serine/threonine-protein kinase RIO2

hetero molecules

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

Unit cell

Length a, b, c (Å)	92.010, 92.860, 237.650
Angle α, β, γ (deg.)	90.00, 99.10, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: _ / Refine code: _

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	GLY	GLY	SER	SER	A	A	2 - 301	3 - 302
2	1	GLY	GLY	SER	SER	B	B	2 - 301	3 - 302
1	2	GLY	GLY	SER	SER	A	A	2 - 301	3 - 302
2	2	GLY	GLY	SER	SER	C	C	2 - 301	3 - 302
1	3	GLY	GLY	SER	SER	A	A	2 - 301	3 - 302
2	3	GLY	GLY	SER	SER	D	D	2 - 301	3 - 302
1	4	GLY	GLY	SER	SER	A	A	2 - 301	3 - 302
2	4	GLY	GLY	SER	SER	E	E	2 - 301	3 - 302
1	5	GLY	GLY	SER	SER	A	A	2 - 301	3 - 302
2	5	GLY	GLY	SER	SER	F	F	2 - 301	3 - 302
1	6	VAL	VAL	SER	SER	A	A	6 - 301	7 - 302
2	6	VAL	VAL	SER	SER	G	G	6 - 301	7 - 302
1	7	LYS	LYS	SER	SER	A	A	3 - 301	4 - 302
2	7	LYS	LYS	SER	SER	H	H	3 - 301	4 - 302
1	8	GLY	GLY	VAL	VAL	A	A	2 - 298	3 - 299
2	8	GLY	GLY	VAL	VAL	I	I	2 - 298	3 - 299
1	9	GLY	GLY	SER	SER	A	A	2 - 301	3 - 302
2	9	GLY	GLY	SER	SER	J	J	2 - 301	3 - 302
1	10	GLY	GLY	SER	SER	B	B	2 - 301	3 - 302
2	10	GLY	GLY	SER	SER	C	C	2 - 301	3 - 302
1	11	GLY	GLY	SER	SER	B	B	2 - 301	3 - 302
2	11	GLY	GLY	SER	SER	D	D	2 - 301	3 - 302
1	12	GLY	GLY	SER	SER	B	B	2 - 301	3 - 302
2	12	GLY	GLY	SER	SER	E	E	2 - 301	3 - 302
1	13	GLY	GLY	SER	SER	B	B	2 - 301	3 - 302
2	13	GLY	GLY	SER	SER	F	F	2 - 301	3 - 302
1	14	VAL	VAL	SER	SER	B	B	6 - 301	7 - 302
2	14	VAL	VAL	SER	SER	G	G	6 - 301	7 - 302
1	15	LYS	LYS	SER	SER	B	B	3 - 301	4 - 302
2	15	LYS	LYS	SER	SER	H	H	3 - 301	4 - 302
1	16	GLY	GLY	VAL	VAL	B	B	2 - 298	3 - 299
2	16	GLY	GLY	VAL	VAL	I	I	2 - 298	3 - 299
1	17	GLY	GLY	SER	SER	B	B	2 - 301	3 - 302
2	17	GLY	GLY	SER	SER	J	J	2 - 301	3 - 302
1	18	GLY	GLY	SER	SER	C	C	2 - 301	3 - 302
2	18	GLY	GLY	SER	SER	D	D	2 - 301	3 - 302
1	19	GLY	GLY	SER	SER	C	C	2 - 301	3 - 302
2	19	GLY	GLY	SER	SER	E	E	2 - 301	3 - 302
1	20	GLY	GLY	SER	SER	C	C	2 - 301	3 - 302
2	20	GLY	GLY	SER	SER	F	F	2 - 301	3 - 302
1	21	VAL	VAL	SER	SER	C	C	6 - 301	7 - 302
2	21	VAL	VAL	SER	SER	G	G	6 - 301	7 - 302
1	22	LYS	LYS	SER	SER	C	C	3 - 301	4 - 302
2	22	LYS	LYS	SER	SER	H	H	3 - 301	4 - 302
1	23	GLY	GLY	VAL	VAL	C	C	2 - 298	3 - 299
2	23	GLY	GLY	VAL	VAL	I	I	2 - 298	3 - 299
1	24	GLY	GLY	SER	SER	C	C	2 - 301	3 - 302
2	24	GLY	GLY	SER	SER	J	J	2 - 301	3 - 302
1	25	GLY	GLY	SER	SER	D	D	2 - 301	3 - 302
2	25	GLY	GLY	SER	SER	E	E	2 - 301	3 - 302
1	26	GLY	GLY	SER	SER	D	D	2 - 301	3 - 302
2	26	GLY	GLY	SER	SER	F	F	2 - 301	3 - 302
1	27	VAL	VAL	SER	SER	D	D	6 - 301	7 - 302
2	27	VAL	VAL	SER	SER	G	G	6 - 301	7 - 302
1	28	LYS	LYS	SER	SER	D	D	3 - 301	4 - 302
2	28	LYS	LYS	SER	SER	H	H	3 - 301	4 - 302
1	29	GLY	GLY	VAL	VAL	D	D	2 - 298	3 - 299
2	29	GLY	GLY	VAL	VAL	I	I	2 - 298	3 - 299
1	30	GLY	GLY	SER	SER	D	D	2 - 301	3 - 302
2	30	GLY	GLY	SER	SER	J	J	2 - 301	3 - 302
1	31	GLY	GLY	SER	SER	E	E	2 - 301	3 - 302
2	31	GLY	GLY	SER	SER	F	F	2 - 301	3 - 302
1	32	VAL	VAL	SER	SER	E	E	6 - 301	7 - 302
2	32	VAL	VAL	SER	SER	G	G	6 - 301	7 - 302
1	33	LYS	LYS	SER	SER	E	E	3 - 301	4 - 302
2	33	LYS	LYS	SER	SER	H	H	3 - 301	4 - 302
1	34	GLY	GLY	VAL	VAL	E	E	2 - 298	3 - 299
2	34	GLY	GLY	VAL	VAL	I	I	2 - 298	3 - 299
1	35	GLY	GLY	SER	SER	E	E	2 - 301	3 - 302
2	35	GLY	GLY	SER	SER	J	J	2 - 301	3 - 302
1	36	VAL	VAL	SER	SER	F	F	6 - 301	7 - 302
2	36	VAL	VAL	SER	SER	G	G	6 - 301	7 - 302
1	37	LYS	LYS	SER	SER	F	F	3 - 301	4 - 302
2	37	LYS	LYS	SER	SER	H	H	3 - 301	4 - 302
1	38	GLY	GLY	VAL	VAL	F	F	2 - 298	3 - 299
2	38	GLY	GLY	VAL	VAL	I	I	2 - 298	3 - 299
1	39	GLY	GLY	SER	SER	F	F	2 - 301	3 - 302
2	39	GLY	GLY	SER	SER	J	J	2 - 301	3 - 302
1	40	VAL	VAL	SER	SER	G	G	6 - 301	7 - 302
2	40	VAL	VAL	SER	SER	H	H	6 - 301	7 - 302
1	41	VAL	VAL	GLU	GLU	G	G	6 - 299	7 - 300
2	41	VAL	VAL	GLU	GLU	I	I	6 - 299	7 - 300
1	42	VAL	VAL	SER	SER	G	G	6 - 301	7 - 302
2	42	VAL	VAL	SER	SER	J	J	6 - 301	7 - 302
1	43	LYS	LYS	GLU	GLU	H	H	3 - 299	4 - 300
2	43	LYS	LYS	GLU	GLU	I	I	3 - 299	4 - 300
1	44	LYS	LYS	SER	SER	H	H	3 - 301	4 - 302
2	44	LYS	LYS	SER	SER	J	J	3 - 301	4 - 302
1	45	GLY	GLY	VAL	VAL	I	I	2 - 298	3 - 299
2	45	GLY	GLY	VAL	VAL	J	J	2 - 298	3 - 299

NCS ensembles :

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Protein , 1 types, 10 molecules ABCDEFGHIJ

#1: Protein	Serine/threonine-protein kinase RIO2 / RIO kinase 2 Mass: 38264.785 Da / Num. of mol.: 10 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RIOK2, RIO2 / Details (production host): pNIC-Zb / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: Q9BVS4, non-specific serine/threonine protein kinase

#1: Protein

Serine/threonine-protein kinase RIO2 / RIO kinase 2

Mass: 38264.785 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Homo sapiens (human) / Gene: RIOK2, RIO2 / Details (production host): pNIC-Zb / Production host:

Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q9BVS4, non-specific serine/threonine protein kinase

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Non-polymers , 5 types, 401 molecules

#2: Chemical	ChemComp-G8H / 2-naphthalen-2-yl-~{N}-pyridin-2-yl-ethanamide Mass: 262.306 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C₁₇H₁₄N₂O
#3: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#4: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C₂H₆O₂
#5: Chemical	ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES Mass: 238.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₈H₁₈N₂O₄S / Comment: pH buffer*YM
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 376 / 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: 2.62 Å³/Da / Density % sol: 53.05 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 20% PEG3350, 10% ethylene glycol, 0.1 M bis-tris-propane pH 6.5 and 0.2 M sodium/potassium tartrat

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9201 Å
Detector	Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Feb 8, 2016
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9201 Å / Relative weight: 1
Reflection	Resolution: 2.35→92.86 Å / Num. obs: 164333 / % possible obs: 99.7 % / Redundancy: 3.1 % / R_merge(I) obs: 0.11 / Net I/σ(I): 6.6
Reflection shell	Resolution: 2.35→2.39 Å / Redundancy: 2.8 % / R_merge(I) obs: 0.59 / Mean I/σ(I) obs: 1.8 / Num. unique obs: 8004 / % possible all: 98.3

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0232	refinement
MOSFLM		data reduction
Aimless		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 4GYI

4gyi

Resolution: 2.35→78.34 Å / Cor.coef. F_o:F_c: 0.94 / Cor.coef. F_o:F_c free: 0.932 / SU B: 18.895 / SU ML: 0.208 / Cross valid method: THROUGHOUT / ESU R: 0.314 / ESU R Free: 0.218 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.23543	8217	5 %	RANDOM
R_work	0.21494	-	-	-
obs	0.21595	156092	99.66 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å

Displacement parameters

B_iso mean: 53.696 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.75 Å²	-0 Å²	-0.26 Å²
2-	-	-0.64 Å²	-0 Å²
3-	-	-	-0.03 Å²

Refinement step

Cycle: 1 / Resolution: 2.35→78.34 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	22681	0	292	376	23349

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.008	0.013	23484
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.017	21359
X-RAY DIFFRACTION	r_angle_refined_deg	1.415	1.636	31766
X-RAY DIFFRACTION	r_angle_other_deg	1.252	1.574	49250
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.299	5	2847
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	30.625	22.23	1220
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	17.398	15	3888
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	23.505	15	136
X-RAY DIFFRACTION	r_chiral_restr	0.069	0.2	2984
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	26263
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	5159
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	1.093	2.308	11454
X-RAY DIFFRACTION	r_mcbond_other	1.093	2.308	11453
X-RAY DIFFRACTION	r_mcangle_it	1.928	3.454	14279
X-RAY DIFFRACTION	r_mcangle_other	1.928	3.454	14280
X-RAY DIFFRACTION	r_scbond_it	1.269	2.468	12030
X-RAY DIFFRACTION	r_scbond_other	1.268	2.468	12031
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	2.063	3.649	17488
X-RAY DIFFRACTION	r_long_range_B_refined	4.416	26.435	25214
X-RAY DIFFRACTION	r_long_range_B_other	4.416	26.435	25214
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 / Type: interatomic distance / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	A	9286	0.05
1	2	B	9286	0.05
2	1	A	9236	0.06
2	2	C	9236	0.06
3	1	A	9162	0.04
3	2	D	9162	0.04
4	1	A	9109	0.05
4	2	E	9109	0.05
5	1	A	9128	0.04
5	2	F	9128	0.04
6	1	A	8714	0.05
6	2	G	8714	0.05
7	1	A	9033	0.05
7	2	H	9033	0.05
8	1	A	9095	0.06
8	2	I	9095	0.06
9	1	A	9017	0.05
9	2	J	9017	0.05
10	1	B	9277	0.04
10	2	C	9277	0.04
11	1	B	9207	0.02
11	2	D	9207	0.02
12	1	B	9145	0.03
12	2	E	9145	0.03
13	1	B	9181	0.03
13	2	F	9181	0.03
14	1	B	8767	0.04
14	2	G	8767	0.04
15	1	B	9014	0.04
15	2	H	9014	0.04
16	1	B	9164	0.04
16	2	I	9164	0.04
17	1	B	9042	0.05
17	2	J	9042	0.05
18	1	C	9167	0.04
18	2	D	9167	0.04
19	1	C	9106	0.04
19	2	E	9106	0.04
20	1	C	9154	0.03
20	2	F	9154	0.03
21	1	C	8725	0.04
21	2	G	8725	0.04
22	1	C	8974	0.05
22	2	H	8974	0.05
23	1	C	9090	0.05
23	2	I	9090	0.05
24	1	C	9000	0.06
24	2	J	9000	0.06
25	1	D	9093	0.02
25	2	E	9093	0.02
26	1	D	9113	0.03
26	2	F	9113	0.03
27	1	D	8690	0.03
27	2	G	8690	0.03
28	1	D	8929	0.03
28	2	H	8929	0.03
29	1	D	9058	0.03
29	2	I	9058	0.03
30	1	D	9019	0.04
30	2	J	9019	0.04
31	1	E	9071	0.03
31	2	F	9071	0.03
32	1	E	8667	0.03
32	2	G	8667	0.03
33	1	E	8910	0.03
33	2	H	8910	0.03
34	1	E	8990	0.04
34	2	I	8990	0.04
35	1	E	8965	0.04
35	2	J	8965	0.04
36	1	F	8721	0.03
36	2	G	8721	0.03
37	1	F	8906	0.03
37	2	H	8906	0.03
38	1	F	9026	0.04
38	2	I	9026	0.04
39	1	F	8983	0.04
39	2	J	8983	0.04
40	1	G	8715	0.04
40	2	H	8715	0.04
41	1	G	8636	0.05
41	2	I	8636	0.05
42	1	G	8580	0.05
42	2	J	8580	0.05
43	1	H	8878	0.05
43	2	I	8878	0.05
44	1	H	8807	0.05
44	2	J	8807	0.05
45	1	I	9024	0.03
45	2	J	9024	0.03

LS refinement shell

Resolution: 2.35→2.411 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.329	633	-
R_work	0.327	11360	-
obs	-	-	98.69 %

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	2.3972	-0.8349	0.3209	0.961	-0.0003	1.3031	0.0228	0.0538	-0.1144	-0.0144	-0.0086	-0.0133	0.0557	0.0152	-0.0142	0.0317	-0.0261	0.017	0.2563	-0.0169	0.0198	-66.1513	-11.0372	88.2785
2	1.5851	-0.1278	0.4095	1.6625	0.6335	2.2074	0.0069	-0.1838	0.137	-0.0557	0.0949	-0.2526	-0.2427	-0.0322	-0.1017	0.0494	-0.0064	0.0481	0.2994	-0.0499	0.107	-66.5476	14.4291	88.9671
3	1.0631	0.0232	-0.5161	1.9395	-0.2194	2.5026	0.075	0.1838	0.1381	-0.4541	0.0196	-0.044	0.0503	-0.0064	-0.0946	0.2179	0.0197	0.0726	0.2989	-0.0596	0.074	-47.3375	-10.6368	46.3146
4	1.2835	-0.6083	-0.1249	2.2358	-0.0724	2.5647	-0.0664	-0.3066	-0.1532	0.2295	0.1004	0.1417	0.5178	-0.1139	-0.034	0.4772	0.1078	0.0714	0.3756	0.0165	0.0655	-36.9853	-45.3134	49.1278
5	2.0008	0.3742	0.0409	1.7827	0.7109	2.114	0.0969	0.0351	-0.4011	-0.1131	-0.1121	-0.0622	0.6027	-0.0563	0.0153	0.5468	0.0394	0.0485	0.3237	-0.0506	0.1016	-45.0917	-51.665	26.2238
6	2.078	-0.3075	0.1316	1.2203	0.2251	2.4407	-0.0047	0.1943	0.1854	-0.1559	-0.0658	0.2266	-0.2621	-0.3702	0.0706	0.1996	0.0031	-0.0035	0.4272	-0.0853	0.0996	-71.5413	-14.935	52.7795
7	2.3814	0.0132	-0.9513	1.1923	-0.1298	2.0302	-0.3336	-0.1293	-0.5698	0.0382	0.1455	-0.4075	0.2578	0.363	0.1881	0.846	0.2991	0.1649	0.5312	-0.0268	0.4717	-94.4313	-64.7546	14.711
8	2.6383	-0.1117	-0.2591	1.6218	-0.1564	1.3343	0.0154	0.2305	0.0382	-0.0735	-0.0808	-0.3247	0.049	0.3127	0.0653	0.0096	-0.0057	0.0159	0.4365	0.0382	0.0666	-27.4617	-32.2213	116.325
9	2.4082	1.2287	0.4808	1.7204	0.664	1.5477	-0.036	0.1074	-0.0318	-0.1207	0.0065	0.0631	-0.1768	-0.4188	0.0296	0.0412	0.1205	0.0119	0.5549	-0.0037	0.0915	-102.5112	17.5934	92.5598
10	2.8562	0.2146	-0.0229	1.9183	0.3415	1.7001	0.0205	0.1033	0.161	-0.2507	-0.0315	-0.5449	0.1031	0.4208	0.011	0.6783	0.1495	0.2418	0.5565	0.0216	0.2803	-106.5882	-43.3049	8.674

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 350
2	X-RAY DIFFRACTION	2	B	1 - 350
3	X-RAY DIFFRACTION	3	C	1 - 350
4	X-RAY DIFFRACTION	4	D	1 - 350
5	X-RAY DIFFRACTION	5	E	1 - 350
6	X-RAY DIFFRACTION	6	F	1 - 350
7	X-RAY DIFFRACTION	7	G	1 - 350
8	X-RAY DIFFRACTION	8	H	1 - 350
9	X-RAY DIFFRACTION	9	I	1 - 350
10	X-RAY DIFFRACTION	10	J	1 - 350

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