PDB-1pf9: GroEL-GroES-ADP

ID or keywords:

Entry

Database: PDB / ID: 1pf9

Title

GroEL-GroES-ADP

Components

groEL protein
groES protein

Keywords

CHAPERONE / Chaperonin / Co-chaperonin

Function / homology

Function and homology information

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

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON / Resolution: 2.993 Å

Authors

Chaudhry, C. / Farr, G.W. / Todd, M.J. / Rye, H.S. / Brunger, A.T. / Adams, P.D. / Horwich, A.L. / Sigler, P.B.

Citation

Journal: Embo J. / Year: 2003
Title: Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics.
Authors: Chaudhry, C. / Farr, G.W. / Todd, M.J. / Rye, H.S. / Brunger, A.T. / Adams, P.D. / Horwich, A.L. / Sigler, P.B.

History

Deposition	May 24, 2003	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Nov 4, 2003	Provider: repository / Type: Initial release
Revision 1.1	Apr 29, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Refinement description / Version format compliance
Revision 1.3	Feb 14, 2024	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_struct_conn_angle / struct_conn / struct_ncs_dom_lim / 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_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.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_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_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_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	1pf9.cif.gz	1.3 MB	Display	PDBx/mmCIF format
PDB format	pdb1pf9.ent.gz	1.1 MB	Display	PDB format
PDBx/mmJSON format	1pf9.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	1pf9_validation.pdf.gz	3.1 MB	Display	wwPDB validaton report
Full document	1pf9_full_validation.pdf.gz	3.4 MB	Display
Data in XML	1pf9_validation.xml.gz	262 KB	Display
Data in CIF	1pf9_validation.cif.gz	356.9 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/pf/1pf9 ftp://data.pdbj.org/pub/pdb/validation_reports/pf/1pf9	HTTPS FTP

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Related structure data

Related structure data	1pcqC 1aon C: citing same article (ref.)
Similar structure data	1sx4-d 1pcq-d 3zq1-d 3zpz-d 1aon-d 1gru-d 2c7c-d 3zq0-d 4v4o-2 1svt-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 (19) #13 - Jan 2001 Alcohol Dehydrogenase 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

O: groES protein

P: groES protein

Q: groES protein

R: groES protein

S: groES protein

T: groES protein

U: groES protein

hetero molecules

849 kDa, 21 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)	255.260, 265.250, 184.400
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	18
Space group name H-M	P2₁2₁2

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	2	1	GLY	GLY	PRO	PRO	A	A	410 - 525	409 - 524
9	2	1	GLY	GLY	PRO	PRO	B	B	410 - 525	409 - 524
10	2	1	GLY	GLY	PRO	PRO	C	C	410 - 525	409 - 524
11	2	1	GLY	GLY	PRO	PRO	D	D	410 - 525	409 - 524
12	2	1	GLY	GLY	PRO	PRO	E	E	410 - 525	409 - 524
13	2	1	GLY	GLY	PRO	PRO	F	F	410 - 525	409 - 524
14	2	1	GLY	GLY	PRO	PRO	G	G	410 - 525	409 - 524
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	2	2	GLY	GLY	GLU	GLU	A	A	375 - 409	374 - 408
9	2	2	GLY	GLY	GLU	GLU	B	B	375 - 409	374 - 408
10	2	2	GLY	GLY	GLU	GLU	C	C	375 - 409	374 - 408
11	2	2	GLY	GLY	GLU	GLU	D	D	375 - 409	374 - 408
12	2	2	GLY	GLY	GLU	GLU	E	E	375 - 409	374 - 408
13	2	2	GLY	GLY	GLU	GLU	F	F	375 - 409	374 - 408
14	2	2	GLY	GLY	GLU	GLU	G	G	375 - 409	374 - 408
1	1	3	GLU	GLU	GLY	GLY	A	A	191 - 374	190 - 373
2	1	3	GLU	GLU	GLY	GLY	B	B	191 - 374	190 - 373
3	1	3	GLU	GLU	GLY	GLY	C	C	191 - 374	190 - 373
4	1	3	GLU	GLU	GLY	GLY	D	D	191 - 374	190 - 373
5	1	3	GLU	GLU	GLY	GLY	E	E	191 - 374	190 - 373
6	1	3	GLU	GLU	GLY	GLY	F	F	191 - 374	190 - 373
7	1	3	GLU	GLU	GLY	GLY	G	G	191 - 374	190 - 373
1	1	4	ALA	ALA	SER	SER	H	H	2 - 135	1 - 134
2	1	4	ALA	ALA	SER	SER	I	I	2 - 135	1 - 134
3	1	4	ALA	ALA	SER	SER	J	J	2 - 135	1 - 134
4	1	4	ALA	ALA	SER	SER	K	K	2 - 135	1 - 134
5	1	4	ALA	ALA	SER	SER	L	L	2 - 135	1 - 134
6	1	4	ALA	ALA	SER	SER	M	M	2 - 135	1 - 134
7	1	4	ALA	ALA	SER	SER	N	N	2 - 135	1 - 134
8	2	4	GLY	GLY	PRO	PRO	H	H	410 - 525	409 - 524
9	2	4	GLY	GLY	PRO	PRO	I	I	410 - 525	409 - 524
10	2	4	GLY	GLY	PRO	PRO	J	J	410 - 525	409 - 524
11	2	4	GLY	GLY	PRO	PRO	K	K	410 - 525	409 - 524
12	2	4	GLY	GLY	PRO	PRO	L	L	410 - 525	409 - 524
13	2	4	GLY	GLY	PRO	PRO	M	M	410 - 525	409 - 524
14	2	4	GLY	GLY	PRO	PRO	N	N	410 - 525	409 - 524
1	1	5	VAL	VAL	VAL	VAL	H	H	136 - 190	135 - 189
2	1	5	VAL	VAL	VAL	VAL	I	I	136 - 190	135 - 189
3	1	5	VAL	VAL	VAL	VAL	J	J	136 - 190	135 - 189
4	1	5	VAL	VAL	VAL	VAL	K	K	136 - 190	135 - 189
5	1	5	VAL	VAL	VAL	VAL	L	L	136 - 190	135 - 189
6	1	5	VAL	VAL	VAL	VAL	M	M	136 - 190	135 - 189
7	1	5	VAL	VAL	VAL	VAL	N	N	136 - 190	135 - 189
8	2	5	GLY	GLY	GLU	GLU	H	H	375 - 409	374 - 408
9	2	5	GLY	GLY	GLU	GLU	I	I	375 - 409	374 - 408
10	2	5	GLY	GLY	GLU	GLU	J	J	375 - 409	374 - 408
11	2	5	GLY	GLY	GLU	GLU	K	K	375 - 409	374 - 408
12	2	5	GLY	GLY	GLU	GLU	L	L	375 - 409	374 - 408
13	2	5	GLY	GLY	GLU	GLU	M	M	375 - 409	374 - 408
14	2	5	GLY	GLY	GLU	GLU	N	N	375 - 409	374 - 408
1	1	6	GLU	GLU	GLY	GLY	H	H	191 - 374	190 - 373
2	1	6	GLU	GLU	GLY	GLY	I	I	191 - 374	190 - 373
3	1	6	GLU	GLU	GLY	GLY	J	J	191 - 374	190 - 373
4	1	6	GLU	GLU	GLY	GLY	K	K	191 - 374	190 - 373
5	1	6	GLU	GLU	GLY	GLY	L	L	191 - 374	190 - 373
6	1	6	GLU	GLU	GLY	GLY	M	M	191 - 374	190 - 373
7	1	6	GLU	GLU	GLY	GLY	N	N	191 - 374	190 - 373
1	1	7	MET	MET	ALA	ALA	O	O	1 - 97	1 - 97
2	1	7	MET	MET	ALA	ALA	P	P	1 - 97	1 - 97
3	1	7	MET	MET	ALA	ALA	Q	Q	1 - 97	1 - 97
4	1	7	MET	MET	ALA	ALA	R	R	1 - 97	1 - 97
5	1	7	MET	MET	ALA	ALA	S	S	1 - 97	1 - 97
6	1	7	MET	MET	ALA	ALA	T	T	1 - 97	1 - 97
7	1	7	MET	MET	ALA	ALA	U	U	1 - 97	1 - 97

NCS ensembles :

ID
1
2
3
4
5
6
7

#1: Protein	groEL protein / Protein Cpn60 / 60 kDa chaperonin Mass: 55220.105 Da / Num. of mol.: 14 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: GROL OR GROEL OR MOPA OR B4143 OR C5227 OR Z5748 OR ECS5124 OR SF4297 Plasmid: IQ-TRC / Production host: Escherichia coli (E. coli) / Strain (production host): DH 5 ALPHA / References: UniProt: P06139, UniProt: P0A6F5*PLUS
#2: Protein	groES protein / Protein Cpn10 / 10 kDa chaperonin Mass: 10400.938 Da / Num. of mol.: 7 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: GROS OR GROES OR MOPB OR B4142 OR C5226 OR Z5747 OR ECS5123 OR SF4296 Plasmid: IQ-TRC / Production host: Escherichia coli (E. coli) / Strain (production host): DH 5 ALPHA / References: UniProt: P05380, UniProt: P0A6F9*PLUS
#3: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Mg
#4: Chemical	ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE Mass: 427.201 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C₁₀H₁₅N₅O₁₀P₂ / Comment: ADP, energy-carrying molecule*YM
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION

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Sample preparation

Crystal	Density Matthews: 3.69 Å³/Da / Density % sol: 66.66 % Description: Information in remark 200 is from PDB entry 1AON. The authors of this entry rerefined 1AON, but did not grow new crystals or collect any new data.

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 0.95
Detector	Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 15, 1996 / Details: MIRRORS
Radiation	Monochromator: TWO CRYSTAL NON-DISPERSIVE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.95 Å / Relative weight: 1
Reflection	Resolution: 3→99 Å / Num. obs: 242684 / % possible obs: 96.7 % / Redundancy: 3.3 % / R_sym value: 0.121 / Net I/σ(I): 9.1
Reflection shell	Resolution: 3→3.14 Å / Redundancy: 2.4 % / Mean I/σ(I) obs: 1.8 / R_sym value: 0.53 / % possible all: 91.2

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Processing

Software

Name	Version	Classification
REFMAC	refmac_5.1.24 24/04/2001	refinement
DENZO		data reduction
SCALEPACK		data scaling
X-PLOR		phasing

Refinement

Resolution: 2.993→40.161 Å / TLS residual ADP flag: LIKELY RESIDUAL / σ(F): 0

	R_factor	Num. reflection	% reflection
R_free	0.2866	12081	4.979 %
R_work	0.2685	-	-
obs	-	242644	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å

Displacement parameters

B_iso mean: 7.453 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-1.34 Å²	0 Å²	0 Å²
2-	-	-1.412 Å²	0 Å²
3-	-	-	2.751 Å²

Refinement step

Cycle: LAST / Resolution: 2.993→40.161 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	59080	0	196	7	59283

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	Bond distances: refined atoms	0.013	0.022	59703
X-RAY DIFFRACTION	Bond angles : refined atoms	1.375	1.988	80619
X-RAY DIFFRACTION	Torsion angles, period 1. refined	5.136	5	7994
X-RAY DIFFRACTION	Chiral centres: refined atoms	0.087	0.2	9800
X-RAY DIFFRACTION	Planar groups: refined atoms	0.004	0.02	43302
X-RAY DIFFRACTION	VDW repulsions: refined atoms	0.238	0.2	29906
X-RAY DIFFRACTION	VDW; torsion: refined atoms	0.307	0.2	41356
X-RAY DIFFRACTION	HBOND: refined atoms	0.132	0.2	1780
X-RAY DIFFRACTION	Metal-ion: refined atoms	0.136	0.2	11
X-RAY DIFFRACTION	VDW repulsions; symmetry: refined atoms	0.3	0.2	64
X-RAY DIFFRACTION	HBOND; symmetry: refined atoms	0.11	0.2	3
X-RAY DIFFRACTION	M. chain bond B values: refined atoms	0.221	1.5	39515
X-RAY DIFFRACTION	M. chain angle B values: refined atoms	0.403	2	63273
X-RAY DIFFRACTION	S. chain bond B values: refined atoms	0.749	3	20188
X-RAY DIFFRACTION	S. chain angle B values: refined atoms	1.182	4.5	17346

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	1840	tight positional	0.058	0.05
1	1	A	1840	tight thermal	0.097	0.5
1	1	B	1840	tight positional	0.049	0.05
1	1	B	1840	tight thermal	0.089	0.5
1	1	C	1840	tight positional	0.056	0.05
1	1	C	1840	tight thermal	0.1	0.5
1	1	D	1840	tight positional	0.056	0.05
1	1	D	1840	tight thermal	0.089	0.5
1	1	E	1840	tight positional	0.044	0.05
1	1	E	1840	tight thermal	0.083	0.5
1	1	F	1840	tight positional	0.044	0.05
1	1	F	1840	tight thermal	0.079	0.5
1	1	G	1840	tight positional	0.056	0.05
1	1	G	1840	tight thermal	0.097	0.5
2	2	A	647	tight positional	0.038	0.05
2	2	A	647	tight thermal	0.065	0.5
2	2	B	647	tight positional	0.029	0.05
2	2	B	647	tight thermal	0.044	0.5
2	2	C	647	tight positional	0.035	0.05
2	2	C	647	tight thermal	0.056	0.5
2	2	D	647	tight positional	0.038	0.05
2	2	D	647	tight thermal	0.06	0.5
2	2	E	647	tight positional	0.029	0.05
2	2	E	647	tight thermal	0.045	0.5
2	2	F	647	tight positional	0.025	0.05
2	2	F	647	tight thermal	0.044	0.5
2	2	G	647	tight positional	0.03	0.05
2	2	G	647	tight thermal	0.047	0.5
3	3	A	1398	tight positional	0.029	0.05
3	3	A	1398	tight thermal	0.015	0.5
3	3	B	1398	tight positional	0.038	0.05
3	3	B	1398	tight thermal	0.012	0.5
3	3	C	1398	tight positional	0.029	0.05
3	3	C	1398	tight thermal	0.013	0.5
3	3	D	1398	tight positional	0.029	0.05
3	3	D	1398	tight thermal	0.015	0.5
3	3	E	1398	tight positional	0.025	0.05
3	3	E	1398	tight thermal	0.012	0.5
3	3	F	1398	tight positional	0.029	0.05
3	3	F	1398	tight thermal	0.012	0.5
3	3	G	1398	tight positional	0.031	0.05
3	3	G	1398	tight thermal	0.012	0.5
4	4	H	1811	tight positional	0.05	0.05
4	4	H	1811	tight thermal	0.086	0.5
4	4	I	1811	tight positional	0.058	0.05
4	4	I	1811	tight thermal	0.104	0.5
4	4	J	1811	tight positional	0.057	0.05
4	4	J	1811	tight thermal	0.092	0.5
4	4	K	1811	tight positional	0.043	0.05
4	4	K	1811	tight thermal	0.077	0.5
4	4	L	1811	tight positional	0.045	0.05
4	4	L	1811	tight thermal	0.078	0.5
4	4	M	1811	tight positional	0.056	0.05
4	4	M	1811	tight thermal	0.089	0.5
4	4	N	1811	tight positional	0.053	0.05
4	4	N	1811	tight thermal	0.088	0.5
5	5	H	647	tight positional	0.025	0.05
5	5	H	647	tight thermal	0.034	0.5
5	5	I	647	tight positional	0.029	0.05
5	5	I	647	tight thermal	0.046	0.5
5	5	J	647	tight positional	0.027	0.05
5	5	J	647	tight thermal	0.036	0.5
5	5	K	647	tight positional	0.025	0.05
5	5	K	647	tight thermal	0.032	0.5
5	5	L	647	tight positional	0.02	0.05
5	5	L	647	tight thermal	0.031	0.5
5	5	M	647	tight positional	0.027	0.05
5	5	M	647	tight thermal	0.038	0.5
5	5	N	647	tight positional	0.027	0.05
5	5	N	647	tight thermal	0.036	0.5
6	6	H	1398	tight positional	0.021	0.05
6	6	H	1398	tight thermal	0.024	0.5
6	6	I	1398	tight positional	0.024	0.05
6	6	I	1398	tight thermal	0.028	0.5
6	6	J	1398	tight positional	0.023	0.05
6	6	J	1398	tight thermal	0.027	0.5
6	6	K	1398	tight positional	0.02	0.05
6	6	K	1398	tight thermal	0.022	0.5
6	6	L	1398	tight positional	0.03	0.05
6	6	L	1398	tight thermal	0.023	0.5
6	6	M	1398	tight positional	0.032	0.05
6	6	M	1398	tight thermal	0.034	0.5
6	6	N	1398	tight positional	0.02	0.05
6	6	N	1398	tight thermal	0.024	0.5
7	7	O	728	tight positional	0.017	0.05
7	7	O	728	tight thermal	0.02	0.5
7	7	P	728	tight positional	0.016	0.05
7	7	P	728	tight thermal	0.02	0.5
7	7	Q	728	tight positional	0.017	0.05
7	7	Q	728	tight thermal	0.021	0.5
7	7	R	728	tight positional	0.019	0.05
7	7	R	728	tight thermal	0.024	0.5
7	7	S	728	tight positional	0.017	0.05
7	7	S	728	tight thermal	0.021	0.5
7	7	T	728	tight positional	0.016	0.05
7	7	T	728	tight thermal	0.02	0.5
7	7	U	728	tight positional	0.016	0.05
7	7	U	728	tight thermal	0.02	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
2.993-3.0703	0.391	755	0.361	15143	X-RAY DIFFRACTION	15898
3.07-3.1539	0.357	856	0.342	16313	X-RAY DIFFRACTION	17169
3.154-3.2448	0.333	908	0.324	15904	X-RAY DIFFRACTION	16812
3.245-3.344	0.342	788	0.313	15642	X-RAY DIFFRACTION	16430
3.344-3.4528	0.339	782	0.299	15216	X-RAY DIFFRACTION	15998
3.453-3.5731	0.295	748	0.28	14722	X-RAY DIFFRACTION	15470
3.573-3.7068	0.276	769	0.27	14250	X-RAY DIFFRACTION	15019
3.707-3.8568	0.274	733	0.264	13683	X-RAY DIFFRACTION	14416
3.857-4.0266	0.28	687	0.259	13124	X-RAY DIFFRACTION	13811
4.027-4.2211	0.265	653	0.241	12566	X-RAY DIFFRACTION	13219
4.221-4.4467	0.263	626	0.236	11954	X-RAY DIFFRACTION	12580
4.447-4.7128	0.255	598	0.236	11277	X-RAY DIFFRACTION	11875
4.713-5.0332	0.264	550	0.245	10680	X-RAY DIFFRACTION	11230
5.033-5.4294	0.28	514	0.27	10069	X-RAY DIFFRACTION	10583
5.429-5.9368	0.331	528	0.302	9273	X-RAY DIFFRACTION	9801
5.937-6.6195	0.299	446	0.288	8461	X-RAY DIFFRACTION	8907
6.619-7.6091	0.239	382	0.236	7564	X-RAY DIFFRACTION	7946
7.609-9.2367	0.21	334	0.19	6458	X-RAY DIFFRACTION	6792
9.237-12.7303	0.207	266	0.188	5119	X-RAY DIFFRACTION	5385
12.73-40.161	0.387	158	0.39	3145	X-RAY DIFFRACTION	3303

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	3.3332	-1.2649	-0.203	3.7919	-0.4213	0.4012	-0.044	0.1124	-0.0066	0.0774	0.0797	0.072	0.0224	-0.1304	-0.0357	0.031	-0.0172	0.0142	0.1454	-0.0852	0.3066	33.305	-53.258	-12.183
2	9.0929	4.2927	-0.1763	7.9514	0.6292	2.1303	-0.6108	1.0533	-0.0172	-0.9805	0.4906	-0.5673	-0.389	-0.068	0.1203	0.3387	-0.0025	0.031	0.4178	-0.0423	0.749	30.11	-34.433	-31.146
3	9.948	0.6915	-3.4614	10.5316	-1.9614	30.0954	-0.2109	0.0842	0.7954	0.251	-0.0713	0.0343	1.3075	1.8162	0.2821	1.5571	-0.1079	0.302	1.4885	-0.5115	0.9637	37.599	-36.976	-61.849
4	5.5315	-0.3117	0.1902	1.7293	-0.2855	0.87	-0.0254	-0.0174	-0.1	-0.0434	-0.0921	0.4465	0.201	-0.1765	0.1175	0.0869	-0.0387	0.046	0.1093	-0.1297	0.5642	51.67	-88.664	-12.35
5	-1.0346	-2.6355	-1.5443	14.5742	-2.8493	5.7639	0.2562	0.8137	0.2916	-1.5434	-0.1397	0.2667	-0.424	-0.5178	-0.1165	0.3	0.0289	0.0179	0.7893	-0.0257	1.2911	34.765	-79.575	-31.186
6	5.8211	0.5983	-5.3977	8.7262	-5.6397	32.2165	0.0837	-0.5159	-0.0867	-0.0104	-0.3072	0.0744	0.4742	1.7717	0.2236	1.5256	0.0902	0.2343	1.7299	-0.0421	1.2016	41.364	-75.303	-61.991
7	3.7937	1.2523	0.146	3.322	-0.1269	0.5597	0.0304	0.014	-0.0678	-0.0035	-0.0935	0.4015	0.1827	0.0483	0.0632	0.1085	0.0107	0.0448	0.0831	-0.0116	0.1746	90.981	-96.174	-12.481
8	7.8617	-5.4507	-0.9346	6.8699	-0.8277	4.8391	0.4677	1.3254	0.2904	-1.0089	-0.2679	0.4797	-0.1175	-0.7522	-0.1997	0.5188	-0.0869	-0.0836	0.4619	0.0764	0.8508	73.2098	-103.6973	-31.2985
9	12.7605	-1.2768	-0.0997	8.1553	-6.194	31.7632	-0.1115	-0.115	-0.2765	0.6429	0.3226	0.4714	-2.2051	0.2062	-0.2111	1.5272	0.0514	0.1409	1.3873	0.2671	0.9121	73.999	-95.691	-61.975
10	2.3713	-0.1279	0.0312	3.7304	0.2111	0.3781	-0.0226	0.1136	-0.0337	0.0662	0.053	-0.0018	-0.0039	0.1142	-0.0304	0.0458	-0.0159	0.0096	0.1856	0.0875	0.3782	121.357	-70.187	-12.221
11	11.1012	3.3951	-0.0832	3.9926	-0.279	3.2352	-0.2709	1.3311	0.0984	-0.5552	0.2712	0.5786	0.3985	-0.1262	-0.0003	0.3235	-0.0066	-0.0234	0.417	0.0544	0.7847	116.035	-88.569	-31.121
12	12.4554	6.1087	8.5165	13.6758	-0.3711	35.4028	0.0923	-0.395	-0.2157	0.784	-0.9424	0.9513	-1.8031	-1.1894	0.8501	1.4886	-0.1034	0.2829	1.4494	0.4036	0.9396	110.369	-83.031	-61.882
13	4.9742	-0.8188	0.0005	3.5768	0.3071	0.3579	-0.0757	-0.0388	0.2895	0.0133	-0.0054	-0.5499	-0.0977	0.2127	0.0811	0.0813	-0.0669	-0.0482	0.2206	0.175	0.8785	120.268	-30.228	-12.362
14	0.5264	3.1226	0.9361	11.3076	0.4116	4.3286	-0.2356	0.7304	-0.3732	-1.4921	0.0262	-0.1724	0.409	0.2579	0.2094	0.4227	0.1358	-0.0543	0.7507	0.0825	1.4495	131.418	-45.906	-31.158
15	5.5872	-0.6616	6.6677	10.1974	3.813	36.0522	-0.4529	-0.4101	-0.2484	0.038	0.1848	-0.4911	-1.2207	-1.8669	0.2681	1.485	0.0093	-0.1967	1.7503	0.3924	1.2178	123.499	-46.803	-61.872
16	4.2368	0.6671	-0.065	3.5211	0.5966	0.9227	-0.0104	0.0262	0.2296	-0.0797	-0.07	-0.679	-0.3126	0.0946	0.0805	0.1916	-0.0341	-0.0916	0.1042	0.0955	0.8664	88.207	-6.219	-12.548
17	8.6149	-6.7224	0.4676	8.8281	-1.5287	3.364	0.831	1.8459	-0.732	-1.5887	-0.7059	-0.2794	0.5009	0.5969	-0.1251	0.7976	-0.2106	0.0696	0.9893	-0.1666	1.6023	107.531	-7.014	-31.308
18	9.0743	-1.0308	2.1281	9.2047	4.4606	32.5551	0.3603	-0.5514	0.6563	0.9145	0.2966	-0.7441	1.4729	-1.2712	-0.6569	1.7006	-0.0255	-0.248	1.6772	-0.0152	1.3232	103.294	-13.77	-62.142
19	2.3741	0.9727	-0.0824	3.8197	-0.2595	0.4044	0.0081	0.0803	0.2253	0.0409	-0.1013	-0.1354	-0.1352	-0.0466	0.0932	0.1144	0.0195	-0.0472	0.0919	-0.0543	0.3919	49.371	-16.637	-12.608
20	10.0565	-1.2156	-0.3916	4.445	1.9382	4.4246	0.0972	1.3679	0.0071	-0.7214	0.0842	-0.7814	-0.1782	0.67	-0.1814	0.7045	-0.052	0.1398	0.4233	0.0053	0.8778	62.098	-2.171	-31.513
21	8.87	-0.3091	-3.2387	5.9979	2.9684	33.6042	0.1246	-0.4254	0.5922	0.349	0.1615	-0.112	2.3089	0.2713	-0.2861	1.5893	-0.0484	0.0249	1.4924	-0.312	1.256	64.975	-9.715	-62.11
22	4.1729	0.3602	0.1822	5.8126	0.3855	1.374	-0.0135	0.025	-0.3899	-0.0537	0.0735	0.6445	0.0771	-0.2111	-0.06	0.0618	-0.0187	0.06	0.1336	0.0224	0.4483	40.693	-76.272	19.689
23	6.4048	-2.5272	5.3268	4.6858	-3.0182	8.2574	0.6896	-0.2694	-0.1795	0.4872	-0.3669	-0.2034	1.1715	0.1902	-0.3226	0.8639	-0.2275	0.0306	0.7079	0.0466	0.8237	38.669	-93.156	44.548
24	8.1888	1.9137	0.3863	10.5966	-0.0018	7.5985	-0.1727	-0.1215	1.2127	0.4697	-0.0053	0.744	-0.3995	-0.1587	0.1779	0.9425	-0.0163	-0.2162	0.8399	-0.0309	0.9032	40.859	-70.807	59.465
25	4.4663	-1.5336	-0.4622	5.7935	0.7366	0.9803	0.1458	0.0804	-0.2901	-0.0612	-0.1296	0.2028	0.0809	-0.0918	-0.0162	0.0716	0.0087	-0.002	0.1043	0.0208	0.1018	74.373	-96.971	19.672
26	4.3686	0.9116	3.3957	3.0308	3.8363	8.2866	-0.2461	-0.335	0.2234	0.8529	0.5056	-0.2768	0.4631	1.0443	-0.2595	0.884	0.1178	-0.0242	0.6879	0.0984	0.5253	86.4878	-109.2748	44.5518
27	9.905	-2.9739	-0.9633	9.7424	0.2272	6.1658	-0.5253	-0.9384	0.842	0.5496	0.6145	0.7092	0.0013	-0.3446	-0.0892	1.0445	0.1308	-0.0663	1.0523	-0.0276	0.4428	70.075	-94.093	59.412
28	9.0805	-0.0027	-0.6297	2.839	-0.0759	0.5736	-0.1187	0.1598	-0.3369	0.005	0.0877	-0.283	0.0898	0.0431	0.031	0.0729	-0.0005	-0.0088	0.1482	-0.0189	0.2301	111.819	-83.708	19.784
29	3.8762	-0.4076	1.2542	9.3069	7.4053	11.0803	-0.0986	-1.0681	0.4149	0.1476	0.1002	-0.1947	-0.8693	0.7784	-0.0016	0.5364	0.0392	0.0436	1.0694	0.0522	0.799	128.371	-82.038	44.871
30	15.5534	-3.9817	-0.0832	8.7347	-0.2879	5.9814	0.6136	-1.7029	0.5492	0.9267	-0.9163	1.724	0.3984	0.0693	0.3028	0.9105	-0.1878	0.0396	1.4125	-0.385	0.6329	106.272	-85.176	59.67
31	5.1749	1.9848	-0.5596	6.3335	-0.7978	1.4058	-0.0211	-0.0591	0.0843	-0.0971	-0.0927	-0.965	-0.05	0.3011	0.1138	0.0717	-0.0209	-0.075	0.2075	0.0245	0.7344	124.698	-45.953	19.706
32	6.5473	-3.3274	-5.2824	1.281	5.2509	10.9264	0.852	-0.7691	0.3634	0.255	-0.776	-0.4992	-1.6833	0.5803	-0.076	0.9736	-0.5648	-0.1791	1.0889	0.0859	1.2328	133.323	-31.863	44.651
33	12.2497	1.7369	-0.8955	8.1468	-0.8402	8.3397	-0.1541	-0.1904	-1.3474	0.9222	-0.1635	0.314	0.2126	0.4564	0.3176	0.9789	-0.2919	0.1452	1.021	-0.1378	1.0317	121.674	-51.105	59.365
34	5.3171	-1.605	0.2053	7.1434	-1.1793	1.8068	0.1821	0.167	0.848	-0.0664	-0.3642	-0.7958	-0.3494	0.2126	0.1821	0.1697	-0.0321	-0.057	0.1711	0.0038	0.8194	103.294	-12.379	19.843
35	2.8014	-0.8841	-5.0337	4.3548	1.4696	6.6952	0.0964	-0.0704	0.7106	1.1342	-0.0147	0.2412	-0.6135	-0.6901	-0.0817	1.7333	-0.1175	-0.0764	0.7621	-0.1204	1.2528	97.078	3.535	44.649
36	8.6061	-1.22	-1.1319	10.4003	-0.3141	6.9205	-0.3931	-0.5793	-0.3811	0.9011	0.3678	-0.6457	-0.4866	0.3362	0.0253	1.7034	-0.1525	0.0133	0.8641	-0.0323	0.8222	104.837	-17.741	59.177
37	6.1374	-2.0672	1.4372	6.6541	-0.8661	0.8378	0.0112	0.3945	0.2632	0.1379	-0.0579	-0.2343	-0.1035	0.1122	0.0467	0.1038	-0.0184	0.0031	0.1196	-0.0032	0.2255	63.757	-8.535	19.676
38	4.6048	-0.0791	-3.3902	2.0672	-3.3163	8.3492	-0.3417	-0.7758	-0.3896	1.3589	0.6985	0.3111	-0.1369	-1.0225	-0.3568	1.3209	0.1502	0.0578	0.8298	0.0314	0.5887	47.129	-2.962	44.532
39	14.6161	-5.2244	1.7965	10.1184	-0.7757	6.9315	-0.2847	-1.3131	-0.7463	0.5008	0.291	-1.72	-0.6116	0.0573	-0.0063	1.5579	0.0016	0.0338	1.1604	0.0788	0.4235	68.497	-9.465	59.393
40	7.6358	1.9398	0.5856	3.9441	0.6096	0.5944	-0.235	0.1056	0.4887	-0.1314	0.1767	0.3899	-0.0913	-0.0947	0.0583	0.1164	0.0011	-0.0094	0.1283	0.0156	0.3284	35.884	-36.796	19.814
41	0.1672	-2.2186	0.8738	9.2758	-4.3511	9.8736	0.0414	-1.1287	-0.5076	0.4167	0.0502	-0.4091	0.7728	-0.2852	-0.0916	0.592	-0.024	-0.114	1.0938	-0.0856	0.9597	21.598	-45.66	44.935
42	14.3154	1.72	-1.2941	6.2779	0.2076	5.7897	1.0394	-0.9308	0.1236	1.105	-1.2676	-1.3256	-0.8299	0.4027	0.2282	1.2941	-0.3006	-0.3551	1.2725	0.3012	0.7307	40.049	-33.336	59.703
43	19.9614	9.7968	-4.8108	11.7911	-2.9313	16.1372	0.4956	-1.4968	1.4726	0.9433	-0.0351	1.0207	-0.4943	0.3609	-0.4605	1.4006	0.0622	0.0544	1.3395	-0.2589	0.7148	65.368	-29.023	-97.43
44	10.7101	1.5443	-1.3182	22.3128	-7.864	12.8562	0.2047	-1.2996	-0.4062	1.432	0.281	1.0311	-0.9957	-0.4901	-0.4858	1.2552	0.0222	0.0729	1.3363	-0.1902	0.6947	52.89	-48.262	-97.342
45	14.7286	-5.7324	4.4108	15.4786	-8.0057	19.2549	0.2928	-1.9365	-0.8124	0.9996	0.2806	0.8912	-0.3738	-0.0784	-0.5733	1.2592	0.0148	0.0282	1.2982	-0.026	0.6091	60.051	-70.169	-97.459
46	18.9067	-0.536	7.7191	10.1314	-2.0938	19.6694	0.1061	-1.5454	-1.0542	1.118	0.4708	-0.4194	-0.0619	-0.7492	-0.5769	1.4907	0.0716	0.0741	1.3048	0.1679	0.4047	81.653	-78.075	-97.503
47	15.6606	8.5336	6.0094	17.7773	8.6253	17.1183	0.64	-1.8613	-0.545	1.0675	-0.2279	-1.1774	0.7889	-0.3312	-0.4121	1.321	0.0724	-0.0567	1.2525	0.2717	0.6022	101.19	-66.172	-97.394
48	7.8653	-3.9907	-2.5253	20.9209	8.2986	18.4805	0.022	-1.148	0.6652	1.6478	0.9464	-1.2879	0.7166	0.8255	-0.9684	1.3602	0.0046	-0.0167	1.3531	0.0536	0.7359	104.219	-43.396	-97.588

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	2 - 135
2	X-RAY DIFFRACTION	1	A	410 - 525
3	X-RAY DIFFRACTION	2	A	136 - 190
4	X-RAY DIFFRACTION	2	A	375 - 409
5	X-RAY DIFFRACTION	3	A	191 - 374
6	X-RAY DIFFRACTION	4	B	2 - 135
7	X-RAY DIFFRACTION	4	B	410 - 525
8	X-RAY DIFFRACTION	5	B	136 - 190
9	X-RAY DIFFRACTION	5	B	375 - 409
10	X-RAY DIFFRACTION	6	B	191 - 374
11	X-RAY DIFFRACTION	7	C	2 - 135
12	X-RAY DIFFRACTION	7	C	410 - 525
13	X-RAY DIFFRACTION	8	C	136 - 190
14	X-RAY DIFFRACTION	8	C	375 - 409
15	X-RAY DIFFRACTION	9	C	191 - 374
16	X-RAY DIFFRACTION	10	D	2 - 135
17	X-RAY DIFFRACTION	10	D	410 - 525
18	X-RAY DIFFRACTION	11	D	136 - 190
19	X-RAY DIFFRACTION	11	D	375 - 409
20	X-RAY DIFFRACTION	12	D	191 - 374
21	X-RAY DIFFRACTION	13	E	2 - 135
22	X-RAY DIFFRACTION	13	E	410 - 525
23	X-RAY DIFFRACTION	14	E	136 - 190
24	X-RAY DIFFRACTION	14	E	375 - 409
25	X-RAY DIFFRACTION	15	E	191 - 374
26	X-RAY DIFFRACTION	16	F	2 - 135
27	X-RAY DIFFRACTION	16	F	410 - 525
28	X-RAY DIFFRACTION	17	F	136 - 190
29	X-RAY DIFFRACTION	17	F	375 - 409
30	X-RAY DIFFRACTION	18	F	191 - 374
31	X-RAY DIFFRACTION	19	G	2 - 135
32	X-RAY DIFFRACTION	19	G	410 - 525
33	X-RAY DIFFRACTION	20	G	136 - 190
34	X-RAY DIFFRACTION	20	G	375 - 409
35	X-RAY DIFFRACTION	21	G	191 - 374
36	X-RAY DIFFRACTION	22	H	2 - 135
37	X-RAY DIFFRACTION	22	H	410 - 525
38	X-RAY DIFFRACTION	23	H	136 - 190
39	X-RAY DIFFRACTION	23	H	375 - 409
40	X-RAY DIFFRACTION	24	H	191 - 374
41	X-RAY DIFFRACTION	25	I	2 - 135
42	X-RAY DIFFRACTION	25	I	410 - 525
43	X-RAY DIFFRACTION	26	I	136 - 190
44	X-RAY DIFFRACTION	26	I	375 - 409
45	X-RAY DIFFRACTION	27	I	191 - 374
46	X-RAY DIFFRACTION	28	J	2 - 135
47	X-RAY DIFFRACTION	28	J	410 - 525
48	X-RAY DIFFRACTION	29	J	136 - 190
49	X-RAY DIFFRACTION	29	J	375 - 409
50	X-RAY DIFFRACTION	30	J	191 - 374
51	X-RAY DIFFRACTION	31	K	2 - 135
52	X-RAY DIFFRACTION	31	K	410 - 525
53	X-RAY DIFFRACTION	32	K	136 - 190
54	X-RAY DIFFRACTION	32	K	375 - 409
55	X-RAY DIFFRACTION	33	K	191 - 374
56	X-RAY DIFFRACTION	34	L	2 - 135
57	X-RAY DIFFRACTION	34	L	410 - 525
58	X-RAY DIFFRACTION	35	L	136 - 190
59	X-RAY DIFFRACTION	35	L	375 - 409
60	X-RAY DIFFRACTION	36	L	191 - 374
61	X-RAY DIFFRACTION	37	M	2 - 135
62	X-RAY DIFFRACTION	37	M	410 - 525
63	X-RAY DIFFRACTION	38	M	136 - 190
64	X-RAY DIFFRACTION	38	M	375 - 409
65	X-RAY DIFFRACTION	39	M	191 - 374
66	X-RAY DIFFRACTION	40	N	2 - 135
67	X-RAY DIFFRACTION	40	N	410 - 525
68	X-RAY DIFFRACTION	41	N	136 - 190
69	X-RAY DIFFRACTION	41	N	375 - 409
70	X-RAY DIFFRACTION	42	N	191 - 374
71	X-RAY DIFFRACTION	43	O	1 - 97
72	X-RAY DIFFRACTION	44	P	1 - 97
73	X-RAY DIFFRACTION	45	Q	1 - 97
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75	X-RAY DIFFRACTION	47	S	1 - 97
76	X-RAY DIFFRACTION	48	T	1 - 97

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