PDB-2qc8: Crystal structure of human glutamine synthetase in complex with A...

ID or keywords:

Entry

Database: PDB / ID: 2qc8

Title

Crystal structure of human glutamine synthetase in complex with ADP and methionine sulfoximine phosphate

Components

Glutamine synthetase

Keywords

LIGASE / Amino-acid biosynthesis / Synthetase /

Structural Genomics /

Structural Genomics Consortium / SGC

Function / homology

Function and homology information

protein S-acyltransferase / Astrocytic Glutamate-Glutamine Uptake And Metabolism / protein palmitoylation / protein-cysteine S-palmitoyltransferase activity / regulation of protein localization to nucleolus /

regulation of sprouting angiogenesis / regulation of endothelial cell migration / glutamate catabolic process /

glutamine synthetase / glutamine biosynthetic process ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.6 Å

Authors

Karlberg, T. / Lehtio, L. / Arrowsmith, C.H. / Berglund, H. / Busam, R.D. / Collins, R. / Dahlgren, L.G. / Edwards, A. / Flodin, S. / Flores, A. ...

Citation

Journal: J.Mol.Biol. / Year: 2008
Title: Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
Authors: Krajewski, W.W. / Collins, R. / Holmberg-Schiavone, L. / Jones, T.A. / Karlberg, T. / Mowbray, S.L.

History

Deposition	Jun 19, 2007	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jul 3, 2007	Provider: repository / Type: Initial release
Revision 1.1	Nov 20, 2007	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.3	Aug 30, 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 / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / 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_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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_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_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ref_seq_dif.details / _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

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qc/2qc8 ftp://data.pdbj.org/pub/pdb/validation_reports/qc/2qc8	HTTPS FTP

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Related structure data

Related structure data	2ojwSC 2uu7C S: Starting model for refinement C: citing same article (ref.)
Similar structure data	2uu7-2 2uu7-1 2d3c-d 2d3a-d 2d3b-d 2ojw-1 4bax-d 4ghb-1 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	#30 - Jun 2002 Glutamine Synthetase similarity (12)

Deposited unit

A: Glutamine synthetase

B: Glutamine synthetase

C: Glutamine synthetase

D: Glutamine synthetase

E: Glutamine synthetase

F: Glutamine synthetase

G: Glutamine synthetase

H: Glutamine synthetase

I: Glutamine synthetase

J: Glutamine synthetase

hetero molecules

443 kDa, 10 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author

Unit cell

Length a, b, c (Å)	181.210, 126.080, 188.170
Angle α, β, γ (deg.)	90.00, 92.14, 90.00
Int Tables number	5
Space group name H-M	C121

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
3	1	C
4	1	D
5	1	E
6	1	F
7	1	G
8	1	H
9	1	I
10	1	J

NCS domain segments:

Ens-ID: 1

Dom-ID	Component-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	ASN	ASN	VAL	VAL	3	A	A	10 - 54	29 - 73
2	1	ASN	ASN	VAL	VAL	3	B	B	10 - 54	29 - 73
3	1	ASN	ASN	VAL	VAL	3	C	C	10 - 54	29 - 73
4	1	ASN	ASN	VAL	VAL	3	D	D	10 - 54	29 - 73
5	1	ASN	ASN	VAL	VAL	3	E	E	10 - 54	29 - 73
6	1	ASN	ASN	VAL	VAL	3	F	F	10 - 54	29 - 73
7	1	ASN	ASN	VAL	VAL	3	G	G	10 - 54	29 - 73
8	1	ASN	ASN	VAL	VAL	3	H	H	10 - 54	29 - 73
9	1	ASN	ASN	VAL	VAL	3	I	I	10 - 54	29 - 73
10	1	ASN	ASN	VAL	VAL	3	J	J	10 - 54	29 - 73
1	2	GLU	GLU	ARG	ARG	3	A	A	56 - 106	75 - 125
2	2	GLU	GLU	ARG	ARG	3	B	B	56 - 106	75 - 125
3	2	GLU	GLU	ARG	ARG	3	C	C	56 - 106	75 - 125
4	2	GLU	GLU	ARG	ARG	3	D	D	56 - 106	75 - 125
5	2	GLU	GLU	ARG	ARG	3	E	E	56 - 106	75 - 125
6	2	GLU	GLU	ARG	ARG	3	F	F	56 - 106	75 - 125
7	2	GLU	GLU	ARG	ARG	3	G	G	56 - 106	75 - 125
8	2	GLU	GLU	ARG	ARG	3	H	H	56 - 106	75 - 125
9	2	GLU	GLU	ARG	ARG	3	I	I	56 - 106	75 - 125
10	2	GLU	GLU	ARG	ARG	3	J	J	56 - 106	75 - 125
1	3	PRO	PRO	ASP	ASP	3	A	A	108 - 122	127 - 141
2	3	PRO	PRO	ASP	ASP	3	B	B	108 - 122	127 - 141
3	3	PRO	PRO	ASP	ASP	3	C	C	108 - 122	127 - 141
4	3	PRO	PRO	ASP	ASP	3	D	D	108 - 122	127 - 141
5	3	PRO	PRO	ASP	ASP	3	E	E	108 - 122	127 - 141
6	3	PRO	PRO	ASP	ASP	3	F	F	108 - 122	127 - 141
7	3	PRO	PRO	ASP	ASP	3	G	G	108 - 122	127 - 141
8	3	PRO	PRO	ASP	ASP	3	H	H	108 - 122	127 - 141
9	3	PRO	PRO	ASP	ASP	3	I	I	108 - 122	127 - 141
10	3	PRO	PRO	ASP	ASP	3	J	J	108 - 122	127 - 141
1	4	VAL	VAL	HIS	HIS	3	A	A	124 - 281	143 - 300
2	4	VAL	VAL	HIS	HIS	3	B	B	124 - 281	143 - 300
3	4	VAL	VAL	HIS	HIS	3	C	C	124 - 281	143 - 300
4	4	VAL	VAL	HIS	HIS	3	D	D	124 - 281	143 - 300
5	4	VAL	VAL	HIS	HIS	3	E	E	124 - 281	143 - 300
6	4	VAL	VAL	HIS	HIS	3	F	F	124 - 281	143 - 300
7	4	VAL	VAL	HIS	HIS	3	G	G	124 - 281	143 - 300
8	4	VAL	VAL	HIS	HIS	3	H	H	124 - 281	143 - 300
9	4	VAL	VAL	HIS	HIS	3	I	I	124 - 281	143 - 300
10	4	VAL	VAL	HIS	HIS	3	J	J	124 - 281	143 - 300
1	5	TYR	TYR	ASN	ASN	3	A	A	283 - 310	302 - 329
2	5	TYR	TYR	ASN	ASN	3	B	B	283 - 310	302 - 329
3	5	TYR	TYR	ASN	ASN	3	C	C	283 - 310	302 - 329
4	5	TYR	TYR	ASN	ASN	3	D	D	283 - 310	302 - 329
5	5	TYR	TYR	ASN	ASN	3	E	E	283 - 310	302 - 329
6	5	TYR	TYR	ASN	ASN	3	F	F	283 - 310	302 - 329
7	5	TYR	TYR	ASN	ASN	3	G	G	283 - 310	302 - 329
8	5	TYR	TYR	ASN	ASN	3	H	H	283 - 310	302 - 329
9	5	TYR	TYR	ASN	ASN	3	I	I	283 - 310	302 - 329
10	5	TYR	TYR	ASN	ASN	3	J	J	283 - 310	302 - 329
1	6	PHE	PHE	GLY	GLY	4	A	A	312 - 365	331 - 384
2	6	PHE	PHE	GLY	GLY	4	B	B	312 - 365	331 - 384
3	6	PHE	PHE	GLY	GLY	4	C	C	312 - 365	331 - 384
4	6	PHE	PHE	GLY	GLY	4	D	D	312 - 365	331 - 384
5	6	PHE	PHE	THR	THR	4	E	E	312 - 364	331 - 383
6	6	PHE	PHE	GLY	GLY	4	F	F	312 - 365	331 - 384
7	6	PHE	PHE	GLY	GLY	4	G	G	312 - 365	331 - 384
8	6	PHE	PHE	GLY	GLY	4	H	H	312 - 365	331 - 384
9	6	PHE	PHE	GLY	GLY	4	I	I	312 - 365	331 - 384
10	6	PHE	PHE	GLY	GLY	4	J	J	312 - 365	331 - 384

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Protein , 1 types, 10 molecules ABCDEFGHIJ

#1: Protein	Glutamine synthetase / / Glutamate-ammonia ligase / GS Mass: 43364.773 Da / Num. of mol.: 10 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GLUL, GLNS / Plasmid: pNIC-Bsa4 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)gold pRARE2 / References: UniProt: P15104, glutamine synthetase

#1: Protein

Glutamine synthetase /

/ Glutamate-ammonia ligase / GS

Mass: 43364.773 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Homo sapiens (human) / Gene: GLUL, GLNS / Plasmid: pNIC-Bsa4 / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21(DE3)gold pRARE2 / References: UniProt: P15104,

glutamine synthetase

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Non-polymers , 5 types, 291 molecules

#2: Chemical	... ChemComp-MN / MANGANESE (II) ION Mass: 54.938 Da / Num. of mol.: 30 / Source method: obtained synthetically / Formula: Mn
#3: Chemical	ChemComp-CL / CHLORIDE ION / Chloride Mass: 35.453 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Cl
#4: Chemical	ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate Mass: 427.201 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C₁₀H₁₅N₅O₁₀P₂ / Comment: ADP, energy-carrying molecule*YM
#5: Chemical	ChemComp-P3S / L-METHIONINE-S-SULFOXIMINE PHOSPHATE Mass: 260.205 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C₅H₁₃N₂O₆PS
#6: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 231 / 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: 2.48 Å³/Da / Density % sol: 50.31 %
Crystal grow	Temperature: 298 K / pH: 7 Details: 1.1M Sodium malonate, 0.5% Jeffamine ED-2001, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K, pH 7.00

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.00595
Detector	Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 1, 2007
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.00595 Å / Relative weight: 1
Reflection	Resolution: 2.6→40 Å / Num. obs: 129787 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 7.5 % / R_merge(I) obs: 0.12 / R_sym value: 0.092 / Net I/σ(I): 15.6
Reflection shell	Resolution: 2.6→2.7 Å / Redundancy: 7.2 % / R_merge(I) obs: 0.526 / Mean I/σ(I) obs: 4.1 / R_sym value: 0.324 / % possible all: 100

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Processing

Software

Name	Version	Classification
REFMAC	5.3.0032	refinement
XDS		data reduction
XSCALE		data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2OJW

2ojw

Resolution: 2.6→39.94 Å / Cor.coef. F_o:F_c: 0.951 / Cor.coef. F_o:F_c free: 0.916 / SU B: 17.298 / SU ML: 0.187 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.827 / ESU R Free: 0.277 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.217	6497	5 %	RANDOM
R_work	0.166	-	-	-
obs	0.168	123433	100 %	-

Solvent computation

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

Displacement parameters

B_iso mean: 37.49 Å²

	B_aniso -1	B_aniso -2
1-	0 Å²	0 Å²
2-	-	0 Å²
3-	-	-

Refinement step

Cycle: LAST / Resolution: 2.6→39.94 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	28146	0	460	231	28837

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.015	0.022	29330
X-RAY DIFFRACTION	r_bond_other_d	0.002	0.02	20417
X-RAY DIFFRACTION	r_angle_refined_deg	1.592	1.959	39745
X-RAY DIFFRACTION	r_angle_other_deg	0.943	3	49193
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	11.089	5	3549
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	37.616	23.403	1440
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.998	15	4740
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	16.467	15	240
X-RAY DIFFRACTION	r_chiral_restr	0.1	0.2	4020
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.02	32893
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	6259
X-RAY DIFFRACTION	r_nbd_refined	0.213	0.2	6220
X-RAY DIFFRACTION	r_nbd_other	0.202	0.2	21699
X-RAY DIFFRACTION	r_nbtor_refined	0.186	0.2	14173
X-RAY DIFFRACTION	r_nbtor_other	0.086	0.2	15102
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.141	0.2	874
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.438	0.2	32
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.293	0.2	42
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.087	0.2	2
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	0.72	1.5	22600
X-RAY DIFFRACTION	r_mcbond_other	0.133	1.5	7237
X-RAY DIFFRACTION	r_mcangle_it	0.893	2	28445
X-RAY DIFFRACTION	r_scbond_it	1.491	3	13824
X-RAY DIFFRACTION	r_scangle_it	2.178	4.5	11300
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	1732	tight positional	0.13	0.05
2	B	1732	tight positional	0.13	0
3	C	1732	tight positional	0.11	0
4	D	1732	tight positional	0.12	0
5	E	1732	tight positional	0.12	0
6	F	1732	tight positional	0.12	0
7	G	1732	tight positional	0.12	0
8	H	1732	tight positional	0.12	0
9	I	1732	tight positional	0.12	0
10	J	1732	tight positional	0.12	0
1	A	713	medium positional	0.16	0.5
2	B	713	medium positional	0.18	0
3	C	713	medium positional	0.15	0
4	D	713	medium positional	0.14	0
5	E	713	medium positional	0.14	0
6	F	713	medium positional	0.15	0
7	G	713	medium positional	0.17	0
8	H	713	medium positional	0.17	0
9	I	713	medium positional	0.14	0
10	J	713	medium positional	0.15	0
1	A	2309	loose positional	0.19	5
2	B	2309	loose positional	0.24	0
3	C	2309	loose positional	0.18	0
4	D	2309	loose positional	0.18	0
5	E	2309	loose positional	0.19	0
6	F	2309	loose positional	0.2	0
7	G	2309	loose positional	0.19	0
8	H	2309	loose positional	0.18	0
9	I	2309	loose positional	0.24	0
10	J	2309	loose positional	0.21	0
1	A	1732	tight thermal	0.42	0.5
2	B	1732	tight thermal	0.47	0
3	C	1732	tight thermal	0.48	0
4	D	1732	tight thermal	0.42	0
5	E	1732	tight thermal	0.42	0
6	F	1732	tight thermal	0.33	0
7	G	1732	tight thermal	0.31	0
8	H	1732	tight thermal	0.35	0
9	I	1732	tight thermal	0.35	0
10	J	1732	tight thermal	0.3	0
1	A	713	medium thermal	0.46	2
2	B	713	medium thermal	0.53	0
3	C	713	medium thermal	0.55	0
4	D	713	medium thermal	0.48	0
5	E	713	medium thermal	0.48	0
6	F	713	medium thermal	0.31	0
7	G	713	medium thermal	0.34	0
8	H	713	medium thermal	0.35	0
9	I	713	medium thermal	0.35	0
10	J	713	medium thermal	0.4	0
1	A	2309	loose thermal	0.59	10
2	B	2309	loose thermal	0.65	0
3	C	2309	loose thermal	0.68	0
4	D	2309	loose thermal	0.61	0
5	E	2309	loose thermal	0.62	0
6	F	2309	loose thermal	0.47	0
7	G	2309	loose thermal	0.46	0
8	H	2309	loose thermal	0.48	0
9	I	2309	loose thermal	0.48	0
10	J	2309	loose thermal	0.47	0

LS refinement shell

Resolution: 2.6→2.67 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.3	479	-
R_work	0.239	9094	-
obs	-	-	100 %

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	0.9585	-0.0431	0.2733	0.3036	-0.0974	0.2482	-0.0257	0.0644	0.2027	-0.029	0.0195	0.0432	-0.041	0.002	0.0061	-0.1653	-0.0168	0.0164	-0.0739	0.0097	0.0341	-48.755	33.908	-23.587
2	0.5004	0.1297	0.1294	0.7758	-0.0167	0.0369	0.017	0.0457	-0.002	-0.0239	-0.026	0.0394	0.0199	-0.0287	0.009	-0.244	-0.018	0.0048	-0.0331	0.0026	-0.0815	-18.379	9.749	-15.807
3	0.8924	0.1045	0.0974	0.3287	-0.0228	0.1064	-0.0173	0.0641	-0.0864	-0.0244	0.0305	-0.0077	-0.0351	-0.0084	-0.0132	-0.2313	0.0065	0.0175	-0.0844	0.0109	-0.0434	-31.066	-27.392	-19.116
4	0.6912	-0.214	0.0776	0.7057	-0.1192	0.0376	0.0075	0.0872	-0.0726	-0.0776	0.0203	0.0347	-0.0265	0.0052	-0.0278	-0.2306	-0.0215	0.0105	-0.0413	-0.0041	-0.0338	-69.144	-26.438	-29.135
5	0.869	0.2816	0.0847	0.7916	0.1296	0.0479	-0.018	0.0447	0.0973	-0.0893	0.0127	0.0827	-0.0156	0.0466	0.0053	-0.2145	0.0291	-0.0063	-0.0313	0.0307	-0.0161	-80.174	11.226	-31.725
6	1.1111	0.0073	0.2731	0.5265	-0.2223	0.606	-0.0675	0.2535	0.294	-0.0712	-0.0002	-0.1398	-0.2707	0.0446	0.0676	0.101	-0.0653	0.0042	0.1993	0.1728	0.0965	-34.087	33.892	-69.309
7	0.4974	0.0339	-0.0762	1.0235	-0.1036	0.3643	0.0143	0.287	0.1104	-0.1604	0.0163	0.179	-0.0106	-0.2341	-0.0306	-0.0136	-0.0172	-0.0566	0.4316	0.1059	0.0212	-67.126	14.135	-78.01
8	0.986	-0.2243	0.0219	0.7083	-0.1679	0.4044	-0.0971	0.3292	-0.1996	-0.1889	0.0811	0.1504	0.1821	-0.1158	0.016	0.098	-0.1232	0.0328	0.3118	-0.123	0.0359	-59.075	-24.56	-76.132
9	0.8991	0.4373	-0.0439	0.8823	0.0347	0.4542	-0.0867	0.1315	-0.2759	-0.2134	-0.02	-0.2612	0.1689	0.1802	0.1068	0.0232	0.0717	0.1654	0.2653	-0.0415	0.1457	-21.19	-28.667	-66.077
10	0.6677	-0.1474	0.0336	1.2717	-0.2846	0.4455	-0.0058	0.1969	0.0752	-0.0911	-0.1245	-0.3904	-0.0739	0.2708	0.1304	-0.0989	-0.0835	0.0791	0.3741	0.1256	0.1743	-5.572	7.412	-62.003

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	X-RAY DIFFRACTION	1	A	A	10 - 365	29 - 384
2	X-RAY DIFFRACTION	2	B	B	10 - 365	29 - 384
3	X-RAY DIFFRACTION	3	C	C	10 - 365	29 - 384
4	X-RAY DIFFRACTION	4	D	D	10 - 365	29 - 384
5	X-RAY DIFFRACTION	5	E	E	10 - 364	29 - 383
6	X-RAY DIFFRACTION	6	F	F	10 - 365	29 - 384
7	X-RAY DIFFRACTION	7	G	G	10 - 365	29 - 384
8	X-RAY DIFFRACTION	8	H	H	10 - 365	29 - 384
9	X-RAY DIFFRACTION	9	I	I	10 - 365	29 - 384
10	X-RAY DIFFRACTION	10	J	J	10 - 365	29 - 384

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