PDB-5jhq: ARCs 1-3 of human Tankyrase-1 bound to a peptide derived from IRAP

ID or keywords:

Entry

Database: PDB / ID: 5jhq

Title

ARCs 1-3 of human Tankyrase-1 bound to a peptide derived from IRAP

Components

Peptide derived from insulin-responsive aminopeptidase (IRAP)
Tankyrase-1

Keywords

TRANSFERASE / ADP-ribosyl transferase / PARP / Tankyrase-1 / TNKS

Function / homology

Function and homology information

cystinyl aminopeptidase / antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent / : / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / positive regulation of telomere maintenance via telomere lengthening / regulation of telomere maintenance via telomerase / XAV939 stabilizes AXIN / positive regulation of telomere capping / NAD+ ADP-ribosyltransferase / negative regulation of cold-induced thermogenesis ...cystinyl aminopeptidase / antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent / : / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / positive regulation of telomere maintenance via telomere lengthening / regulation of telomere maintenance via telomerase / XAV939 stabilizes AXIN / positive regulation of telomere capping / NAD+ ADP-ribosyltransferase / negative regulation of cold-induced thermogenesis / negative regulation of telomere maintenance via telomere lengthening / protein auto-ADP-ribosylation / protein localization to chromosome, telomeric region / NAD+-protein-aspartate ADP-ribosyltransferase activity / protein poly-ADP-ribosylation / peptide catabolic process / NAD+-protein-glutamate ADP-ribosyltransferase activity / pericentriolar material / mitotic spindle pole / NAD+-protein mono-ADP-ribosyltransferase activity / metalloaminopeptidase activity / NAD+ poly-ADP-ribosyltransferase activity / Transferases; Glycosyltransferases; Pentosyltransferases / mRNA transport / aminopeptidase activity / nuclear pore / spindle assembly / positive regulation of telomere maintenance via telomerase / nucleotidyltransferase activity / peptidyl-threonine phosphorylation / cytoplasmic vesicle membrane / peptide binding / early endosome lumen / mitotic spindle organization / TCF dependent signaling in response to WNT / female pregnancy / Translocation of SLC2A4 (GLUT4) to the plasma membrane / Endosomal/Vacuolar pathway / Degradation of AXIN / protein catabolic process / regulation of blood pressure / Wnt signaling pathway / Regulation of PTEN stability and activity / protein polyubiquitination / metallopeptidase activity / positive regulation of canonical Wnt signaling pathway / Antigen processing: Ubiquitination & Proteasome degradation / protein transport / cell-cell signaling / peptidyl-serine phosphorylation / nuclear membrane / histone binding / chromosome, telomeric region / Ub-specific processing proteases / nuclear body / Golgi membrane / lysosomal membrane / cell division / perinuclear region of cytoplasm / Golgi apparatus / positive regulation of transcription by RNA polymerase II / proteolysis / extracellular space / zinc ion binding / nucleoplasm / nucleus / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.2 Å

Authors

Eisemann, T. / Pascal, J.M.

Funding support

United States, 1items

Citation

Journal: Structure / Year: 2016
Title: Tankyrase-1 Ankyrin Repeats Form an Adaptable Binding Platform for Targets of ADP-Ribose Modification.
Authors: Eisemann, T. / McCauley, M. / Langelier, M.F. / Gupta, K. / Roy, S. / Van Duyne, G.D. / Pascal, J.M.

History

Deposition	Apr 21, 2016	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 21, 2016	Provider: repository / Type: Initial release
Revision 1.1	Oct 19, 2016	Group: Database references
Revision 1.2	Sep 27, 2017	Group: Author supporting evidence / Database references / Derived calculations Category: citation / pdbx_audit_support / pdbx_struct_oper_list Item: _citation.journal_id_CSD / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3	Dec 25, 2019	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4	Sep 27, 2023	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 / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_symmetry / _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
Revision 1.5	Oct 23, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/jh/5jhq ftp://data.pdbj.org/pub/pdb/validation_reports/jh/5jhq	HTTPS FTP

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Related structure data

Related structure data	3twwS S: Starting model for refinement
Similar structure data	4xvg-d 5bqe-1 4jw1-1 4jq7-1 3u2p-d 1401 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

3twwS

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	#250 - Oct 2020 Capsaicin Receptor TRPV1 similarity (1) #60 - Dec 2004 Ubiquitin similarity (1) #222 - Jun 2018 Proteins and Nanoparticles similarity (1) #245 - May 2020 Spliceosomes similarity (1) #44 - Aug 2003 Calmodulin similarity (1) #223 - Jul 2018 Piezo1 Mechanosensitive Channel similarity (1) #234 - Jun 2019 MDM2 and Cancer similarity (1) #196 - Apr 2016 Lead Poisoning similarity (1) #28 - Apr 2002 Anthrax Toxin similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#250 - Oct 2020
Capsaicin Receptor TRPV1
similarity (1)
#60 - Dec 2004
Ubiquitin
similarity (1)
#222 - Jun 2018
Proteins and Nanoparticles
similarity (1)
#245 - May 2020
Spliceosomes
similarity (1)
#44 - Aug 2003
Calmodulin
similarity (1)
#223 - Jul 2018
Piezo1 Mechanosensitive Channel
similarity (1)
#234 - Jun 2019
MDM2 and Cancer
similarity (1)
#196 - Apr 2016
Lead Poisoning
similarity (1)
#28 - Apr 2002
Anthrax Toxin
similarity (1)

Deposited unit

A: Tankyrase-1

B: Tankyrase-1

C: Tankyrase-1

D: Tankyrase-1

E: Peptide derived from insulin-responsive aminopeptidase (IRAP)

F: Peptide derived from insulin-responsive aminopeptidase (IRAP)

G: Peptide derived from insulin-responsive aminopeptidase (IRAP)

H: Peptide derived from insulin-responsive aminopeptidase (IRAP)

I: Peptide derived from insulin-responsive aminopeptidase (IRAP)

J: Peptide derived from insulin-responsive aminopeptidase (IRAP)

K: Peptide derived from insulin-responsive aminopeptidase (IRAP)

L: Peptide derived from insulin-responsive aminopeptidase (IRAP)

221 kDa, 12 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Tankyrase-1

E: Peptide derived from insulin-responsive aminopeptidase (IRAP)

F: Peptide derived from insulin-responsive aminopeptidase (IRAP)

defined by author
55.3 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Tankyrase-1

G: Peptide derived from insulin-responsive aminopeptidase (IRAP)

H: Peptide derived from insulin-responsive aminopeptidase (IRAP)

defined by author
55.3 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: Tankyrase-1

I: Peptide derived from insulin-responsive aminopeptidase (IRAP)

J: Peptide derived from insulin-responsive aminopeptidase (IRAP)

defined by author
55.3 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: Tankyrase-1

K: Peptide derived from insulin-responsive aminopeptidase (IRAP)

L: Peptide derived from insulin-responsive aminopeptidase (IRAP)

defined by author
55.3 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	94.510, 129.830, 123.950
Angle α, β, γ (deg.)	90.00, 92.31, 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	ALA	ALA	GLU	GLU	A	A	182 - 641	15 - 474
2	1	ALA	ALA	GLU	GLU	B	B	182 - 641	15 - 474
1	2	ALA	ALA	GLU	GLU	A	A	182 - 641	15 - 474
2	2	ALA	ALA	GLU	GLU	C	C	182 - 641	15 - 474
1	3	GLY	GLY	GLU	GLU	A	A	181 - 641	14 - 474
2	3	GLY	GLY	GLU	GLU	D	D	181 - 641	14 - 474
1	4	ALA	ALA	SER	SER	B	B	182 - 642	15 - 475
2	4	ALA	ALA	SER	SER	C	C	182 - 642	15 - 475
1	5	ALA	ALA	GLU	GLU	B	B	182 - 641	15 - 474
2	5	ALA	ALA	GLU	GLU	D	D	182 - 641	15 - 474
1	6	ALA	ALA	GLU	GLU	C	C	182 - 641	15 - 474
2	6	ALA	ALA	GLU	GLU	D	D	182 - 641	15 - 474
1	7	GLY	GLY	CYS	CYS	E	E	3 - 12	3 - 12
2	7	GLY	GLY	CYS	CYS	F	F	3 - 12	3 - 12
1	8	TYR	TYR	SER	SER	E	E	4 - 13	4 - 13
2	8	TYR	TYR	SER	SER	G	G	4 - 13	4 - 13
1	9	TYR	TYR	CYS	CYS	E	E	4 - 12	4 - 12
2	9	TYR	TYR	CYS	CYS	H	H	4 - 12	4 - 12
1	10	TYR	TYR	SER	SER	E	E	4 - 13	4 - 13
2	10	TYR	TYR	SER	SER	I	I	4 - 13	4 - 13
1	11	TYR	TYR	CYS	CYS	E	E	4 - 12	4 - 12
2	11	TYR	TYR	CYS	CYS	J	J	4 - 12	4 - 12
1	12	TYR	TYR	CYS	CYS	E	E	4 - 12	4 - 12
2	12	TYR	TYR	CYS	CYS	K	K	4 - 12	4 - 12
1	13	TYR	TYR	CYS	CYS	F	F	4 - 12	4 - 12
2	13	TYR	TYR	CYS	CYS	G	G	4 - 12	4 - 12
1	14	TYR	TYR	CYS	CYS	F	F	4 - 12	4 - 12
2	14	TYR	TYR	CYS	CYS	H	H	4 - 12	4 - 12
1	15	TYR	TYR	CYS	CYS	F	F	4 - 12	4 - 12
2	15	TYR	TYR	CYS	CYS	I	I	4 - 12	4 - 12
1	16	TYR	TYR	CYS	CYS	F	F	4 - 12	4 - 12
2	16	TYR	TYR	CYS	CYS	J	J	4 - 12	4 - 12
1	17	TYR	TYR	CYS	CYS	F	F	4 - 12	4 - 12
2	17	TYR	TYR	CYS	CYS	K	K	4 - 12	4 - 12
1	18	TYR	TYR	CYS	CYS	G	G	4 - 12	4 - 12
2	18	TYR	TYR	CYS	CYS	H	H	4 - 12	4 - 12
1	19	TYR	TYR	VAL	VAL	G	G	4 - 14	4 - 14
2	19	TYR	TYR	VAL	VAL	I	I	4 - 14	4 - 14
1	20	TYR	TYR	CYS	CYS	G	G	4 - 12	4 - 12
2	20	TYR	TYR	CYS	CYS	J	J	4 - 12	4 - 12
1	21	TYR	TYR	CYS	CYS	G	G	4 - 12	4 - 12
2	21	TYR	TYR	CYS	CYS	K	K	4 - 12	4 - 12
1	22	TYR	TYR	CYS	CYS	H	H	4 - 12	4 - 12
2	22	TYR	TYR	CYS	CYS	I	I	4 - 12	4 - 12
1	23	TYR	TYR	SER	SER	H	H	4 - 13	4 - 13
2	23	TYR	TYR	SER	SER	J	J	4 - 13	4 - 13
1	24	TYR	TYR	SER	SER	H	H	4 - 13	4 - 13
2	24	TYR	TYR	SER	SER	K	K	4 - 13	4 - 13
1	25	TYR	TYR	CYS	CYS	I	I	4 - 12	4 - 12
2	25	TYR	TYR	CYS	CYS	J	J	4 - 12	4 - 12
1	26	TYR	TYR	CYS	CYS	I	I	4 - 12	4 - 12
2	26	TYR	TYR	CYS	CYS	K	K	4 - 12	4 - 12
1	27	TYR	TYR	SER	SER	J	J	4 - 13	4 - 13
2	27	TYR	TYR	SER	SER	K	K	4 - 13	4 - 13

NCS ensembles :

#1: Protein	Tankyrase-1 / TANK1 / ADP-ribosyltransferase diphtheria toxin-like 5 / ARTD5 / Poly [ADP-ribose] polymerase 5A / ...TANK1 / ADP-ribosyltransferase diphtheria toxin-like 5 / ARTD5 / Poly [ADP-ribose] polymerase 5A / TNKS-1 / TRF1-interacting ankyrin-related ADP-ribose polymerase / Tankyrase I Mass: 52120.441 Da / Num. of mol.: 4 / Fragment: UNP residues 174-649 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TNKS, PARP5A, PARPL, TIN1, TINF1, TNKS1 / Production host: Escherichia coli (E. coli) / References: UniProt: O95271, NAD+ ADP-ribosyltransferase
#2: Protein/peptide	Peptide derived from insulin-responsive aminopeptidase (IRAP) Mass: 1596.699 Da / Num. of mol.: 8 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q9UIQ6*PLUS
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 34 / Source method: isolated from a natural source / Formula: H₂O
Has protein modification	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.43 Å³/Da / Density % sol: 64.18 %
Crystal grow	Temperature: 290 K / Method: vapor diffusion, sitting drop / Details: 1.8 M (NH4)2SO4 100 mM Tris pH 8.5

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.0332 Å
Detector	Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Dec 12, 2012
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.0332 Å / Relative weight: 1
Reflection	Resolution: 3.2→30 Å / Num. obs: 48511 / % possible obs: 98.2 % / Redundancy: 5.7 % / Net I/σ(I): 11.8

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0135	refinement
XDS		data reduction
XDS		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 3TWW

3tww

Resolution: 3.2→20 Å / Cor.coef. F_o:F_c: 0.953 / Cor.coef. F_o:F_c free: 0.947 / SU B: 56.93 / SU ML: 0.384 / Cross valid method: THROUGHOUT / ESU R Free: 0.448 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.23947	2411	5 %	RANDOM
R_work	0.21382	-	-	-
obs	0.21514	45374	96.57 %	-

Solvent computation

Ion probe radii: 0.9 Å / Shrinkage radii: 0.9 Å / VDW probe radii: 1 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 138.813 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	5.71 Å²	0 Å²	-6.01 Å²
2-	-	-4.84 Å²	0 Å²
3-	-	-	-0.38 Å²

Refinement step

Cycle: LAST / Resolution: 3.2→20 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	14623	0	0	34	14657

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.008	0.019	14876
X-RAY DIFFRACTION	r_bond_other_d	0.004	0.02	14497
X-RAY DIFFRACTION	r_angle_refined_deg	1.301	1.96	20120
X-RAY DIFFRACTION	r_angle_other_deg	1.078	3	33308
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.132	5	1919
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	38.159	24.377	658
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.614	15	2561
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	12.767	15	96
X-RAY DIFFRACTION	r_chiral_restr	0.072	0.2	2294
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.021	17061
X-RAY DIFFRACTION	r_gen_planes_other	0.004	0.02	3331
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	1.568	9.239	7712
X-RAY DIFFRACTION	r_mcbond_other	1.568	9.239	7711
X-RAY DIFFRACTION	r_mcangle_it	2.685	13.858	9619
X-RAY DIFFRACTION	r_mcangle_other	2.685	13.858	9620
X-RAY DIFFRACTION	r_scbond_it	1.54	9.391	7163
X-RAY DIFFRACTION	r_scbond_other	1.54	9.391	7163
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	2.717	14.019	10502
X-RAY DIFFRACTION	r_long_range_B_refined	6.314	87.284	61648
X-RAY DIFFRACTION	r_long_range_B_other	6.31	87.282	61638
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	59754	0.01
1	2	B	59754	0.01
2	1	A	58918	0.05
2	2	C	58918	0.05
3	1	A	58994	0.05
3	2	D	58994	0.05
4	1	B	58970	0.05
4	2	C	58970	0.05
5	1	B	58952	0.05
5	2	D	58952	0.05
6	1	C	59778	0.02
6	2	D	59778	0.02
7	1	E	526	0.15
7	2	F	526	0.15
8	1	E	508	0.06
8	2	G	508	0.06
9	1	E	466	0.07
9	2	H	466	0.07
10	1	E	508	0.06
10	2	I	508	0.06
11	1	E	428	0.22
11	2	J	428	0.22
12	1	E	468	0.06
12	2	K	468	0.06
13	1	F	462	0.09
13	2	G	462	0.09
14	1	F	454	0.1
14	2	H	454	0.1
15	1	F	458	0.09
15	2	I	458	0.09
16	1	F	426	0.21
16	2	J	426	0.21
17	1	F	458	0.09
17	2	K	458	0.09
18	1	G	478	0.03
18	2	H	478	0.03
19	1	G	600	0.01
19	2	I	600	0.01
20	1	G	444	0.22
20	2	J	444	0.22
21	1	G	482	0
21	2	K	482	0
22	1	H	484	0.03
22	2	I	484	0.03
23	1	H	478	0.23
23	2	J	478	0.23
24	1	H	520	0.09
24	2	K	520	0.09
25	1	I	446	0.22
25	2	J	446	0.22
26	1	I	488	0
26	2	K	488	0
27	1	J	476	0.22
27	2	K	476	0.22

LS refinement shell

Resolution: 3.2→3.281 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.375	162	-
R_work	0.357	3086	-
obs	-	-	90.83 %

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	2.2346	-1.5828	5.3097	1.9585	-4.9879	14.4661	0.2547	0.2455	-0.0945	0.3106	-0.2565	-0.1024	-0.206	0.5631	0.0018	0.9429	0.1269	-0.0536	0.5267	-0.1373	0.5282	4.2513	54.0647	55.3507
2	0.4895	0.0715	1.9434	0.6431	0.6956	7.9985	-0.0297	0.1642	0.2609	0.4211	-0.6916	-0.3413	0.1132	0.1716	0.7213	0.7777	-0.2862	-0.0474	1.1372	0.2085	1.1501	70.1597	2.2119	25.1288
3	8.1026	10.4654	-1.3128	14.4663	-3.6816	4.3693	-0.2757	-0.0209	0.7347	-0.073	0.4676	0.9819	-0.5644	-1.0073	-0.1918	0.7911	0.087	0.2113	1.0991	-0.2915	1.3457	-25.5621	37.3197	20.639
4	10.0191	-5.8425	8.0274	6.2324	-4.7326	6.4465	-0.5728	-0.3357	0.1574	0.0086	0.339	-0.1574	-0.4502	-0.2604	0.2339	0.5636	-0.0556	0.0006	0.3036	0.023	0.8328	18.0471	81.8501	13.8149
5	16.7252	-7.5912	-2.1188	8.1084	-1.7964	4.7188	-0.0556	0.4943	-1.4009	-0.1226	0.2304	0.4474	-0.3367	-0.142	-0.1749	0.4906	-0.071	0.0869	0.1498	-0.2009	0.5092	25.8269	-42.1857	6.9092
6	16.7986	-0.9954	-6.8998	1.3939	-1.5283	5.7226	0.2197	-0.253	0.7907	-0.2496	0.2361	0.1617	0.3674	-0.1771	-0.4558	0.6144	-0.0143	0.0285	0.421	-0.0333	0.6176	35.3226	-20.2795	52.8114
7	5.4858	1.5571	-1.8619	5.5376	-2.3881	5.1604	-0.0568	0.011	0.4163	0.2298	0.004	-0.0489	-0.3805	0.1735	0.0528	0.6138	0.1074	-0.1188	0.4383	0.0564	0.2958	53.1085	-14.5182	67.2453
8	2.5082	-1.4949	2.6228	1.6072	-2.7086	7.6182	0.3802	0.4036	-0.2002	-0.1775	-0.1497	-0.4333	0.5126	0.7818	-0.2304	0.4108	0.0311	0.0241	0.7651	-0.0162	0.8958	60.1754	0.5193	28.8537
9	6.2924	0.8486	-1.4335	6.5709	-1.3147	6.5393	-0.1791	0.401	-0.0858	-0.2596	-0.2487	-0.1759	-0.0676	0.2737	0.4278	0.0518	-0.0173	0.0271	0.25	-0.1225	0.1502	25.2165	-0.4137	19.4352
10	5.8733	0.6394	1.1745	4.9433	-1.8187	7.2378	-0.5384	-0.067	0.543	0.2898	0.2247	-0.3652	-0.1716	0.0934	0.3138	0.399	-0.0039	-0.2714	0.0219	0.0138	0.6471	14.5856	73.0106	12.1268
11	1.872	1.5765	-1.7599	10.0823	-4.6993	4.6041	-0.1376	0.0796	0.3053	0.6545	-0.006	-0.2168	-0.8566	-0.5495	0.1436	0.4679	0.305	-0.0751	0.5732	-0.2174	0.4082	6.1621	48.9793	46.3397
12	3.552	-1.0646	-0.1037	5.8247	3.8107	8.6016	0.2385	0.114	-0.0836	-0.0575	-0.6022	0.8077	-0.4089	-0.8179	0.3637	0.0964	0.0407	0.091	0.3709	-0.2098	0.3269	3.9038	13.767	32.139
13	6.3197	3.1899	2.6977	6.7007	0.5821	4.6122	0.2018	0.2617	-0.5612	0.1803	0.1537	-0.7933	0.3868	0.3777	-0.3555	0.5519	0.3049	0.2041	0.7375	-0.3795	0.6226	-13.8926	48.7721	66.4666
14	3.1866	-2.0348	-3.354	2.1069	3.272	7.2255	0.3461	0.2534	0.4329	-0.107	-0.3243	0.3003	-0.7992	-0.4848	-0.0218	0.5596	0.256	0.0403	0.8844	-0.2469	0.6475	-16.2526	37.5163	26.5735
15	6.8958	0.1614	2.2112	5.3157	0.895	4.9026	-0.3358	0.4333	0.3201	-0.3783	0.0452	0.2376	-0.3519	-0.5145	0.2907	0.2687	0.1242	0.0674	0.2826	0.1252	0.1414	19.6096	39.4479	21.4959
16	5.9475	-0.1216	-2.7398	2.6172	0.8816	8.1645	-0.0446	0.0995	0.2187	0.0027	0.0203	-0.0923	0.2704	0.071	0.0243	0.1753	-0.0408	0.2252	0.0246	-0.086	0.4249	31.3793	-33.5394	6.5837
17	2.8648	-0.5411	1.6249	7.3143	3.5634	6.4072	-0.1171	0.1022	-0.4209	0.5988	0.2707	-0.353	0.5971	0.3152	-0.1535	0.184	0.0506	0.0836	0.2014	0.0765	0.2053	36.0831	-12.9225	44.0654
18	4.0515	0.4732	-1.2417	4.0277	-1.9002	7.044	0.0475	-0.0305	-0.0043	0.2782	-0.201	-0.39	-0.1616	0.2485	0.1536	0.0468	-0.0198	0.0144	0.0285	0.026	0.116	39.5786	23.8549	34.7166
19	4.6779	5.0533	2.5302	7.0084	0.7416	3.9352	1.0747	-0.7447	-0.0642	1.5717	-1.2233	-0.2091	0.0403	0.0721	0.1487	0.9534	-0.0315	-0.2181	0.9036	0.0355	0.4743	59.6601	-14.2079	74.7875
20	2.992	6.1993	-1.6863	27.7142	-11.6401	8.3754	0.4369	-0.1973	-0.3365	0.8465	-0.0754	-0.0705	-0.1841	-0.1497	-0.3615	0.4761	0.1304	0.158	0.608	-0.1623	0.3557	-21.6105	49.4226	72.1718

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	H	4 - 13
2	X-RAY DIFFRACTION	2	L	4 - 12
3	X-RAY DIFFRACTION	3	J	4 - 13
4	X-RAY DIFFRACTION	4	G	4 - 14
5	X-RAY DIFFRACTION	5	E	3 - 14
6	X-RAY DIFFRACTION	6	F	3 - 13
7	X-RAY DIFFRACTION	7	D	180 - 332
8	X-RAY DIFFRACTION	8	D	333 - 489
9	X-RAY DIFFRACTION	9	D	490 - 642
10	X-RAY DIFFRACTION	10	B	182 - 332
11	X-RAY DIFFRACTION	11	B	333 - 489
12	X-RAY DIFFRACTION	12	B	490 - 642
13	X-RAY DIFFRACTION	13	C	182 - 332
14	X-RAY DIFFRACTION	14	C	333 - 489
15	X-RAY DIFFRACTION	15	C	490 - 642
16	X-RAY DIFFRACTION	16	A	181 - 332
17	X-RAY DIFFRACTION	17	A	333 - 489
18	X-RAY DIFFRACTION	18	A	490 - 642
19	X-RAY DIFFRACTION	19	K	4 - 13
20	X-RAY DIFFRACTION	20	I	4 - 14

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