PDB-3qa8: Crystal Structure of inhibitor of kappa B kinase beta

ID or keywords:

Entry

Database: PDB / ID: 3qa8

Title

Crystal Structure of inhibitor of kappa B kinase beta

Components

MGC80376 protein

Keywords

IMMUNE SYSTEM /

SIGNALING PROTEIN / kinase ubiquitin-like domain /

phosphorylation /

kinase domain /

ubiquitin-like domain /

kinase / substrate binding

Function / homology

Function and homology information

IkappaB kinase /

IkappaB kinase activity /

ATP binding / identical protein binding /

nucleus /

cytoplasm
Similarity search - Function

Biological species

Xenopus laevis (African clawed frog)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.6 Å

Authors

Xu, G. / Lo, Y.C. / Li, Q. / Napolitano, G. / Wu, X. / Jiang, X. / Dreano, M. / Karin, M. / Wu, H.

Citation

Journal: Nature / Year: 2011
Title: Crystal structure of inhibitor of kappa B kinase beta.
Authors: Xu, G. / Lo, Y.C. / Li, Q. / Napolitano, G. / Wu, X. / Jiang, X. / Dreano, M. / Karin, M. / Wu, H.

History

Deposition	Jan 10, 2011	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 6, 2011	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Version format compliance
Revision 1.2	Jul 26, 2023	Group: Database references / Category: citation / database_2 / struct_ref_seq_dif Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.3	May 22, 2024	Group: Data collection / Category: chem_comp_atom / chem_comp_bond

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	3qa8.cif.gz	2 MB	Display	PDBx/mmCIF format
PDB format	pdb3qa8.ent.gz	1.7 MB	Display	PDB format
PDBx/mmJSON format	3qa8.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qa/3qa8 ftp://data.pdbj.org/pub/pdb/validation_reports/qa/3qa8	HTTPS FTP

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Related structure data

Related structure data	3rzfC C: citing same article (ref.)
Similar structure data	7nd9-d 7ndb-d 3fwc-d 5hxb-d 5xeb-d 3hhd-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) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: MGC80376 protein

B: MGC80376 protein

C: MGC80376 protein

D: MGC80376 protein

E: MGC80376 protein

F: MGC80376 protein

G: MGC80376 protein

H: MGC80376 protein

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

1

A: MGC80376 protein

B: MGC80376 protein

C: MGC80376 protein

D: MGC80376 protein

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

2

E: MGC80376 protein

F: MGC80376 protein

G: MGC80376 protein

H: MGC80376 protein

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

Unit cell

Length a, b, c (Å)	103.170, 140.339, 161.167
Angle α, β, γ (deg.)	71.28, 79.56, 86.04
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Selection details
1	1	1	CHAIN A AND (RESSEQ 16:100 )
2	1	1	CHAIN B AND (RESSEQ 16:100 )
3	1	1	CHAIN C AND (RESSEQ 16:100 )
4	1	1	CHAIN D AND (RESSEQ 16:100 )
5	1	1	CHAIN E AND (RESSEQ 16:100 )
6	1	1	CHAIN F AND (RESSEQ 16:100 )
7	1	1	CHAIN G AND (RESSEQ 16:100 )
8	1	1	CHAIN H AND (RESSEQ 16:100 )
1	1	2	CHAIN A AND (RESSEQ 101:199 )
2	1	2	CHAIN B AND (RESSEQ 101:199 )
3	1	2	CHAIN C AND (RESSEQ 101:199 )
4	1	2	CHAIN D AND (RESSEQ 101:199 )
5	1	2	CHAIN E AND (RESSEQ 101:199 )
6	1	2	CHAIN F AND (RESSEQ 101:199 )
7	1	2	CHAIN G AND (RESSEQ 101:199 )
8	1	2	CHAIN H AND (RESSEQ 101:199 )
1	1	3	CHAIN A AND (RESSEQ 200:236 OR RESSEQ 243:286 OR RESSEQ 290:309 )
2	1	3	CHAIN B AND (RESSEQ 200:236 OR RESSEQ 243:286 OR RESSEQ 290:309 )
3	1	3	CHAIN C AND (RESSEQ 200:236 OR RESSEQ 243:286 OR RESSEQ 290:309 )
4	1	3	CHAIN D AND (RESSEQ 200:236 OR RESSEQ 243:286 OR RESSEQ 290:309 )
5	1	3	CHAIN E AND (RESSEQ 200:236 OR RESSEQ 243:286 OR RESSEQ 290:309 )
6	1	3	CHAIN F AND (RESSEQ 200:236 OR RESSEQ 243:286 OR RESSEQ 290:309 )
7	1	3	CHAIN G AND (RESSEQ 200:236 OR RESSEQ 243:286 OR RESSEQ 290:309 )
8	1	3	CHAIN H AND (RESSEQ 200:236 OR RESSEQ 243:286 OR RESSEQ 290:309 )
1	1	4	CHAIN A AND (RESSEQ 310:376 OR RESSEQ 384:394 )
2	1	4	CHAIN B AND (RESSEQ 310:376 OR RESSEQ 384:394 )
3	1	4	CHAIN C AND (RESSEQ 310:376 OR RESSEQ 384:394 )
4	1	4	CHAIN D AND (RESSEQ 310:376 OR RESSEQ 384:394 )
5	1	4	CHAIN E AND (RESSEQ 310:376 OR RESSEQ 384:394 )
6	1	4	CHAIN F AND (RESSEQ 310:376 OR RESSEQ 384:394 )
7	1	4	CHAIN G AND (RESSEQ 310:376 OR RESSEQ 384:394 )
8	1	4	CHAIN H AND (RESSEQ 310:376 OR RESSEQ 384:394 )
1	1	5	CHAIN A AND (RESSEQ 401:445 )
2	1	5	CHAIN B AND (RESSEQ 401:445 )
3	1	5	CHAIN C AND (RESSEQ 401:445 )
4	1	5	CHAIN D AND (RESSEQ 401:445 )
5	1	5	CHAIN E AND (RESSEQ 401:445 )
6	1	5	CHAIN F AND (RESSEQ 401:445 )
7	1	5	CHAIN G AND (RESSEQ 401:445 )
8	1	5	CHAIN H AND (RESSEQ 401:445 )
1	1	6	CHAIN A AND (RESSEQ 446:475 )
2	1	6	CHAIN B AND (RESSEQ 446:475 )
3	1	6	CHAIN C AND (RESSEQ 446:475 )
4	1	6	CHAIN D AND (RESSEQ 446:475 )
5	1	6	CHAIN E AND (RESSEQ 446:475 )
6	1	6	CHAIN F AND (RESSEQ 446:475 )
7	1	6	CHAIN G AND (RESSEQ 446:475 )
8	1	6	CHAIN H AND (RESSEQ 446:475 )
1	1	7	CHAIN A AND (RESSEQ 476:502 )
2	1	7	CHAIN B AND (RESSEQ 476:502 )
3	1	7	CHAIN C AND (RESSEQ 476:502 )
4	1	7	CHAIN D AND (RESSEQ 476:502 )
5	1	7	CHAIN E AND (RESSEQ 476:502 )
6	1	7	CHAIN F AND (RESSEQ 476:502 )
1	1	8	CHAIN A AND (RESSEQ 505:523 )
2	1	8	CHAIN B AND (RESSEQ 505:523 )
3	1	8	CHAIN C AND (RESSEQ 505:523 )
4	1	8	CHAIN D AND (RESSEQ 505:523 )
5	1	8	CHAIN E AND (RESSEQ 505:523 )
6	1	8	CHAIN F AND (RESSEQ 505:523 )
1	1	9	CHAIN A AND (RESSEQ 528:551 )
2	1	9	CHAIN B AND (RESSEQ 528:551 )
3	1	9	CHAIN C AND (RESSEQ 528:551 )
4	1	9	CHAIN D AND (RESSEQ 528:551 )
5	1	9	CHAIN E AND (RESSEQ 528:551 )
6	1	9	CHAIN F AND (RESSEQ 528:551 )
7	1	9	CHAIN G AND (RESSEQ 528:551 )
8	1	9	CHAIN H AND (RESSEQ 528:551 )
1	1	10	CHAIN A AND (RESSEQ 559:585 )
2	1	10	CHAIN B AND (RESSEQ 559:585 )
3	1	10	CHAIN C AND (RESSEQ 559:585 )
4	1	10	CHAIN D AND (RESSEQ 559:585 )
5	1	10	CHAIN E AND (RESSEQ 559:585 )
6	1	10	CHAIN F AND (RESSEQ 559:585 )
7	1	10	CHAIN G AND (RESSEQ 559:585 )
8	1	10	CHAIN H AND (RESSEQ 559:585 )
1	1	11	CHAIN A AND (RESSEQ 586:610 )
2	1	11	CHAIN B AND (RESSEQ 586:610 )
3	1	11	CHAIN C AND (RESSEQ 586:610 )
4	1	11	CHAIN D AND (RESSEQ 586:610 )
5	1	11	CHAIN E AND (RESSEQ 586:610 )
6	1	11	CHAIN F AND (RESSEQ 586:610 )
7	1	11	CHAIN G AND (RESSEQ 586:610 )
8	1	11	CHAIN H AND (RESSEQ 586:610 )
1	1	12	CHAIN A AND (RESSEQ 611:637 )
2	1	12	CHAIN B AND (RESSEQ 611:637 )
3	1	12	CHAIN C AND (RESSEQ 611:637 )
4	1	12	CHAIN D AND (RESSEQ 611:637 )
5	1	12	CHAIN E AND (RESSEQ 611:637 )
6	1	12	CHAIN F AND (RESSEQ 611:637 )
7	1	12	CHAIN G AND (RESSEQ 611:637 )
8	1	12	CHAIN H AND (RESSEQ 611:637 )
1	1	13	CHAIN A AND (RESSEQ 638:650 )
2	1	13	CHAIN B AND (RESSEQ 638:650 )
3	1	13	CHAIN C AND (RESSEQ 638:650 )
4	1	13	CHAIN D AND (RESSEQ 638:650 )
5	1	13	CHAIN E AND (RESSEQ 638:650 )
6	1	13	CHAIN F AND (RESSEQ 638:650 )
1	1	14	CHAIN A AND (RESSEQ 651:666 )
2	1	14	CHAIN B AND (RESSEQ 651:666 )
3	1	14	CHAIN C AND (RESSEQ 651:666 )
4	1	14	CHAIN D AND (RESSEQ 651:666 )
5	1	14	CHAIN E AND (RESSEQ 651:666 )
6	1	14	CHAIN F AND (RESSEQ 651:666 )

NCS ensembles :

ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14

#1: Protein	MGC80376 protein Mass: 77873.383 Da / Num. of mol.: 8 / Mutation: S177E, S181E / Source method: isolated from a natural source / Source: (natural) Xenopus laevis (African clawed frog) / References: UniProt: Q6INT1

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.49 Å³/Da / Density % sol: 64.74 %
Crystal grow	Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 100mM N-(2-acetamido) iminodiacetic acid, 10%(w/v) polyethylene glycol (PEG)6000, 50mM Li2SO4, 300mM NaCl, 10mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

Diffraction	Mean temperature: 298 K
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97922 Å
Detector	Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 8, 2009
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97922 Å / Relative weight: 1
Reflection	Resolution: 3.6→50 Å / Num. all: 90090 / Num. obs: 75637 / % possible obs: 92.5 % / Observed criterion σ(F): 1.2 / Observed criterion σ(I): 1.2 / Redundancy: 1.9 % / R_merge(I) obs: 0.072 / R_sym value: 0.042 / Net I/σ(I): 9.2
Reflection shell	Resolution: 3.6→3.66 Å / Redundancy: 1.8 % / R_merge(I) obs: 0.432 / Mean I/σ(I) obs: 1.2 / R_sym value: 0.261 / % possible all: 76.6

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Processing

Software

Name	Version	Classification
HKL-2000		data collection
PHASES		phasing
PHENIX	(phenix.refine: 1.6.4_486)	refinement
HKL-2000		data reduction
HKL-2000		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 3.6→14.999 Å / SU ML: 0.56 / σ(F): 0.14 / Phase error: 44.59 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.3435	3825	5.06 %
R_work	0.3078	-	-
obs	0.3097	75637	78.65 %
all	-	90090	-

Solvent computation

Shrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / B_sol: 38.189 Å² / k_sol: 0.177 e/Å³

Displacement parameters

	B_aniso -1	B_aniso -2	B_aniso -3
1-	6.972 Å²	29.7379 Å²	-40.3815 Å²
2-	-	-47.6786 Å²	-4.9605 Å²
3-	-	-	26.1452 Å²

Refinement step

Cycle: LAST / Resolution: 3.6→14.999 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	39026	0	0	0	39026

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.054	40855
X-RAY DIFFRACTION	f_angle_d	2.086	53610
X-RAY DIFFRACTION	f_dihedral_angle_d	20.142	15396
X-RAY DIFFRACTION	f_chiral_restr	0.139	6004
X-RAY DIFFRACTION	f_plane_restr	0.006	6898

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Type	Rms dev position (Å)
1	1	A	683	X-RAY DIFFRACTION	POSITIONAL
1	2	B	683	X-RAY DIFFRACTION	POSITIONAL	0.012
1	3	C	683	X-RAY DIFFRACTION	POSITIONAL	0.012
1	4	D	683	X-RAY DIFFRACTION	POSITIONAL	0.011
1	5	E	683	X-RAY DIFFRACTION	POSITIONAL	0.013
1	6	F	683	X-RAY DIFFRACTION	POSITIONAL	0.012
1	7	G	683	X-RAY DIFFRACTION	POSITIONAL	0.011
1	8	H	683	X-RAY DIFFRACTION	POSITIONAL	0.012
2	1	A	801	X-RAY DIFFRACTION	POSITIONAL
2	2	B	801	X-RAY DIFFRACTION	POSITIONAL	0.019
2	3	C	801	X-RAY DIFFRACTION	POSITIONAL	0.02
2	4	D	801	X-RAY DIFFRACTION	POSITIONAL	0.019
2	5	E	801	X-RAY DIFFRACTION	POSITIONAL	0.021
2	6	F	801	X-RAY DIFFRACTION	POSITIONAL	0.02
2	7	G	801	X-RAY DIFFRACTION	POSITIONAL	0.019
2	8	H	801	X-RAY DIFFRACTION	POSITIONAL	0.02
3	1	A	809	X-RAY DIFFRACTION	POSITIONAL
3	2	B	809	X-RAY DIFFRACTION	POSITIONAL	0.023
3	3	C	809	X-RAY DIFFRACTION	POSITIONAL	0.027
3	4	D	809	X-RAY DIFFRACTION	POSITIONAL	0.022
3	5	E	809	X-RAY DIFFRACTION	POSITIONAL	0.028
3	6	F	809	X-RAY DIFFRACTION	POSITIONAL	0.024
3	7	G	809	X-RAY DIFFRACTION	POSITIONAL	0.021
3	8	H	809	X-RAY DIFFRACTION	POSITIONAL	0.025
4	1	A	617	X-RAY DIFFRACTION	POSITIONAL
4	2	B	617	X-RAY DIFFRACTION	POSITIONAL	0.021
4	3	C	617	X-RAY DIFFRACTION	POSITIONAL	0.021
4	4	D	617	X-RAY DIFFRACTION	POSITIONAL	0.021
4	5	E	617	X-RAY DIFFRACTION	POSITIONAL	0.022
4	6	F	617	X-RAY DIFFRACTION	POSITIONAL	0.022
4	7	G	617	X-RAY DIFFRACTION	POSITIONAL	0.02
4	8	H	617	X-RAY DIFFRACTION	POSITIONAL	0.022
5	1	A	368	X-RAY DIFFRACTION	POSITIONAL
5	2	B	368	X-RAY DIFFRACTION	POSITIONAL	0.024
5	3	C	368	X-RAY DIFFRACTION	POSITIONAL	0.024
5	4	D	368	X-RAY DIFFRACTION	POSITIONAL	0.022
5	5	E	368	X-RAY DIFFRACTION	POSITIONAL	0.023
5	6	F	368	X-RAY DIFFRACTION	POSITIONAL	0.024
5	7	G	368	X-RAY DIFFRACTION	POSITIONAL	0.023
5	8	H	368	X-RAY DIFFRACTION	POSITIONAL	0.025
6	1	A	244	X-RAY DIFFRACTION	POSITIONAL
6	2	B	244	X-RAY DIFFRACTION	POSITIONAL	0.026
6	3	C	244	X-RAY DIFFRACTION	POSITIONAL	0.024
6	4	D	244	X-RAY DIFFRACTION	POSITIONAL	0.023
6	5	E	244	X-RAY DIFFRACTION	POSITIONAL	0.021
6	6	F	244	X-RAY DIFFRACTION	POSITIONAL	0.025
6	7	G	244	X-RAY DIFFRACTION	POSITIONAL	0.024
6	8	H	244	X-RAY DIFFRACTION	POSITIONAL	0.022
7	1	A	228	X-RAY DIFFRACTION	POSITIONAL
7	2	B	228	X-RAY DIFFRACTION	POSITIONAL	0.029
7	3	C	228	X-RAY DIFFRACTION	POSITIONAL	0.027
7	4	D	228	X-RAY DIFFRACTION	POSITIONAL	0.023
7	5	E	228	X-RAY DIFFRACTION	POSITIONAL	0.026
7	6	F	228	X-RAY DIFFRACTION	POSITIONAL	0.025
8	1	A	155	X-RAY DIFFRACTION	POSITIONAL
8	2	B	155	X-RAY DIFFRACTION	POSITIONAL	0.023
8	3	C	155	X-RAY DIFFRACTION	POSITIONAL	0.022
8	4	D	155	X-RAY DIFFRACTION	POSITIONAL	0.022
8	5	E	155	X-RAY DIFFRACTION	POSITIONAL	0.021
8	6	F	155	X-RAY DIFFRACTION	POSITIONAL	0.021
9	1	A	190	X-RAY DIFFRACTION	POSITIONAL
9	2	B	190	X-RAY DIFFRACTION	POSITIONAL	0.016
9	3	C	190	X-RAY DIFFRACTION	POSITIONAL	0.016
9	4	D	190	X-RAY DIFFRACTION	POSITIONAL	0.015
9	5	E	190	X-RAY DIFFRACTION	POSITIONAL	0.015
9	6	F	190	X-RAY DIFFRACTION	POSITIONAL	0.016
9	7	G	190	X-RAY DIFFRACTION	POSITIONAL	0.015
9	8	H	190	X-RAY DIFFRACTION	POSITIONAL	0.016
10	1	A	235	X-RAY DIFFRACTION	POSITIONAL
10	2	B	235	X-RAY DIFFRACTION	POSITIONAL	0.02
10	3	C	235	X-RAY DIFFRACTION	POSITIONAL	0.02
10	4	D	235	X-RAY DIFFRACTION	POSITIONAL	0.019
10	5	E	235	X-RAY DIFFRACTION	POSITIONAL	0.018
10	6	F	235	X-RAY DIFFRACTION	POSITIONAL	0.019
10	7	G	235	X-RAY DIFFRACTION	POSITIONAL	0.019
10	8	H	235	X-RAY DIFFRACTION	POSITIONAL	0.02
11	1	A	207	X-RAY DIFFRACTION	POSITIONAL
11	2	B	207	X-RAY DIFFRACTION	POSITIONAL	0.024
11	3	C	207	X-RAY DIFFRACTION	POSITIONAL	0.027
11	4	D	207	X-RAY DIFFRACTION	POSITIONAL	0.022
11	5	E	207	X-RAY DIFFRACTION	POSITIONAL	0.024
11	6	F	207	X-RAY DIFFRACTION	POSITIONAL	0.025
11	7	G	207	X-RAY DIFFRACTION	POSITIONAL	0.021
11	8	H	207	X-RAY DIFFRACTION	POSITIONAL	0.023
12	1	A	215	X-RAY DIFFRACTION	POSITIONAL
12	2	B	215	X-RAY DIFFRACTION	POSITIONAL	0.027
12	3	C	215	X-RAY DIFFRACTION	POSITIONAL	0.024
12	4	D	215	X-RAY DIFFRACTION	POSITIONAL	0.021
12	5	E	215	X-RAY DIFFRACTION	POSITIONAL	0.02
12	6	F	215	X-RAY DIFFRACTION	POSITIONAL	0.023
12	7	G	215	X-RAY DIFFRACTION	POSITIONAL	0.022
12	8	H	215	X-RAY DIFFRACTION	POSITIONAL	0.027
13	1	A	117	X-RAY DIFFRACTION	POSITIONAL
13	2	B	117	X-RAY DIFFRACTION	POSITIONAL	0.027
13	3	C	117	X-RAY DIFFRACTION	POSITIONAL	0.02
13	4	D	117	X-RAY DIFFRACTION	POSITIONAL	0.024
13	5	E	117	X-RAY DIFFRACTION	POSITIONAL	0.02
13	6	F	117	X-RAY DIFFRACTION	POSITIONAL	0.027
14	1	A	134	X-RAY DIFFRACTION	POSITIONAL
14	2	B	134	X-RAY DIFFRACTION	POSITIONAL	0.027
14	3	C	134	X-RAY DIFFRACTION	POSITIONAL	0.024
14	4	D	134	X-RAY DIFFRACTION	POSITIONAL	0.022
14	5	E	134	X-RAY DIFFRACTION	POSITIONAL	0.025
14	6	F	134	X-RAY DIFFRACTION	POSITIONAL	0.023

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 (%)
3.6-3.645	0.4917	93	0.4447	1834	X-RAY DIFFRACTION	55
3.645-3.6922	0.4648	98	0.4547	1980	X-RAY DIFFRACTION	58
3.6922-3.7421	0.496	103	0.4377	1934	X-RAY DIFFRACTION	57
3.7421-3.7947	0.4586	92	0.4241	2023	X-RAY DIFFRACTION	59
3.7947-3.8504	0.4733	110	0.4222	2021	X-RAY DIFFRACTION	60
3.8504-3.9095	0.434	111	0.4064	2142	X-RAY DIFFRACTION	63
3.9095-3.9724	0.3954	105	0.3968	2179	X-RAY DIFFRACTION	64
3.9724-4.0396	0.4425	114	0.375	2264	X-RAY DIFFRACTION	68
4.0396-4.1116	0.394	135	0.363	2363	X-RAY DIFFRACTION	70
4.1116-4.189	0.38	127	0.369	2418	X-RAY DIFFRACTION	72
4.189-4.2726	0.3522	128	0.3502	2608	X-RAY DIFFRACTION	76
4.2726-4.3632	0.3896	151	0.3341	2684	X-RAY DIFFRACTION	80
4.3632-4.4621	0.3806	144	0.337	2774	X-RAY DIFFRACTION	81
4.4621-4.5706	0.3466	144	0.3242	2715	X-RAY DIFFRACTION	81
4.5706-4.6905	0.4082	152	0.3155	2880	X-RAY DIFFRACTION	84
4.6905-4.8241	0.3435	143	0.2998	2885	X-RAY DIFFRACTION	86
4.8241-4.9743	0.3245	155	0.2938	2897	X-RAY DIFFRACTION	86
4.9743-5.1452	0.3014	149	0.2938	2973	X-RAY DIFFRACTION	87
5.1452-5.3422	0.3628	171	0.3433	2989	X-RAY DIFFRACTION	89
5.3422-5.5734	0.4012	161	0.3389	3039	X-RAY DIFFRACTION	90
5.5734-5.8507	0.3546	158	0.3339	3108	X-RAY DIFFRACTION	92
5.8507-6.1928	0.3502	199	0.3449	3102	X-RAY DIFFRACTION	93
6.1928-6.6324	0.3743	193	0.3227	3139	X-RAY DIFFRACTION	94
6.6324-7.231	0.3493	165	0.2943	3193	X-RAY DIFFRACTION	95
7.231-8.1284	0.3339	163	0.2769	3113	X-RAY DIFFRACTION	92
8.1284-9.7492	0.2761	164	0.2365	3330	X-RAY DIFFRACTION	98
9.7492-14.9987	0.2416	197	0.2038	3225	X-RAY DIFFRACTION	96

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	0.1794	0.0146	-0.1698	0.2186	0.2025	0.3494	0.8069	0.509	-0.4735	-0.8492	-1.3789	-0.2634	0.7851	0.4106	0	1.3245	0.038	0.1725	1.0568	-0.0392	1.3708	-21.9516	-26.9758	42.0749
2	2.3969	-0.9748	-0.6522	2.5102	1.0577	0.9796	-0.6528	-0.3902	0.1202	1.1891	-0.0446	-0.504	0.4279	0.0739	-0.0331	0.79	0.1992	0.002	0.645	-0.2597	0.2475	-1.6239	-10.6023	40.0871
3	1.571	0.178	0.212	0.9939	0.7965	0.7635	-0.5301	-0.2704	1.8164	0.4864	1.4551	0.041	0.3877	0.2283	0.0091	1.1863	0.2242	-0.4148	0.6977	-0.1008	1.3045	-7.4941	22.9058	29.6038
4	2.06	-2.1086	0.5305	1.7429	-0.3972	0.2268	-0.2124	-0.1661	0.3142	0.3276	0.2853	0.3435	0.3451	0.0731	0.0376	-0.0983	-0.4949	-0.0029	0.5479	0.0276	0.8227	-15.6077	31.8581	5.6014
5	0.1661	-0.2614	0.25	0.3474	-0.3336	0.3204	-0.1401	0.1485	0.7402	1.2061	-0.8864	-0.7394	-0.092	0.6177	-0.0106	0.8963	0.0583	0.392	1.0959	0.1158	1.9859	13.691	-20.4099	-21.4327
6	2.4611	0.4334	-2.8803	1.2423	-1.0183	2.8066	0.0165	0.2625	-0.0355	-0.3992	-0.5305	-0.2342	0.1158	0.4918	0.0093	0.1992	-0.1817	0.134	0.4704	0.2718	0.5658	-12.3754	-21.9555	-20.4863
7	0.997	0.7052	-0.2213	1.8004	1.0641	1.1114	1.519	-0.0928	0.8658	-1.0224	-0.2041	-0.0129	0.3958	0.2232	0.0089	1.2189	-0.02	-0.4104	0.5506	0.3663	1.3802	-32.465	6.6669	-15.889
8	0.1951	0.2395	-0.5462	2.1263	-0.6579	0.2595	0.2263	0.0099	0.8549	0.0071	-0.3755	-0.4622	-0.2046	0.0651	-0.0056	-0.0095	-0.38	-0.1814	0.5018	-0.0542	1.2239	-37.1192	21.9682	0.9339
9	0.8923	0.2615	0.301	0.628	0.0653	0.0946	-0.1574	-0.4496	0.0176	1.9912	0.1742	0.681	-0.1207	0.1314	0	2.1278	0.4089	0.2304	1.605	-0.3654	0.9061	-29.3789	-50.9466	23.5542
10	0.5739	0.2439	-0.92	2.6594	-0.3168	2.8674	0.122	-0.1069	0.6243	0.3879	-0.2799	0.4577	-0.4954	-0.0219	-0.0408	-0.5942	-0.2244	0.9536	0.4728	0.0928	-0.5086	-21.0676	-59.0312	0.1701
11	2.4946	-0.5814	0.6314	1.6976	1.3091	2.8649	-1.2261	-0.5815	-0.1969	0.2201	0.9803	0.3026	0.3892	0.5214	-0.0882	0.1759	0.0304	-0.1992	0.3475	0.0208	0.7464	-2.4647	-88.9833	-2.8958
12	0.8157	-0.9687	0.5259	3.3156	-2.1597	0.1137	-0.0462	-0.0965	0.136	0.8032	-0.0753	-0.4189	1.0049	0.0111	-0.0633	-0.2983	-0.1336	-0.0564	0.7721	-0.1708	0.2901	23.2312	-94.14	5.4651
13	0.0904	-0.1329	0.1269	0.1945	-0.1635	0.1765	0.4718	0.4679	0.4164	-1.6109	-0.2244	0.1338	-0.9837	0.5641	0	2.2166	0.1984	0.1246	1.7959	0.1995	1.8348	38.7316	-26.5277	4.9149
14	2.1973	0.5862	-1.535	2.0892	-1.0163	0.9561	-0.7649	0.0586	0.7486	1.1409	0.5864	-1.3017	0.136	0.6556	-0.0078	0.8483	0.4217	-0.0676	0.8519	-0.2093	0.8909	31.9469	-35.1999	28.517
15	0.4484	0.333	-0.0051	2.5723	-0.4895	1.3923	-1.0354	-0.6903	-0.4249	0.202	0.4518	-1.9142	1.2395	0.0479	-0.0638	1.7715	0.9238	0.0632	1.141	-0.0967	0.5297	36.2029	-69.4096	37.0422
16	0.4569	-0.6721	-0.2469	1.85	0.9187	-0.3358	0.189	0.0709	0.1117	0.383	-0.323	-0.3715	-0.0242	-0.1871	0.0062	1.3832	0.1669	-0.0481	0.8996	-0.0503	0.5475	24.4388	-90.7306	29.5994
17	0.5866	-0.4144	-0.404	0.2489	0.2644	0.8272	0.4579	0.8608	-1.0996	-1.0501	-1.0651	0.4235	0.1165	0.173	-0	1.8855	0.0689	-0.4015	1.2973	-0.6253	1.5226	-24.9049	-102.4144	-45.4156
18	4.6535	1.2449	1.0466	2.7594	1.03	0.2672	0.0649	0.6734	0.4244	-0.2226	-0.0202	-0.6073	0.6885	0.3746	-0.0904	0.4203	-0.0184	-0.0474	0.0808	-0.1684	0.0163	-17.3063	-83.6878	-28.7526
19	0.7943	-0.3799	0.4852	2.2074	0.0279	1.7129	0.0274	0.4477	0.4499	-0.9591	0.102	1.5236	-0.228	0.1977	-0.0337	0.427	-0.1038	0.019	0.3819	0.2099	0.4167	-35.4112	-53.377	-25.9434
20	3.777	-1.6386	2.0163	1.3238	-1.5319	1.2589	0.0116	0.7499	0.5917	0.0224	-0.4678	0.0117	-0.3069	-0.3198	-0.0406	0.6384	-0.2238	-0.2066	0.4139	0.0075	0.1402	-38.1162	-33.2453	-44.1291
21	0.0034	0.0467	-0.0517	0.2389	-0.2492	0.241	-0.7881	-0.0747	1.5818	0.4827	0.4054	-0.9802	0.3307	0.2577	-0	2.0005	0.5128	-0.5295	2.4131	-0.5982	3.6924	20.3223	-48.9339	-70.3476
22	2.731	-2.5814	-0.4078	2.4965	0.5384	0.0449	0.2094	0.9238	0.6287	-0.4896	-0.8877	-0.753	-0.8953	0.5815	-0.0091	1.6657	0.5191	0.0324	1.2508	-0.0801	1.0347	0.5111	-58.7568	-84.4798
23	1.4766	0.0151	-0.4325	1.2214	-0.1156	1.0641	0.0672	-0.0034	1.5396	-0.4088	-0.4081	0.3697	0.159	-0.7957	-0.0043	1.3396	0.6477	-0.1979	1.0338	-0.5715	0.9785	-32.2127	-44.7719	-81.7881
24	0.675	-0.2462	-0.6026	1.3504	0.9781	0.3868	-0.6198	-0.1861	0.4658	0.6618	0.043	-0.158	0.0637	-0.2235	-0.0006	1.0869	0.509	-0.3397	1.1178	-0.3429	0.2814	-47.9569	-42.7418	-64.3174
25	0.1352	0.0402	-0.1286	0.0066	-0.0194	0.0776	0.4369	0.8574	-0.8638	0.5451	-0.3482	1.1093	1.2986	1.2434	-0	1.7009	0.9581	0.2149	1.7327	0.1256	1.9888	-10.4442	-112.2168	-71.7401
26	1.3087	-0.0229	-1.0716	1.225	0.8481	1.1056	0.1342	0.0261	-0.0409	-0.0039	-0.4492	0.3114	0.4102	0.4126	-0.0002	1.1954	0.7536	0.0057	1.1749	-0.1069	0.4956	8.4172	-101.3287	-86.1747
27	0.522	-0.0933	-0.6166	0.1619	0.1208	0.7209	1.5514	-0.772	-0.5495	-1.6034	-1.1748	-1.1943	0.4829	2.1349	-0	2.0926	1.3998	0.1477	3.051	-0.0935	1.6952	41.1704	-115.6515	-86.309
28	0.9729	0.0132	0.748	1.211	-0.4259	0.5277	0.4078	-0.1449	-1.0872	0.5105	0.3122	-0.4667	0.6488	0.4272	0	1.2596	0.5856	-0.3676	1.6693	-0.5136	1.5696	43.6692	-103.5062	-70.2692
29	0.2565	-0.2874	0.1541	0.2884	-0.2108	0.3396	-0.9199	0.7603	0.391	0.1076	-0.4183	-1.5954	0.0109	1.0176	0	1.1949	-0.02	0.4628	0.9959	0.4512	2.315	33.4712	-64.9782	-42.7792
30	2.1308	1.4833	1.2774	2.1413	0.8059	0.4345	-0.1124	0.2944	0.2991	-0.2027	-0.2638	-0.45	-0.0176	0.4177	-0.0014	0.3208	0.0675	0.2467	0.5394	0.1338	0.8258	25.9415	-86.4749	-30.0646
31	0.6286	0.6964	0.3692	0.7447	0.5848	2.184	0.707	-0.3618	-0.9826	0.6673	0.3601	-1.7906	1.5378	-0.2743	0.0119	0.967	0.6481	-0.5558	1.0447	-0.2706	1.666	42.8623	-117.3276	-34.2818
32	2.7249	1.0341	-0.1176	1.4106	1.2987	1.4319	0.3861	0.6228	-1.1375	-0.4356	0.1037	-1.0259	-0.2953	0.1287	0	0.6801	0.1553	-0.3007	0.7635	-0.2186	1.6369	29.9263	-119.841	-49.3175

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	CHAIN A AND (RESSEQ 16:99)
2	X-RAY DIFFRACTION	2	CHAIN A AND (RESSEQ 100:309)
3	X-RAY DIFFRACTION	3	CHAIN A AND (RESSEQ 310:394)
4	X-RAY DIFFRACTION	4	CHAIN A AND (RESSEQ 401:666)
5	X-RAY DIFFRACTION	5	CHAIN B AND (RESSEQ 16:99)
6	X-RAY DIFFRACTION	6	CHAIN B AND (RESSEQ 100:309)
7	X-RAY DIFFRACTION	7	CHAIN B AND (RESSEQ 310:394)
8	X-RAY DIFFRACTION	8	CHAIN B AND (RESSEQ 401:666)
9	X-RAY DIFFRACTION	9	CHAIN C AND (RESSEQ 16:99)
10	X-RAY DIFFRACTION	10	CHAIN C AND (RESSEQ 100:309)
11	X-RAY DIFFRACTION	11	CHAIN C AND (RESSEQ 310:394)
12	X-RAY DIFFRACTION	12	CHAIN C AND (RESSEQ 401:666)
13	X-RAY DIFFRACTION	13	CHAIN D AND (RESSEQ 16:99)
14	X-RAY DIFFRACTION	14	CHAIN D AND (RESSEQ 100:309)
15	X-RAY DIFFRACTION	15	CHAIN D AND (RESSEQ 310:394)
16	X-RAY DIFFRACTION	16	CHAIN D AND (RESSEQ 401:666)
17	X-RAY DIFFRACTION	17	CHAIN E AND (RESSEQ 16:99)
18	X-RAY DIFFRACTION	18	CHAIN E AND (RESSEQ 100:309)
19	X-RAY DIFFRACTION	19	CHAIN E AND (RESSEQ 310:394)
20	X-RAY DIFFRACTION	20	CHAIN E AND (RESSEQ 401:666)
21	X-RAY DIFFRACTION	21	CHAIN F AND (RESSEQ 16:99)
22	X-RAY DIFFRACTION	22	CHAIN F AND (RESSEQ 100:309)
23	X-RAY DIFFRACTION	23	CHAIN F AND (RESSEQ 310:394)
24	X-RAY DIFFRACTION	24	CHAIN F AND (RESSEQ 401:666)
25	X-RAY DIFFRACTION	25	CHAIN G AND (RESSEQ 16:99)
26	X-RAY DIFFRACTION	26	CHAIN G AND (RESSEQ 100:309)
27	X-RAY DIFFRACTION	27	CHAIN G AND (RESSEQ 310:394)
28	X-RAY DIFFRACTION	28	CHAIN G AND (RESSEQ 401:637)
29	X-RAY DIFFRACTION	29	CHAIN H AND (RESSEQ 16:99)
30	X-RAY DIFFRACTION	30	CHAIN H AND (RESSEQ 100:309)
31	X-RAY DIFFRACTION	31	CHAIN H AND (RESSEQ 310:394)
32	X-RAY DIFFRACTION	32	CHAIN H AND (RESSEQ 401:637)

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