PDB-3i6w: Structure and Activation Mechanism of the CHK2 DNA-Damage Checkpo...

ID or keywords:

Entry

Database: PDB / ID: 3i6w

Title

Structure and Activation Mechanism of the CHK2 DNA-Damage Checkpoint Kinase

Components

Serine/threonine-protein kinase Chk2

Keywords

TRANSFERASE / Ser/Thr protein kinase / FHA domain / ATP-binding / Cell cycle / Disease mutation / Kinase / Li-Fraumeni syndrome / Magnesium / Metal-binding / Nucleotide-binding / Nucleus / Phosphoprotein / Proto-oncogene / Serine/threonine-protein kinase

Function / homology

Function and homology information

mitotic DNA damage checkpoint signaling / mitotic intra-S DNA damage checkpoint signaling / DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator / thymocyte apoptotic process / regulation of protein catabolic process / mitotic spindle assembly / replicative senescence / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / signal transduction in response to DNA damage / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.25 Å

Authors

Pavletich, N.P.

Citation

Journal: Mol.Cell / Year: 2009
Title: Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase.
Authors: Cai, Z. / Chehab, N.H. / Pavletich, N.P.

History

Deposition	Jul 7, 2009	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Nov 10, 2009	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.2	Oct 13, 2021	Group: Database references / Category: database_2 / struct_ref_seq_dif Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.3	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	3i6w.cif.gz	598.5 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	3i6w_validation.pdf.gz	507.8 KB	Display	wwPDB validaton report
Full document	3i6w_full_validation.pdf.gz	601.1 KB	Display
Data in XML	3i6w_validation.xml.gz	103.9 KB	Display
Data in CIF	3i6w_validation.cif.gz	137.7 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/i6/3i6w ftp://data.pdbj.org/pub/pdb/validation_reports/i6/3i6w	HTTPS FTP

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Related structure data

Related structure data	3i6uSC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	3i6u-d 3zkw-d 6gkt-d 5lwq-d 5ki6-d 4edf-1 2no4-2 4edf-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) 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

3i6uSC

S: Starting model for refinement

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#122 - Feb 2010 Enhanceosome similarity (1) #231 - Mar 2019 Measles Virus Proteins similarity (2) #222 - Jun 2018 Proteins and Nanoparticles similarity (1)

Deposited unit

A: Serine/threonine-protein kinase Chk2

B: Serine/threonine-protein kinase Chk2

C: Serine/threonine-protein kinase Chk2

D: Serine/threonine-protein kinase Chk2

E: Serine/threonine-protein kinase Chk2

F: Serine/threonine-protein kinase Chk2

G: Serine/threonine-protein kinase Chk2

H: Serine/threonine-protein kinase Chk2

407 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Serine/threonine-protein kinase Chk2

B: Serine/threonine-protein kinase Chk2

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

2

C: Serine/threonine-protein kinase Chk2

D: Serine/threonine-protein kinase Chk2

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

3

E: Serine/threonine-protein kinase Chk2

F: Serine/threonine-protein kinase Chk2

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

4

G: Serine/threonine-protein kinase Chk2

H: Serine/threonine-protein kinase Chk2

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

Unit cell

Length a, b, c (Å)	76.200, 114.700, 123.000
Angle α, β, γ (deg.)	84.10, 81.20, 80.70
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Refine code: 1

Dom-ID	Component-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	1	PRO	PRO	THR	THR	A	A	92 - 205	23 - 136
2	1	1	PRO	PRO	THR	THR	B	B	92 - 205	23 - 136
3	1	1	PRO	PRO	THR	THR	C	C	92 - 205	23 - 136
4	1	1	PRO	PRO	THR	THR	D	D	92 - 205	23 - 136
5	1	1	PRO	PRO	THR	THR	E	E	92 - 205	23 - 136
6	1	1	PRO	PRO	THR	THR	F	F	92 - 205	23 - 136
7	1	1	PRO	PRO	THR	THR	G	G	92 - 205	23 - 136
8	1	1	PRO	PRO	THR	THR	H	H	92 - 205	23 - 136
1	1	2	VAL	VAL	VAL	VAL	A	A	206 - 211	137 - 142
2	1	2	VAL	VAL	VAL	VAL	B	B	206 - 211	137 - 142
3	1	2	VAL	VAL	VAL	VAL	C	C	206 - 211	137 - 142
4	1	2	VAL	VAL	VAL	VAL	D	D	206 - 211	137 - 142
5	1	2	VAL	VAL	VAL	VAL	E	E	206 - 211	137 - 142
6	1	2	VAL	VAL	VAL	VAL	F	F	206 - 211	137 - 142
7	1	2	VAL	VAL	VAL	VAL	G	G	206 - 211	137 - 142
8	1	2	VAL	VAL	VAL	VAL	H	H	206 - 211	137 - 142
1	1	3	TYR	TYR	LEU	LEU	A	A	212 - 226	143 - 157
2	1	3	TYR	TYR	LEU	LEU	C	C	212 - 226	143 - 157
3	1	3	TYR	TYR	LEU	LEU	E	E	212 - 226	143 - 157
4	1	3	TYR	TYR	LEU	LEU	G	G	212 - 226	143 - 157
1	2	3	GLU	GLU	LYS	LYS	A	A	233 - 253	164 - 184
2	2	3	GLU	GLU	LYS	LYS	C	C	233 - 253	164 - 184
3	2	3	GLU	GLU	LYS	LYS	E	E	233 - 253	164 - 184
4	2	3	GLU	GLU	LYS	LYS	G	G	233 - 253	164 - 184
1	3	3	LEU	LEU	GLU	GLU	A	A	268 - 305	199 - 236
2	3	3	LEU	LEU	GLU	GLU	C	C	268 - 305	199 - 236
3	3	3	LEU	LEU	GLU	GLU	E	E	268 - 305	199 - 236
4	3	3	LEU	LEU	GLU	GLU	G	G	268 - 305	199 - 236
1	1	4	TYR	TYR	LEU	LEU	B	B	212 - 226	143 - 157
2	1	4	TYR	TYR	LEU	LEU	D	D	212 - 226	143 - 157
3	1	4	TYR	TYR	LEU	LEU	F	F	212 - 226	143 - 157
4	1	4	TYR	TYR	LEU	LEU	H	H	212 - 226	143 - 157
1	2	4	GLU	GLU	LYS	LYS	B	B	233 - 253	164 - 184
2	2	4	GLU	GLU	LYS	LYS	D	D	233 - 253	164 - 184
3	2	4	GLU	GLU	LYS	LYS	F	F	233 - 253	164 - 184
4	2	4	GLU	GLU	LYS	LYS	H	H	233 - 253	164 - 184
1	3	4	LEU	LEU	GLU	GLU	B	B	268 - 305	199 - 236
2	3	4	LEU	LEU	GLU	GLU	D	D	268 - 305	199 - 236
3	3	4	LEU	LEU	GLU	GLU	F	F	268 - 305	199 - 236
4	3	4	LEU	LEU	GLU	GLU	H	H	268 - 305	199 - 236
1	1	5	GLY	GLY	ASP	ASP	A	A	306 - 368	237 - 299
2	1	5	GLY	GLY	ASP	ASP	B	B	306 - 368	237 - 299
3	1	5	GLY	GLY	ASP	ASP	C	C	306 - 368	237 - 299
4	1	5	GLY	GLY	ASP	ASP	D	D	306 - 368	237 - 299
5	1	5	GLY	GLY	ASP	ASP	E	E	306 - 368	237 - 299
6	1	5	GLY	GLY	ASP	ASP	F	F	306 - 368	237 - 299
7	1	5	GLY	GLY	ASP	ASP	G	G	306 - 368	237 - 299
8	1	5	GLY	GLY	ASP	ASP	H	H	306 - 368	237 - 299
1	1	6	PHE	PHE	ARG	ARG	B	B	369 - 382	300 - 313
2	1	6	PHE	PHE	ARG	ARG	D	D	369 - 382	300 - 313
3	1	6	PHE	PHE	ARG	ARG	F	F	369 - 382	300 - 313
4	1	6	PHE	PHE	ARG	ARG	H	H	369 - 382	300 - 313
1	1	7	PRO	PRO	VAL	VAL	B	B	388 - 397	319 - 328
2	1	7	PRO	PRO	VAL	VAL	D	D	388 - 397	319 - 328
3	1	7	PRO	PRO	VAL	VAL	F	F	388 - 397	319 - 328
4	1	7	PRO	PRO	VAL	VAL	H	H	388 - 397	319 - 328
1	1	8	PRO	PRO	VAL	VAL	A	A	388 - 397	319 - 328
2	1	8	PRO	PRO	VAL	VAL	C	C	388 - 397	319 - 328
3	1	8	PRO	PRO	VAL	VAL	E	E	388 - 397	319 - 328
4	1	8	PRO	PRO	VAL	VAL	G	G	388 - 397	319 - 328
1	1	9	ALA	ALA	GLU	GLU	A	A	402 - 501	333 - 432
2	1	9	ALA	ALA	GLU	GLU	B	B	402 - 501	333 - 432
3	1	9	ALA	ALA	GLU	GLU	C	C	402 - 501	333 - 432
4	1	9	ALA	ALA	GLU	GLU	D	D	402 - 501	333 - 432
5	1	9	ALA	ALA	GLU	GLU	E	E	402 - 501	333 - 432
6	1	9	ALA	ALA	GLU	GLU	F	F	402 - 501	333 - 432
7	1	9	ALA	ALA	GLU	GLU	G	G	402 - 501	333 - 432
8	1	9	ALA	ALA	GLU	GLU	H	H	402 - 501	333 - 432

NCS ensembles :

ID
1
2
3
4
5
6
7
8
9

Details

transient dimer, four copies of dimer in asymmetric unit

#1: Protein	Serine/threonine-protein kinase Chk2 / Cds1 Mass: 50839.945 Da / Num. of mol.: 8 / Fragment: residues 70-512 / Mutation: K249A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CHEK2, CHK2, RAD53 / Production host: Escherichia coli (E. coli) References: UniProt: O96017, non-specific serine/threonine protein kinase

#1: Protein

Serine/threonine-protein kinase Chk2 / Cds1

Mass: 50839.945 Da / Num. of mol.: 8 / Fragment: residues 70-512 / Mutation: K249A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Homo sapiens (human) / Gene: CHEK2, CHK2, RAD53 / Production host:

Escherichia coli (E. coli)
References: UniProt: O96017, non-specific serine/threonine protein kinase

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.57 Å³/Da / Density % sol: 52.21 %
Crystal grow	Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 1:1 ratio mix of protein solution (~12 mg/ml protein in 20 mM Tris-HCl, 150 mM NaCl, 10 mM dithiothreitol (DTT), 3% (v/v) glycerol, pH 8.0 and well bufffer (100 mM NaHepes, 300 mM Ammonium ...Details: 1:1 ratio mix of protein solution (~12 mg/ml protein in 20 mM Tris-HCl, 150 mM NaCl, 10 mM dithiothreitol (DTT), 3% (v/v) glycerol, pH 8.0 and well bufffer (100 mM NaHepes, 300 mM Ammonium Tartrate, 22% PEG 3350, pH 7.0). Crystals were flash frozen in crystallization buffer supplemented with 16-20% (v/v) glycerol., VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystal

Density Matthews: 2.57 Å³/Da / Density % sol: 52.21 %

Crystal grow

Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 1:1 ratio mix of protein solution (~12 mg/ml protein in 20 mM Tris-HCl, 150 mM NaCl, 10 mM dithiothreitol (DTT), 3% (v/v) glycerol, pH 8.0 and well bufffer (100 mM NaHepes, 300 mM Ammonium ...

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Data collection

Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 1.03944
Detector	Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 10, 2006
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.03944 Å / Relative weight: 1
Reflection	Resolution: 3.25→30 Å / Num. obs: 60983 / % possible obs: 96.2 % / Redundancy: 1.8 % / R_sym value: 0.042

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Processing

Software

Name: REFMAC / Version: 5.3.0036 / Classification: refinement

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 3I6U

3i6u

Resolution: 3.25→30 Å / Cor.coef. F_o:F_c: 0.923 / Cor.coef. F_o:F_c free: 0.894 / SU B: 81.426 / SU ML: 0.579 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.645 / Stereochemistry target values: MAXIMUM LIKELIHOOD

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.287	1755	3 %	RANDOM
R_work	0.251	-	-	-
obs	0.252	56117	90.8 %	-

Solvent computation

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

Displacement parameters

B_iso mean: 137.5 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.26 Å²	-0.34 Å²	1.73 Å²
2-	-	-3.09 Å²	-3.45 Å²
3-	-	-	3.64 Å²

Refinement step

Cycle: LAST / Resolution: 3.25→30 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	24560	0	0	0	24560

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.022	25092
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.138	1.966	33834
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.446	5	2962
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	38.202	24.147	1196
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	19.937	15	4632
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	21.623	15	148
X-RAY DIFFRACTION	r_chiral_restr	0.076	0.2	3724
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.02	18628
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.218	0.2	11364
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.31	0.2	17094
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.144	0.2	720
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	0.619	0.2	247
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.626	0.2	18
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	1.442	1.25	15151
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	2.574	2.25	24182
X-RAY DIFFRACTION	r_scbond_it	2.596	2	11040
X-RAY DIFFRACTION	r_scangle_it	4.357	3.75	9652
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	951	tight positional	0.02	0.03
1	2	B	951	tight positional	0.02	0.03
1	3	C	951	tight positional	0.03	0.03
1	4	D	951	tight positional	0.02	0.03
1	5	E	951	tight positional	0.01	0.03
1	6	F	951	tight positional	0.01	0.03
1	7	G	951	tight positional	0.01	0.03
1	8	H	951	tight positional	0.01	0.03
2	1	A	45	tight positional	0.03	0.03
2	2	B	45	tight positional	0.02	0.03
2	3	C	45	tight positional	0.05	0.03
2	4	D	45	tight positional	0.03	0.03
2	5	E	45	tight positional	0.02	0.03
2	6	F	45	tight positional	0.02	0.03
2	7	G	45	tight positional	0.02	0.03
2	8	H	45	tight positional	0.01	0.03
3	1	A	613	tight positional	0.02	0.03
3	2	C	613	tight positional	0.02	0.03
3	3	E	613	tight positional	0.01	0.03
3	4	G	613	tight positional	0.02	0.03
4	1	B	613	tight positional	0.02	0.03
4	2	D	613	tight positional	0.02	0.03
4	3	F	613	tight positional	0.02	0.03
4	4	H	613	tight positional	0.01	0.03
5	1	A	510	tight positional	0.02	0.03
5	2	B	510	tight positional	0.02	0.03
5	3	C	510	tight positional	0.03	0.03
5	4	D	510	tight positional	0.02	0.03
5	5	E	510	tight positional	0.02	0.03
5	6	F	510	tight positional	0.02	0.03
5	7	G	510	tight positional	0.02	0.03
5	8	H	510	tight positional	0.01	0.03
6	1	B	109	tight positional	0.02	0.03
6	2	D	109	tight positional	0.01	0.03
6	3	F	109	tight positional	0.01	0.03
6	4	H	109	tight positional	0.01	0.03
7	1	B	77	tight positional	0.01	0.03
7	2	D	77	tight positional	0.01	0.03
7	3	F	77	tight positional	0.01	0.03
7	4	H	77	tight positional	0.01	0.03
8	1	A	77	tight positional	0.01	0.03
8	2	C	77	tight positional	0.01	0.03
8	3	E	77	tight positional	0.01	0.03
8	4	G	77	tight positional	0.01	0.03
9	1	A	812	tight positional	0.02	0.03
9	2	B	812	tight positional	0.01	0.03
9	3	C	812	tight positional	0.02	0.03
9	4	D	812	tight positional	0.01	0.03
9	5	E	812	tight positional	0.01	0.03
9	6	F	812	tight positional	0.01	0.03
9	7	G	812	tight positional	0.01	0.03
9	8	H	812	tight positional	0.01	0.03
1	1	A	951	tight thermal	2.64	6
1	2	B	951	tight thermal	3.11	6
1	3	C	951	tight thermal	3.76	6
1	4	D	951	tight thermal	2.36	6
1	5	E	951	tight thermal	2.39	6
1	6	F	951	tight thermal	1.75	6
1	7	G	951	tight thermal	1.77	6
1	8	H	951	tight thermal	1.81	6
2	1	A	45	tight thermal	1.54	6
2	2	B	45	tight thermal	1.75	6
2	3	C	45	tight thermal	3.26	6
2	4	D	45	tight thermal	1.68	6
2	5	E	45	tight thermal	1.46	6
2	6	F	45	tight thermal	1.79	6
2	7	G	45	tight thermal	1.55	6
2	8	H	45	tight thermal	1.92	6
3	1	A	613	tight thermal	2.3	6
3	2	C	613	tight thermal	2.38	6
3	3	E	613	tight thermal	1.77	6
3	4	G	613	tight thermal	2.14	6
4	1	B	613	tight thermal	2.63	6
4	2	D	613	tight thermal	2.72	6
4	3	F	613	tight thermal	1.89	6
4	4	H	613	tight thermal	2.19	6
5	1	A	510	tight thermal	2.94	6
5	2	B	510	tight thermal	2.41	6
5	3	C	510	tight thermal	3.59	6
5	4	D	510	tight thermal	2.36	6
5	5	E	510	tight thermal	2.89	6
5	6	F	510	tight thermal	2.52	6
5	7	G	510	tight thermal	2.52	6
5	8	H	510	tight thermal	1.69	6
6	1	B	109	tight thermal	2.97	6
6	2	D	109	tight thermal	2.26	6
6	3	F	109	tight thermal	2.41	6
6	4	H	109	tight thermal	2.08	6
7	1	B	77	tight thermal	1.47	6
7	2	D	77	tight thermal	1.63	6
7	3	F	77	tight thermal	1.27	6
7	4	H	77	tight thermal	1.5	6
8	1	A	77	tight thermal	2.34	6
8	2	C	77	tight thermal	2.09	6
8	3	E	77	tight thermal	2.23	6
8	4	G	77	tight thermal	1.2	6
9	1	A	812	tight thermal	2.65	6
9	2	B	812	tight thermal	1.86	6
9	3	C	812	tight thermal	3.8	6
9	4	D	812	tight thermal	1.69	6
9	5	E	812	tight thermal	2.24	6
9	6	F	812	tight thermal	1.88	6
9	7	G	812	tight thermal	2.32	6
9	8	H	812	tight thermal	1.84	6

LS refinement shell

Resolution: 3.25→3.33 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.389	100	-
R_work	0.37	3569	-
obs	-	-	77.87 %

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	12.2737	2.3058	-1.8714	14.8407	-5.9301	16.2071	-1.0921	0.4317	-0.6876	0.6885	1.0821	-0.2891	-1.0601	-1.886	0.01	-0.3853	0.2749	-0.041	-0.4827	0.0007	-0.6622	-25.1264	-10.8568	15.5897
2	9.6612	1.436	0.6314	12.3711	0.4349	7.2058	0.2657	-0.7952	0.7039	0.8478	-0.0024	-0.2093	-0.7927	-0.1089	-0.2633	-0.451	-0.0191	-0.1199	-0.662	0.0303	-0.5991	0.4045	-19.0126	24.3489
3	11.0362	0.6714	2.9354	10.6137	0.6197	6.3718	-0.2608	0.5776	1.0029	-0.1392	0.1528	1.1076	-0.215	-0.1661	0.108	-0.7641	-0.0203	0.0413	-1.0001	0.0814	-0.3869	-5.5183	-46.6079	11.7799
4	7.626	1.804	2.6123	20.1697	2.7719	9.5476	0.3123	-0.7669	-0.2759	1.1572	-0.5097	-0.9358	0.393	-0.4701	0.1974	-0.3298	0.0598	0.0556	-0.0726	0.0654	-0.1026	-27.4474	-39.9004	29.2913
5	19.5514	9.8367	-0.8814	13.9807	2.0838	7.7979	-0.4116	-0.4154	0.1611	-1.314	0.0752	0.6206	0.0776	0.062	0.3364	0.6571	-0.0583	-0.51	-0.6667	0.3223	-0.0229	-1.926	-35.4486	-62.1834
6	6.0774	-0.3079	-0.0854	3.8455	-2.0274	6.9545	-0.2606	0.1823	0.4364	0.3166	0.0844	0.7028	0.6059	-1.5142	0.1762	0.9289	-0.3791	-0.1322	0.5202	-0.3284	0.1121	0.3506	-38.6998	-33.9671
7	11.1173	1.257	0.6918	13.3441	6.7969	10.626	0.2525	-0.7539	-0.7609	0.5825	-0.5709	-0.7232	0.0112	-0.2102	0.3184	0.2903	-0.1543	-0.14	-0.3316	0.2475	-0.0235	6.4923	-69.0285	-38.0227
8	7.8753	1.0258	1.9633	14.9148	-0.3094	10.7368	-0.9781	-0.1506	-0.183	1.2109	0.056	0.63	-0.4866	-1.4753	0.9221	0.1429	0.259	0.0391	0.0962	-0.0203	-0.4596	-17.191	-62.0597	-52.9382
9	10.5106	5.1317	-5.8612	4.2738	-2.2856	10.0374	-0.3283	1.1221	-0.6752	-0.2581	0.3719	0.3814	0.7149	-0.9893	-0.0435	-0.0821	0.0507	0.1819	-0.4509	0.1185	-0.1304	9.0736	-12.5657	-2.3429
10	4.5204	1.3408	-1.3746	7.5445	-5.6677	8.0573	-0.2655	-0.3032	0.1629	1.089	0.4813	-0.1238	0.1237	0.1472	-0.2158	-0.1713	0.1135	-0.2158	-0.7043	0.0114	-0.3709	-11.0928	11.4902	2.9205
11	11.2986	3.7726	3.2363	4.859	0.8436	4.7796	-0.159	1.28	1.7355	-0.6256	-0.014	-0.5487	-0.7837	-0.0181	0.173	-0.3022	0.1205	0.1334	-0.176	0.2018	0.1641	-42.9409	-44.3996	4.4241
12	6.669	3.2372	3.7371	9.5148	7.1584	7.193	0.0862	-0.7364	0.1189	0.713	-0.2781	0.354	0.374	-0.1907	0.1919	-0.5477	-0.1012	0.0249	-0.6686	0.1005	-0.0622	-21.7463	-68.6392	2.9293
13	14.3516	4.484	2.2079	7.1642	4.0695	6.0436	-0.055	0.8661	-0.9542	-0.517	0.1246	-0.2019	1.3021	0.4893	-0.0696	0.6563	0.2229	-0.3277	-0.1561	-0.1593	0.1172	29.1609	-35.4497	-38.4328
14	14.7764	2.8102	-2.4478	7.9173	-1.5994	4.8269	0.8384	-0.4384	-0.0109	0.3907	-0.332	0.7648	0.3861	-0.2253	-0.5064	0.4215	0.0635	-0.2078	-0.4468	0.1035	-0.2117	16.1165	-13.4981	-58.7491
15	3.0616	-0.5778	-2.8996	8.1647	7.0931	10.8758	0.0959	-0.3593	0.3967	0.2375	0.0113	-0.7418	-0.9786	0.9632	-0.1072	0.1804	-0.0599	0.0986	0.2619	-0.0183	-0.5586	-2.379	-71.3915	-75.7747
16	5.7325	-3.0567	-1.7496	10.7154	5.8215	7.4972	0.015	-0.734	0.2623	0.715	-0.0778	0.0597	-0.0472	-0.618	0.0628	0.3392	0.088	0.1865	-0.3324	0.2608	0.4172	5.19	-93.4083	-53.9454
17	4.4719	1.4715	-1.4341	12.1994	2.108	6.9317	-0.2712	-0.6558	0.528	0.3917	0.7749	0.2773	-0.3567	0.3776	-0.5036	-0.6062	-0.046	-0.0215	-0.3138	-0.2806	-0.6557	26.6239	10.2549	-2.891
18	4.1528	0.5866	-1.2233	6.3295	1.8439	6.456	-0.1695	1.3377	-0.5759	-0.8102	0.1741	-0.3047	0.891	0.3163	-0.0046	-0.0411	-0.1378	-0.132	-0.0348	-0.0053	-0.4188	-8.6566	10.4614	-24.5361
19	3.8486	0.6024	-0.3349	7.4617	0.6784	4.8158	0.0315	1.2384	-0.2034	-0.5806	0.0371	-0.5542	0.2251	-0.5946	-0.0686	-0.6651	0.0165	0.0592	-0.1675	-0.1463	-0.7873	-58.1972	-69.1527	7.1354
20	5.2058	-0.8172	1.0546	6.413	-0.5587	6.4563	0.1112	0.469	0.8815	-1.0579	-0.1566	0.1003	-0.8911	-0.6093	0.0454	-0.0812	0.0712	0.0208	-0.3357	0.2778	-0.2521	-32.2244	-65.5341	-22.6423
21	9.3819	-1.6895	-1.7606	9.7732	1.3616	6.1996	-0.1003	0.3007	-0.0186	-0.824	0.6708	-0.4526	-0.0194	1.0604	-0.5705	-0.1495	-0.2521	-0.0723	-0.0607	-0.4668	-0.7437	36.8339	-9.0444	-29.5254
22	9.8873	-1.4009	1.2559	4.165	-2.1359	1.8702	0.8276	0.9287	-0.1453	-0.494	-0.4984	-0.1118	0.8429	0.6252	-0.3292	0.7285	0.5901	-0.1118	0.0804	-0.1528	-0.5106	41.8355	-18.027	-67.6392
23	2.8607	2.102	-0.7767	7.6811	-0.6192	5.3399	-0.093	-0.8777	-1.1142	1.1358	-0.0576	0.6927	1.2485	-1.5643	0.1507	0.0311	-0.5131	0.3579	0.3878	-0.0034	-0.1398	-14.1816	-95.5942	-86.404
24	1.5436	1.622	-0.7018	5.0243	-0.5456	6.2053	0.0151	0.5299	0.3851	-0.2433	0.1794	-0.7301	-0.5307	1.143	-0.1945	0.1145	0.0576	0.4447	0.4754	0.1933	0.7759	24.9455	-94.7298	-73.1323

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	92 - 207
2	X-RAY DIFFRACTION	2	B	92 - 207
3	X-RAY DIFFRACTION	3	C	92 - 207
4	X-RAY DIFFRACTION	4	D	92 - 207
5	X-RAY DIFFRACTION	5	E	92 - 207
6	X-RAY DIFFRACTION	6	F	92 - 207
7	X-RAY DIFFRACTION	7	G	92 - 207
8	X-RAY DIFFRACTION	8	H	92 - 207
9	X-RAY DIFFRACTION	9	A	208 - 305
10	X-RAY DIFFRACTION	10	B	208 - 305
11	X-RAY DIFFRACTION	11	C	208 - 305
12	X-RAY DIFFRACTION	12	D	208 - 305
13	X-RAY DIFFRACTION	13	E	208 - 305
14	X-RAY DIFFRACTION	14	F	208 - 305
15	X-RAY DIFFRACTION	15	G	208 - 305
16	X-RAY DIFFRACTION	16	H	208 - 305
17	X-RAY DIFFRACTION	17	A	306 - 501
18	X-RAY DIFFRACTION	18	B	306 - 501
19	X-RAY DIFFRACTION	19	C	306 - 501
20	X-RAY DIFFRACTION	20	D	306 - 501
21	X-RAY DIFFRACTION	21	E	306 - 501
22	X-RAY DIFFRACTION	22	F	306 - 501
23	X-RAY DIFFRACTION	23	G	306 - 501
24	X-RAY DIFFRACTION	24	H	306 - 501

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