PDB-1sx3: GroEL14-(ATPgammaS)14

ID or keywords:

Entry

Database: PDB / ID: 1sx3

Title

GroEL14-(ATPgammaS)14

Components

groEL protein

Keywords

CHAPERONE / GroEL / protein folding / molecular chaperone

Function / homology

Function and homology information

GroEL-GroES complex / chaperonin ATPase / virion assembly / : / isomerase activity / ATP-dependent protein folding chaperone / response to radiation / unfolded protein binding / protein folding / response to heat ...
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

MOLECULAR REPLACEMENT / Resolution: 2 Å

Authors

Chaudhry, C. / Horwich, A.L. / Brunger, A.T. / Adams, P.D.

Citation

Journal: J.Mol.Biol. / Year: 2003
Title: Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution.
Authors: Wang, J. / Boisvert, D.C.

History

Deposition	Mar 30, 2004	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 1, 2005	Provider: repository / Type: Initial release
Revision 1.1	Apr 30, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.3	Jan 22, 2014	Group: Refinement description
Revision 1.4	Mar 26, 2014	Group: Non-polymer description
Revision 1.5	Oct 11, 2017	Group: Refinement description / Category: software
Revision 1.6	Oct 27, 2021	Group: Database references / Derived calculations Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._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_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_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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_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.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_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.7	Feb 14, 2024	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond / 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_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_seq_id

Remark 0

THIS ENTRY 1SX3 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA R1KP8SF DETERMINED ...

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	1sx3.cif.gz	1.3 MB	Display	PDBx/mmCIF format
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Validation report

Summary document	1sx3_validation.pdf.gz	4.2 MB	Display	wwPDB validaton report
Full document	1sx3_full_validation.pdf.gz	4.5 MB	Display
Data in XML	1sx3_validation.xml.gz	261.7 KB	Display
Data in CIF	1sx3_validation.cif.gz	352.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/sx/1sx3 ftp://data.pdbj.org/pub/pdb/validation_reports/sx/1sx3	HTTPS FTP

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Related structure data

Related structure data	1ss8C 1svtC 1sx4C 1kp8 C: citing same article (ref.)
Similar structure data	1kp8-d 1ss8-1 1oel-1 4v43-2 2nwc-d 2ynj-d 4v43-1 4hel-d 6kfv-d 1xck-d 5opw-d 3e76-d 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
Related items in Molecule of the Month	#32 - Aug 2002 Chaperones similarity (11) #150 - Jun 2012 Sliding Clamps similarity (1)

Deposited unit

A: groEL protein

B: groEL protein

C: groEL protein

D: groEL protein

E: groEL protein

F: groEL protein

G: groEL protein

H: groEL protein

I: groEL protein

J: groEL protein

K: groEL protein

L: groEL protein

M: groEL protein

N: groEL protein

hetero molecules

782 kDa, 14 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	135.571, 260.112, 150.200
Angle α, β, γ (deg.)	90.00, 101.14, 90.00
Int Tables number	4
Space group name H-M	P12₁1

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	ALA	ALA	SER	SER	A	A	2 - 135	1 - 134
2	1	1	ALA	ALA	SER	SER	B	B	2 - 135	1 - 134
3	1	1	ALA	ALA	SER	SER	C	C	2 - 135	1 - 134
4	1	1	ALA	ALA	SER	SER	D	D	2 - 135	1 - 134
5	1	1	ALA	ALA	SER	SER	E	E	2 - 135	1 - 134
6	1	1	ALA	ALA	SER	SER	F	F	2 - 135	1 - 134
7	1	1	ALA	ALA	SER	SER	G	G	2 - 135	1 - 134
8	1	1	ALA	ALA	SER	SER	H	H	2 - 135	1 - 134
9	1	1	ALA	ALA	SER	SER	I	I	2 - 135	1 - 134
10	1	1	ALA	ALA	SER	SER	J	J	2 - 135	1 - 134
11	1	1	ALA	ALA	SER	SER	K	K	2 - 135	1 - 134
12	1	1	ALA	ALA	SER	SER	L	L	2 - 135	1 - 134
13	1	1	ALA	ALA	SER	SER	M	M	2 - 135	1 - 134
14	1	1	ALA	ALA	SER	SER	N	N	2 - 135	1 - 134
15	2	1	GLY	GLY	LYS	LYS	A	A	410 - 526	409 - 525
16	2	1	GLY	GLY	LYS	LYS	B	B	410 - 526	409 - 525
17	2	1	GLY	GLY	LYS	LYS	C	C	410 - 526	409 - 525
18	2	1	GLY	GLY	LYS	LYS	D	D	410 - 526	409 - 525
19	2	1	GLY	GLY	LYS	LYS	E	E	410 - 526	409 - 525
20	2	1	GLY	GLY	LYS	LYS	F	F	410 - 526	409 - 525
21	2	1	GLY	GLY	LYS	LYS	G	G	410 - 526	409 - 525
22	2	1	GLY	GLY	LYS	LYS	H	H	410 - 526	409 - 525
23	2	1	GLY	GLY	LYS	LYS	I	I	410 - 526	409 - 525
24	2	1	GLY	GLY	LYS	LYS	J	J	410 - 526	409 - 525
25	2	1	GLY	GLY	LYS	LYS	K	K	410 - 526	409 - 525
26	2	1	GLY	GLY	LYS	LYS	L	L	410 - 526	409 - 525
27	2	1	GLY	GLY	LYS	LYS	M	M	410 - 526	409 - 525
28	2	1	GLY	GLY	LYS	LYS	N	N	410 - 526	409 - 525
29	3	1	MG	MG	HOH	HOH	A	O - GB	550 - 562
30	3	1	MG	MG	HOH	HOH	B	R - HB	550 - 562
31	3	1	MG	MG	HOH	HOH	C	U - IB	550 - 562
32	3	1	MG	MG	HOH	HOH	D	Y - JB	550 - 563
33	3	1	MG	MG	HOH	HOH	E	CA - KB	550 - 562
34	3	1	MG	MG	HOH	HOH	F	FA - LB	550 - 562
35	3	1	MG	MG	HOH	HOH	G	IA - MB	550 - 562
36	3	1	MG	MG	HOH	HOH	H	LA - NB	550 - 562
37	3	1	MG	MG	HOH	HOH	I	OA - OB	550 - 562
38	3	1	MG	MG	HOH	HOH	J	RA - PB	550 - 562
39	3	1	MG	MG	HOH	HOH	K	UA - QB	550 - 562
40	3	1	MG	MG	HOH	HOH	L	XA - RB	550 - 562
41	3	1	MG	MG	HOH	HOH	M	AB - SB	550 - 562
42	3	1	MG	MG	HOH	HOH	N	DB - TB	550 - 562
43	4	1	K	K	HOH	HOH	A	P - GB	560 - 566
44	4	1	K	K	HOH	HOH	B	S - HB	560 - 566
45	4	1	K	K	HOH	HOH	C	V - IB	560 - 566
46	4	1	K	K	HOH	HOH	D	Z - JB	560 - 567
47	4	1	K	K	HOH	HOH	E	DA - KB	560 - 566
48	4	1	K	K	HOH	HOH	F	GA - LB	560 - 566
49	4	1	K	K	HOH	HOH	G	JA - MB	560 - 566
50	4	1	K	K	HOH	HOH	H	MA - NB	560 - 566
51	4	1	K	K	HOH	HOH	I	PA - OB	560 - 566
52	4	1	K	K	HOH	HOH	J	SA - PB	560 - 566
53	4	1	K	K	HOH	HOH	K	VA - QB	560 - 566
54	4	1	K	K	HOH	HOH	L	YA - RB	560 - 566
55	4	1	K	K	HOH	HOH	M	BB - SB	560 - 566
56	4	1	K	K	HOH	HOH	N	EB - TB	560 - 566
1	1	2	VAL	VAL	VAL	VAL	A	A	136 - 190	135 - 189
2	1	2	VAL	VAL	VAL	VAL	B	B	136 - 190	135 - 189
3	1	2	VAL	VAL	VAL	VAL	C	C	136 - 190	135 - 189
4	1	2	VAL	VAL	VAL	VAL	D	D	136 - 190	135 - 189
5	1	2	VAL	VAL	VAL	VAL	E	E	136 - 190	135 - 189
6	1	2	VAL	VAL	VAL	VAL	F	F	136 - 190	135 - 189
7	1	2	VAL	VAL	VAL	VAL	G	G	136 - 190	135 - 189
8	1	2	VAL	VAL	VAL	VAL	H	H	136 - 190	135 - 189
9	1	2	VAL	VAL	VAL	VAL	I	I	136 - 190	135 - 189
10	1	2	VAL	VAL	VAL	VAL	J	J	136 - 190	135 - 189
11	1	2	VAL	VAL	VAL	VAL	K	K	136 - 190	135 - 189
12	1	2	VAL	VAL	VAL	VAL	L	L	136 - 190	135 - 189
13	1	2	VAL	VAL	VAL	VAL	M	M	136 - 190	135 - 189
14	1	2	VAL	VAL	VAL	VAL	N	N	136 - 190	135 - 189
15	2	2	GLY	GLY	GLU	GLU	A	A	375 - 409	374 - 408
16	2	2	GLY	GLY	GLU	GLU	B - A	B - A	375 - 409	374 - 408
17	2	2	GLY	GLY	GLU	GLU	C - A	C - A	375 - 409	374 - 408
18	2	2	GLY	GLY	GLU	GLU	D - A	D - A	375 - 409	374 - 408
19	2	2	GLY	GLY	GLU	GLU	E - A	E - A	375 - 409	374 - 408
20	2	2	GLY	GLY	GLU	GLU	F - A	F - A	375 - 409	374 - 408
21	2	2	GLY	GLY	GLU	GLU	G - A	G - A	375 - 409	374 - 408
22	2	2	GLY	GLY	GLU	GLU	H - A	H - A	375 - 409	374 - 408
23	2	2	GLY	GLY	GLU	GLU	I - A	I - A	375 - 409	374 - 408
24	2	2	GLY	GLY	GLU	GLU	J - A	J - A	375 - 409	374 - 408
25	2	2	GLY	GLY	GLU	GLU	K - A	K - A	375 - 409	374 - 408
26	2	2	GLY	GLY	GLU	GLU	L - A	L - A	375 - 409	374 - 408
27	2	2	GLY	GLY	GLU	GLU	M - A	M - A	375 - 409	374 - 408
28	2	2	GLY	GLY	GLU	GLU	N - A	N - A	375 - 409	374 - 408
1	1	3	ALA	ALA	SER	SER	A	A	2 - 135	1 - 134
2	1	3	ALA	ALA	SER	SER	B	B	2 - 135	1 - 134
3	1	3	ALA	ALA	SER	SER	C	C	2 - 135	1 - 134
4	1	3	ALA	ALA	SER	SER	D	D	2 - 135	1 - 134
5	1	3	ALA	ALA	SER	SER	E	E	2 - 135	1 - 134
6	1	3	ALA	ALA	SER	SER	F	F	2 - 135	1 - 134
7	1	3	ALA	ALA	SER	SER	G	G	2 - 135	1 - 134
8	1	3	ALA	ALA	SER	SER	H	H	2 - 135	1 - 134
9	1	3	ALA	ALA	SER	SER	I	I	2 - 135	1 - 134
10	1	3	ALA	ALA	SER	SER	J	J	2 - 135	1 - 134
11	1	3	ALA	ALA	SER	SER	K	K	2 - 135	1 - 134
12	1	3	ALA	ALA	SER	SER	L	L	2 - 135	1 - 134
13	1	3	ALA	ALA	SER	SER	M	M	2 - 135	1 - 134
14	1	3	ALA	ALA	SER	SER	N	N	2 - 135	1 - 134
15	2	3	GLY	GLY	PRO	PRO	A	A	410 - 525	409 - 524
16	2	3	GLY	GLY	PRO	PRO	B	B	410 - 525	409 - 524
17	2	3	GLY	GLY	PRO	PRO	C	C	410 - 525	409 - 524
18	2	3	GLY	GLY	PRO	PRO	D	D	410 - 525	409 - 524
19	2	3	GLY	GLY	PRO	PRO	E	E	410 - 525	409 - 524
20	2	3	GLY	GLY	PRO	PRO	F	F	410 - 525	409 - 524
21	2	3	GLY	GLY	PRO	PRO	G	G	410 - 525	409 - 524
22	2	3	GLY	GLY	PRO	PRO	H	H	410 - 525	409 - 524
23	2	3	GLY	GLY	PRO	PRO	I	I	410 - 525	409 - 524
24	2	3	GLY	GLY	PRO	PRO	J	J	410 - 525	409 - 524
25	2	3	GLY	GLY	PRO	PRO	K	K	410 - 525	409 - 524
26	2	3	GLY	GLY	PRO	PRO	L	L	410 - 525	409 - 524
27	2	3	GLY	GLY	PRO	PRO	M	M	410 - 525	409 - 524
28	2	3	GLY	GLY	PRO	PRO	N	N	410 - 525	409 - 524

NCS ensembles :

ID
1
2
3

#1: Protein	groEL protein / Protein Cpn60 / 60 kDa chaperonin Mass: 55277.199 Da / Num. of mol.: 14 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: GROL, GROEL, MOPA, B4143, C5227, Z5748, ECS5124, SF4297, S4564 Production host: Escherichia coli (E. coli) / References: UniProt: P0A6F5
#2: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: Mg
#3: Chemical	ChemComp-K / POTASSIUM ION Mass: 39.098 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: K
#4: Chemical	ChemComp-AGS / PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-GAMMA-S / ADENOSINE 5'-(3-THIOTRIPHOSPHATE) / ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE) / ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE Mass: 523.247 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C₁₀H₁₆N₅O₁₂P₃S / Comment: ATP-gamma-S, energy-carrying molecule analogue*YM
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 946 / 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: 3.36 Å³/Da / Density % sol: 63.37 % / Description: AUTHOR USED THE SF DATA FROM ENTRY 1KP8
Crystal grow	Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG 8000, bis-tris propane, ethylene glycol, glycerol, potassium chloride, calcium chloride, ATPgammaS, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Relative weight: 1

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Processing

Software

Name	Version	Classification
REFMAC	refmac_5.1.19	refinement
DENZO		data reduction
SCALEPACK		data scaling
X-PLOR		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2→39.841 Å / Cor.coef. F_o:F_c: 0.937 / Cor.coef. F_o:F_c free: 0.926 / SU B: 7.636 / SU ML: 0.182 / SU R Cruickshank DPI: 0.209 / TLS residual ADP flag: LIKELY RESIDUAL / σ(F): 0 / ESU R Free: 0.172 / Stereochemistry target values: Engh & Huber

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2647	10647	1.969 %	RANDOM
R_work	0.2455	-	-	-
all	0.246	540790	-	-
obs	0.246	540790	-	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK

Displacement parameters

B_iso mean: 13.974 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-3.059 Å²	0 Å²	0.01 Å²
2-	-	-0.144 Å²	0 Å²
3-	-	-	3.206 Å²

Refinement step

Cycle: LAST / Resolution: 2→39.841 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	53970	0	464	946	55380

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.026	0.022	54824
X-RAY DIFFRACTION	r_angle_refined_deg	1.961	1.994	74130
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.388	5	7336
X-RAY DIFFRACTION	r_chiral_restr	0.147	0.2	9002
X-RAY DIFFRACTION	r_gen_planes_refined	0.008	0.02	39564
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.159	0.2	1800
X-RAY DIFFRACTION	r_metal_ion_refined	0.357	0.2	121
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.428	0.2	97
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.417	0.2	16
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined	0.102	0.2	3
X-RAY DIFFRACTION	r_mcbond_it	0.624	1.5	36218
X-RAY DIFFRACTION	r_mcangle_it	0.914	2	57960
X-RAY DIFFRACTION	r_scbond_it	1.893	3	18606
X-RAY DIFFRACTION	r_scangle_it	2.554	4.5	16170

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	1813	tight positional	0.09	0.05
1	2	B	1813	tight positional	0.17	0.05
1	3	C	1813	tight positional	0.07	0.05
1	4	D	1813	tight positional	0.12	0.05
1	5	E	1813	tight positional	0.15	0.05
1	6	F	1813	tight positional	0.09	0.05
1	7	G	1813	tight positional	0.12	0.05
1	8	H	1813	tight positional	0.1	0.05
1	9	I	1813	tight positional	0.09	0.05
1	10	J	1813	tight positional	0.08	0.05
1	11	K	1813	tight positional	0.08	0.05
1	12	L	1813	tight positional	0.09	0.05
1	13	M	1813	tight positional	0.09	0.05
1	14	N	1813	tight positional	0.09	0.05
2	1	A	647	tight positional	0.06	0.05
2	2	B	647	tight positional	0.1	0.05
2	3	C	647	tight positional	0.06	0.05
2	4	D	647	tight positional	0.09	0.05
2	5	E	647	tight positional	0.07	0.05
2	6	F	647	tight positional	0.07	0.05
2	7	G	647	tight positional	0.09	0.05
2	8	H	647	tight positional	0.06	0.05
2	9	I	647	tight positional	0.06	0.05
2	10	J	647	tight positional	0.05	0.05
2	11	K	647	tight positional	0.06	0.05
2	12	L	647	tight positional	0.06	0.05
2	13	M	647	tight positional	0.06	0.05
2	14	N	647	tight positional	0.06	0.05
3	1	A	1398	tight positional	0.04	0.05
3	2	B	1398	tight positional	0.04	0.05
3	3	C	1398	tight positional	0.04	0.05
3	4	D	1398	tight positional	0.07	0.05
3	5	E	1398	tight positional	0.04	0.05
3	6	F	1398	tight positional	0.04	0.05
3	7	G	1398	tight positional	0.07	0.05
3	8	H	1398	tight positional	0.04	0.05
3	9	I	1398	tight positional	0.06	0.05
3	10	J	1398	tight positional	0.05	0.05
3	11	K	1398	tight positional	0.04	0.05
3	12	L	1398	tight positional	0.04	0.05
3	13	M	1398	tight positional	0.05	0.05
3	14	N	1398	tight positional	0.06	0.05
1	1	A	1813	tight thermal	0.33	0.5
1	2	B	1813	tight thermal	0.42	0.5
1	3	C	1813	tight thermal	0.3	0.5
1	4	D	1813	tight thermal	0.39	0.5
1	5	E	1813	tight thermal	0.51	0.5
1	6	F	1813	tight thermal	0.33	0.5
1	7	G	1813	tight thermal	0.4	0.5
1	8	H	1813	tight thermal	0.45	0.5
1	9	I	1813	tight thermal	0.41	0.5
1	10	J	1813	tight thermal	0.31	0.5
1	11	K	1813	tight thermal	0.31	0.5
1	12	L	1813	tight thermal	0.38	0.5
1	13	M	1813	tight thermal	0.31	0.5
1	14	N	1813	tight thermal	0.33	0.5
2	1	A	647	tight thermal	0.13	0.5
2	2	B	647	tight thermal	0.16	0.5
2	3	C	647	tight thermal	0.15	0.5
2	4	D	647	tight thermal	0.29	0.5
2	5	E	647	tight thermal	0.19	0.5
2	6	F	647	tight thermal	0.13	0.5
2	7	G	647	tight thermal	0.27	0.5
2	8	H	647	tight thermal	0.17	0.5
2	9	I	647	tight thermal	0.15	0.5
2	10	J	647	tight thermal	0.15	0.5
2	11	K	647	tight thermal	0.16	0.5
2	12	L	647	tight thermal	0.13	0.5
2	13	M	647	tight thermal	0.17	0.5
2	14	N	647	tight thermal	0.13	0.5
3	1	A	1398	tight thermal	0.09	0.5
3	2	B	1398	tight thermal	0.07	0.5
3	3	C	1398	tight thermal	0.1	0.5
3	4	D	1398	tight thermal	0.23	0.5
3	5	E	1398	tight thermal	0.08	0.5
3	6	F	1398	tight thermal	0.08	0.5
3	7	G	1398	tight thermal	0.19	0.5
3	8	H	1398	tight thermal	0.09	0.5
3	9	I	1398	tight thermal	0.14	0.5
3	10	J	1398	tight thermal	0.07	0.5
3	11	K	1398	tight thermal	0.09	0.5
3	12	L	1398	tight thermal	0.08	0.5
3	13	M	1398	tight thermal	0.09	0.5
3	14	N	1398	tight thermal	0.09	0.5

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	Num. reflection all
2-2.0519	0.464	497	0.473	24808	X-RAY DIFFRACTION	25305
2.052-2.108	0.438	534	0.444	26914	X-RAY DIFFRACTION	27448
2.108-2.1689	0.397	615	0.395	28836	X-RAY DIFFRACTION	29451
2.169-2.2355	0.363	575	0.357	30010	X-RAY DIFFRACTION	30585
2.235-2.3085	0.348	639	0.329	31203	X-RAY DIFFRACTION	31842
2.309-2.3893	0.311	614	0.306	31929	X-RAY DIFFRACTION	32543
2.389-2.4791	0.343	656	0.299	31948	X-RAY DIFFRACTION	32604
2.479-2.58	0.325	617	0.282	32157	X-RAY DIFFRACTION	32774
2.58-2.6942	0.294	645	0.263	31955	X-RAY DIFFRACTION	32600
2.694-2.825	0.266	621	0.246	31743	X-RAY DIFFRACTION	32364
2.825-2.977	0.249	589	0.231	31214	X-RAY DIFFRACTION	31803
2.977-3.1565	0.267	623	0.227	30548	X-RAY DIFFRACTION	31171
3.156-3.3729	0.24	591	0.215	29503	X-RAY DIFFRACTION	30094
3.373-3.641	0.243	602	0.217	28032	X-RAY DIFFRACTION	28634
3.641-3.9852	0.225	565	0.211	25970	X-RAY DIFFRACTION	26535
3.985-4.45	0.22	478	0.198	23606	X-RAY DIFFRACTION	24084
4.45-5.1277	0.234	402	0.211	20926	X-RAY DIFFRACTION	21328
5.128-6.2543	0.268	358	0.25	17711	X-RAY DIFFRACTION	18069
6.254-8.738	0.226	284	0.213	13558	X-RAY DIFFRACTION	13842
8.738-39.841	0.215	142	0.216	7572	X-RAY DIFFRACTION	7714

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	3.2971	-0.6798	-0.096	2.2413	0.1097	0.8398	-0.0165	0.0845	-0.0114	-0.0781	0.0227	-0.0054	-0.1192	0.1344	-0.0062	0.229	0.0057	0.0195	0.2179	0.0637	0.1002	118.905	29.35	9.333
2	3.5855	-1.6953	0.1122	8.1085	4.0753	9.7947	-0.0321	0.1171	0.4138	0.1598	0.1742	-0.6758	-0.8281	0.3834	-0.142	0.4741	-0.0034	0	0.5269	0.0897	0.5141	136.232	37.959	-4.181
3	9.4354	1.0846	0.8057	6.9011	0.3393	4.31	0.0725	0.341	-0.0847	-0.409	-0.0028	-0.7593	-0.3006	0.2541	-0.0698	0.7021	0.0989	0.0135	0.6486	-0.0107	0.5203	129.165	32.829	-28.471
4	2.1805	0.3806	0.0586	2.6268	0.4214	0.6353	-0.0589	0.1397	-0.0847	-0.0421	0.1136	0.1924	0.0106	0.003	-0.0547	0.1611	-0.0009	0.0227	0.2112	-0.0176	0.0955	127.994	-9.59	8.87
5	3.9057	3.5237	4.5065	8.2498	3.588	9.1661	0.1679	0.5027	-0.5618	0.1569	-0.0402	-0.923	-0.0968	0.3024	-0.1278	0.4563	-0.0078	-0.0102	0.4589	-0.0078	0.4563	145.005	-17.991	-5.26
6	11.106	-0.7763	0.3829	9.8982	0.2477	5.7459	-0.0903	0.2729	-0.4735	-0.5122	0.0157	-0.3641	-0.2414	0.1431	0.0747	0.7699	-0.121	-0.0178	0.6724	-0.0363	0.5449	134.427	-15.014	-29.379
7	3.0664	0.8546	0.2446	2.2907	0.1076	0.8147	0.0392	0.1449	-0.117	-0.0605	-0.0103	-0.0558	0.1309	0.0852	-0.0289	0.1919	0.0165	0.0277	0.2252	-0.0506	0.218	103.371	-41.048	9.168
8	11.8922	-1.0694	4.6121	1.7913	-2.8446	7.2935	0.1015	0.1236	-1.2161	-0.5075	-0.4418	0.1435	0.0893	0.2956	0.3403	0.5151	-0.0212	0.0669	0.4741	-0.019	0.5001	107.363	-59.785	-4.651
9	8.4706	0.0809	0.3694	12.1932	0.4587	6.7181	-0.2771	0.3291	-0.6544	-0.2103	0.3295	0.1562	0.3028	0.0629	-0.0524	0.6456	-0.0102	-0.025	0.6849	-0.023	0.5178	102.601	-50.687	-28.528
10	3.0301	0.2929	0.2935	1.8262	-0.0199	0.6127	0.0085	-0.0692	0.094	-0.0625	-0.0365	-0.1487	0.0484	0.0184	0.028	0.2012	0.0124	0.0321	0.1563	-0.071	0.1119	63.337	-41.158	9.587
11	3.0565	-0.1379	-0.8677	3.9184	-1.1244	7.0997	-0.1026	-0.5896	-0.4773	0.3086	0.0209	-0.1745	0.5905	0.5308	0.0817	0.4409	0.0457	-0.0365	0.4115	0.0721	0.4199	51.026	-55.789	-4.257
12	3.7077	-0.083	-0.0446	7.5502	0.258	2.4045	0.1191	0.1803	0.1992	0.0545	-0.1316	1.0311	-0.2676	-0.3657	0.0125	0.5311	0.0485	0.0493	0.4816	0.0016	0.4674	54.804	-45.928	-27.963
13	2.7714	-0.7752	0.0833	2.4388	0.0053	0.7466	-0.0456	0.0246	-0.0431	-0.0442	0.0633	-0.2339	0.0081	-0.0391	-0.0177	0.178	-0.0142	0.0223	0.1537	-0.0376	0.0244	38.449	-10.123	10.877
14	2.8967	0.7613	-0.7885	8.6606	-3.5193	7.6949	0.1741	0.0191	-0.0439	0.1893	0.0585	0.8511	0.4676	-0.5806	-0.2326	0.4634	0.0011	-0.0003	0.4636	-0.0002	0.4633	18.753	-9.923	-2.153
15	8.1352	-0.8192	-0.3671	6.9538	0.0012	4.1311	0.2052	0.5223	0.2671	-0.4644	-0.0835	0.3801	0.2719	-0.1657	-0.1217	0.7853	-0.0069	-0.0217	0.6562	0.038	0.5407	27.068	-7.301	-26.604
16	2.1828	0.8143	-0.1157	2.8546	-0.1046	0.8271	-0.013	0.1329	0.0545	-0.0538	0.0098	0.0299	-0.1125	-0.1	0.0032	0.2143	0.0066	0.0067	0.1992	0.0124	0.1029	46.841	28.874	11.149
17	8.3716	4.2595	-5.058	4.2325	-0.0979	10.7066	0.297	0.2083	1.2033	-0.0469	-0.4903	0.6288	-0.1247	-0.7531	0.1933	0.5211	0.0243	-0.0812	0.476	-0.0157	0.5092	34.251	44.125	-1.85
18	9.4105	-2.4308	-0.0643	10.7539	-0.1865	6.6837	-0.0137	0.202	0.3367	-0.5754	0.0793	-0.1439	-0.1302	0.0224	-0.0656	0.7168	-0.1388	-0.0111	0.7465	0.0444	0.5415	40.929	38.685	-26.423
19	0.3924	0.7592	-0.4221	1.0687	-0.6103	0.3903	0.0157	-0.0142	-0.0425	-0.0217	-0.0115	0.0122	0.0004	-0.0224	-0.0042	0.232	0.0266	0.0038	0.2008	0.0201	0.2514	82.771	46.406	9.945
20	4.6721	-1.4161	0.4257	3.3975	2.9036	7.0374	-0.1165	-0.7572	0.331	0.2932	-0.1287	0.0924	0.1044	-0.673	0.2452	0.4257	0.046	0.0561	0.4368	-0.0457	0.424	86.608	64.925	-4.131
21	5.7745	-1.611	0.2759	6.8591	0.4984	2.8318	0.0585	0.3716	0.1677	-0.0289	0.1029	-0.9275	0.0748	0.5201	-0.1613	0.5228	0.0857	0.0007	0.5639	-0.0429	0.4891	86.601	53.97	-27.629
22	0.7598	-0.0712	-0.0405	-0.0223	0.0412	0.0868	-0.017	-0.0609	0.0568	0.0669	0.0079	-0.0352	0.0023	-0.0618	0.0091	0.2957	-0.0076	0.0184	0.3162	-0.0147	0.1164	38.631	6.671	44.126
23	1.8706	-0.4909	2.269	5.7337	-3.0454	7.9315	-0.1218	-0.3322	0.1588	-0.199	0.1509	0.6593	-0.3686	-0.5545	-0.029	0.4694	-0.0127	0.0119	0.4763	-0.0175	0.4741	19.784	4.961	58.206
24	8.5067	0.4355	0.0283	5.5423	0.6039	3.755	0.0717	-0.2958	-0.6142	0.4361	-0.1615	0.3557	-0.1109	-0.2435	0.0898	0.7047	0.0247	0.0111	0.6149	0.0036	0.5175	30.154	3.113	82.067
25	0.15	0.0108	-0.0184	0.2127	-0.0126	0.0941	0.0066	-0.0598	-0.0948	0.1031	-0.0202	0.0406	0.0699	-0.0318	0.0137	0.3417	-0.0126	0.0347	0.2961	-0.0023	0.2717	50.293	-31.407	43.212
26	0.5002	0.1537	-0.025	0.1662	0.1279	-0.0937	0.0893	-0.2729	-0.3412	0.3485	-0.1623	-0.0673	0.0372	0.1185	0.073	0.6515	0.0494	0.0621	0.5426	0.0255	0.5362	39.711	-47.559	56.674
27	0.0746	0.2713	0.0373	0.3186	-0.2516	-0.033	0.2811	-0.2717	0.1975	0.4124	-0.0411	-0.0483	-0.3566	-0.0267	-0.24	0.7941	0.0807	-0.1179	0.8836	-0.0236	0.61	47.116	-41.567	80.882
28	3.5928	-0.1867	0.1704	2.013	0.1557	0.7241	0.0742	-0.0676	-0.1933	0.1652	-0.0753	-0.0558	0.0999	0.0244	0.0011	0.3024	-0.0041	-0.0132	0.2582	0.0391	0.1126	87.486	-45.935	42.486
29	7.6811	2.9325	3.9444	2.9162	3.8947	8.6431	0.17	-0.0433	-0.9861	0.7338	-0.0754	-0.7994	0.3124	-0.1385	-0.0947	0.4891	0.0344	0.0387	0.4839	0.0359	0.4918	93.585	-64.464	55.773
30	8.1461	-2.4474	0.2751	9.9698	0.4096	5.2077	-0.0228	-0.3295	-0.3427	0.0784	0.0992	-0.4268	0.1101	-0.1625	-0.0763	0.712	-0.1242	-0.0444	0.7601	0.0388	0.5482	93.1	-55.669	80.11
31	3.3747	0.8968	0.0622	2.7652	0.2443	0.8132	0.0066	-0.0944	-0.1636	0.1665	0.0208	-0.1698	0.0888	0.0909	-0.0274	0.2803	0.0104	-0.0397	0.2752	0.0321	0.1223	121.849	-25.741	41.981
32	3.0344	1.0564	-0.8325	11.6607	6.9303	10.1433	-0.2269	-0.2663	-0.2043	0.2245	0.319	-1.1419	0.0482	0.3219	-0.0921	0.4709	-0.0055	-0.0076	0.5069	0.0614	0.4984	140.091	-32.783	55.232
33	12.9986	-0.3278	0.1349	8.9863	1.1927	7.4067	0.2199	-0.4217	0.1017	0.0292	0.0211	-0.294	0.1635	0.1545	-0.241	0.7081	-0.031	-0.0185	0.6657	0.0073	0.5176	132.44	-28.203	79.865
34	2.5855	-0.2735	-0.0075	3.3162	0.5068	0.8092	-0.0628	-0.096	0.0398	0.0532	0.0954	-0.0199	-0.0498	0.0816	-0.0326	0.2194	0.0042	-0.0139	0.3036	-0.0204	0.0022	127.578	13.797	42.184
35	3.9886	-3.7664	-4.7906	5.1687	2.5386	7.0061	0.0974	-0.51	0.6267	-0.1337	-0.2162	-0.4785	-0.1815	0.0256	0.1188	0.4868	-0.0273	-0.0366	0.4786	0.0237	0.4872	144.46	23.25	55.744
36	10.3972	-0.4697	-0.0105	5.5165	-0.3443	4.8163	-0.0392	-0.0326	1.057	0.2331	-0.0001	0.3282	-0.2954	-0.1962	0.0392	0.6993	0.1082	0.0162	0.6589	-0.0372	0.532	134.916	20.214	80.052
37	3.2309	-0.9772	-0.2127	2.466	-0.0921	0.9187	-0.004	-0.1501	0.1457	0.1053	-0.0292	-0.1517	-0.1554	0.0897	0.0332	0.2633	-0.017	-0.0156	0.2663	-0.0329	0.1177	100.51	43.136	42.681
38	9.8919	0.1277	-4.3461	3.8057	-2.4391	9.5546	0.0699	-0.2064	1.1794	0.3025	-0.1928	0.0186	-0.3414	0.3257	0.1229	0.5109	0.0247	-0.0691	0.4754	-0.0237	0.505	103.593	62.366	56.045
39	9.4805	-1.4823	-0.2421	10.7482	0.0895	6.938	-0.045	-0.5265	0.3892	0.4777	0.2226	0.166	-0.267	0.0918	-0.1775	0.6749	0.0294	0.0356	0.6912	-0.0166	0.5236	101.179	53.966	80.49
40	3.3053	0.4402	-0.2191	2.2109	-0.2132	0.8226	-0.0079	-0.0318	0.1667	0.1478	0.0294	0.0366	-0.0929	-0.0334	-0.0215	0.2762	0.0045	0.0169	0.2309	-0.0158	0.0548	60.718	39.859	43.954
41	2.7956	3.3523	-0.8099	6.7095	-5.9235	7.3524	-0.2988	0.1086	0.443	0.4971	0.4902	0.7239	-0.1146	-0.0072	-0.1914	0.4752	0.0256	-0.0166	0.5023	-0.0542	0.4935	47.941	53.468	58.408
42	8.0277	-2.5072	0.3224	9.9756	-0.4509	5.2515	0.1353	-0.4018	0.4433	-0.0106	0.1562	0.8305	-0.3318	-0.3924	-0.2916	0.6806	-0.0812	0.0193	0.6064	-0.0049	0.5172	53.862	44.172	82.151

Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Selection: ALL

ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	A	SA - A	1 - 135	1 - 134
2	1	A	A	410 - 526	409 - 525
3	1	A	Q - GB	550 - 552	1 - 2
4	1	A	EA - GB	560 - 564	1 - 6
5	2	A	A	136 - 190	135 - 189
6	2	A	A	375 - 409	374 - 408
7	3	A	A	191 - 374	190 - 373
8	4	B	TA - B	1 - 135	1 - 134
9	4	B	B	410 - 526	409 - 525
10	4	B	R - HB	550 - 552	1 - 2
11	4	B	FA - HB	560 - 564	1 - 6
12	5	B	B	136 - 190	135 - 189
13	5	B	B	375 - 409	374 - 408
14	6	B	B	191 - 374	190 - 373
15	7	C	UA - C	1 - 135	1 - 134
16	7	C	C	410 - 526	409 - 525
17	7	C	S - IB	550 - 552	1 - 2
18	7	C	GA - IB	560 - 564	1 - 6
19	8	C	C	136 - 190	135 - 189
20	8	C	C	375 - 409	374 - 408
21	9	C	C	191 - 374	190 - 373
22	10	D	VA - D	1 - 135	1 - 134
23	10	D	D	410 - 526	409 - 525
24	10	D	T - JB	550 - 552	1 - 2
25	10	D	HA - JB	560 - 564	1 - 6
26	11	D	D	136 - 190	135 - 189
27	11	D	D	375 - 409	374 - 408
28	12	D	D	191 - 374	190 - 373
29	13	E	WA - E	1 - 135	1 - 134
30	13	E	E	410 - 526	409 - 525
31	13	E	U - KB	550 - 552	1 - 2
32	13	E	IA - KB	560 - 564	1 - 6
33	14	E	E	136 - 190	135 - 189
34	14	E	E	375 - 409	374 - 408
35	15	E	E	191 - 374	190 - 373
36	16	F	XA - F	1 - 135	1 - 134
37	16	F	F	410 - 526	409 - 525
38	16	F	V - LB	550 - 552	1 - 2
39	16	F	JA - LB	560 - 564	1 - 6
40	17	F	F	136 - 190	135 - 189
41	17	F	F	375 - 409	374 - 408
42	18	F	F	191 - 374	190 - 373
43	19	G	YA - G	1 - 135	1 - 134
44	19	G	G	410 - 526	409 - 525
45	19	G	W - MB	550 - 552	1 - 2
46	19	G	KA - MB	560 - 564	1 - 6
47	20	G	G	136 - 190	135 - 189
48	20	G	G	375 - 409	374 - 408
49	21	G	G	191 - 374	190 - 373
50	22	H	ZA - H	1 - 135	1 - 134
51	22	H	H	410 - 526	409 - 525
52	22	H	X - NB	550 - 552	1 - 2
53	22	H	LA - NB	560 - 564	1 - 6
54	23	H	H	136 - 190	135 - 189
55	23	H	H	375 - 409	374 - 408
56	24	H	H	191 - 374	190 - 373
57	25	I	AB - I	1 - 135	1 - 134
58	25	I	I	410 - 526	409 - 525
59	25	I	Y - OB	550 - 552	1 - 2
60	25	I	MA - OB	560 - 564	1 - 6
61	26	I	I	136 - 190	135 - 189
62	26	I	I	375 - 409	374 - 408
63	27	I	I	191 - 374	190 - 373
64	28	J	BB - J	1 - 135	1 - 134
65	28	J	J	410 - 526	409 - 525
66	28	J	Z - PB	550 - 552	1 - 2
67	28	J	NA - PB	560 - 564	1 - 6
68	29	J	J	136 - 190	135 - 189
69	29	J	J	375 - 409	374 - 408
70	30	J	J	191 - 374	190 - 373
71	31	K	CB - K	1 - 135	1 - 134
72	31	K	K	410 - 526	409 - 525
73	31	K	AA - QB	550 - 552	1 - 2
74	31	K	OA - QB	560 - 564	1 - 6
75	32	K	K	136 - 190	135 - 189
76	32	K	K	375 - 409	374 - 408
77	33	K	K	191 - 374	190 - 373
78	34	L	DB - L	1 - 135	1 - 134
79	34	L	L	410 - 526	409 - 525
80	34	L	BA - RB	550 - 552	1 - 2
81	34	L	PA - RB	560 - 564	1 - 6
82	35	L	L	136 - 190	135 - 189
83	35	L	L	375 - 409	374 - 408
84	36	L	L	191 - 374	190 - 373
85	37	M	EB - M	1 - 135	1 - 134
86	37	M	M	410 - 526	409 - 525
87	37	M	CA - SB	550 - 552	1 - 2
88	37	M	QA - SB	560 - 564	1 - 6
89	38	M	M	136 - 190	135 - 189
90	38	M	M	375 - 409	374 - 408
91	39	M	M	191 - 374	190 - 373
92	40	N	FB - N	1 - 135	1 - 134
93	40	N	N	410 - 526	409 - 525
94	40	N	DA - TB	550 - 552	1 - 2
95	40	N	RA - TB	560 - 564	1 - 6
96	41	N	N	136 - 190	135 - 189
97	41	N	N	375 - 409	374 - 408
98	42	N	N	191 - 374	190 - 373

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