PDB-2ce7: EDTA treated

ID or keywords:

Entry

Database: PDB / ID: 2ce7

Title

EDTA treated

Components

CELL DIVISION PROTEIN FTSH

Keywords

CELL DIVISION PROTEIN / CELL DIVISION / METALLOPROTEASE / FTSH

Function / homology

Function and homology information

Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / ATP-dependent peptidase activity / protein catabolic process / metalloendopeptidase activity / ATP hydrolysis activity / proteolysis / zinc ion binding / ATP binding / identical protein binding / plasma membrane
Similarity search - Function

Biological species

Thermotoga maritima (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MAD / Resolution: 2.44 Å

Authors

Bieniossek, C. / Baumann, U.

Citation

Journal: Proc.Natl.Acad.Sci.USA / Year: 2006
Title: The Molecular Architecture of the Metalloprotease Ftsh.
Authors: Bieniossek, C. / Schalch, T. / Bumann, M. / Meister, M. / Meier, R. / Baumann, U.

History

Deposition	Feb 3, 2006	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Feb 9, 2006	Provider: repository / Type: Initial release
Revision 1.1	May 8, 2011	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Version format compliance
Revision 1.3	Mar 7, 2018	Group: Source and taxonomy / Category: entity_src_gen Item: _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id ..._entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant
Revision 1.4	May 8, 2024	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2ce7.cif.gz	481.1 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	2ce7_validation.pdf.gz	811.9 KB	Display	wwPDB validaton report
Full document	2ce7_full_validation.pdf.gz	903 KB	Display
Data in XML	2ce7_validation.xml.gz	59.9 KB	Display
Data in CIF	2ce7_validation.cif.gz	89 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ce/2ce7 ftp://data.pdbj.org/pub/pdb/validation_reports/ce/2ce7	HTTPS FTP

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Related structure data

Related structure data	2ceaC C: citing same article (ref.)
Similar structure data	2cea-1 2cea-2 4ww0-1 10216 4z8x-1 5858 6oab-d 6gcn-1 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
Related items in Molecule of the Month	#80 - Aug 2006 AAA+ Proteases similarity (4) #166 - Oct 2013 Proteasome similarity (4) #167 - Nov 2013 SNARE Proteins similarity (4)

Deposited unit

A: CELL DIVISION PROTEIN FTSH

B: CELL DIVISION PROTEIN FTSH

C: CELL DIVISION PROTEIN FTSH

D: CELL DIVISION PROTEIN FTSH

E: CELL DIVISION PROTEIN FTSH

F: CELL DIVISION PROTEIN FTSH

hetero molecules

320 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: CELL DIVISION PROTEIN FTSH

B: CELL DIVISION PROTEIN FTSH

C: CELL DIVISION PROTEIN FTSH

hetero molecules

A: CELL DIVISION PROTEIN FTSH

B: CELL DIVISION PROTEIN FTSH

C: CELL DIVISION PROTEIN FTSH

hetero molecules

defined by author&software
320 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: CELL DIVISION PROTEIN FTSH

E: CELL DIVISION PROTEIN FTSH

F: CELL DIVISION PROTEIN FTSH

hetero molecules

D: CELL DIVISION PROTEIN FTSH

E: CELL DIVISION PROTEIN FTSH

F: CELL DIVISION PROTEIN FTSH

hetero molecules

defined by author&software
320 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	165.092, 165.092, 235.322
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	92
Space group name H-M	P4₁2₁2

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: 1 / Refine code: 3

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	SER	SER	GLY	GLY	A	A	153 - 320	8 - 175
2	1	SER	SER	GLY	GLY	B	B	153 - 320	8 - 175
3	1	SER	SER	GLY	GLY	C	C	153 - 320	8 - 175
4	1	SER	SER	GLY	GLY	D	D	153 - 320	8 - 175
5	1	SER	SER	GLY	GLY	E	E	153 - 320	8 - 175
6	1	SER	SER	GLY	GLY	F	F	153 - 320	8 - 175
1	2	ILE	ILE	ARG	ARG	A	A	326 - 400	181 - 255
2	2	ILE	ILE	ARG	ARG	B	B	326 - 400	181 - 255
3	2	ILE	ILE	ARG	ARG	C	C	326 - 400	181 - 255
4	2	ILE	ILE	ARG	ARG	D	D	326 - 400	181 - 255
5	2	ILE	ILE	ARG	ARG	E	E	326 - 400	181 - 255
6	2	ILE	ILE	ARG	ARG	F	F	326 - 400	181 - 255
1	3	GLU	GLU	GLU	GLU	A	A	416 - 588	271 - 443
2	3	GLU	GLU	GLU	GLU	B	B	416 - 588	271 - 443
3	3	GLU	GLU	GLU	GLU	C	C	416 - 588	271 - 443
4	3	GLU	GLU	GLU	GLU	D	D	416 - 588	271 - 443
5	3	GLU	GLU	GLU	GLU	E	E	416 - 588	271 - 443
6	3	GLU	GLU	GLU	GLU	F	F	416 - 588	271 - 443

NCS ensembles :

ID
1
2
3

#1: Protein	CELL DIVISION PROTEIN FTSH Mass: 52756.414 Da / Num. of mol.: 6 / Fragment: CYTOPLASMIC DOMAIN, RESIDUES 147-610 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Description: ERMAN COLLECTION OF MICROORGANISMS (DSMZ) / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta / References: UniProt: Q9WZ49
#2: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#3: Chemical	ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₁₀H₁₅N₅O₁₀P₂ / Comment: ADP, energy-carrying molecule*YM
#4: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 199 / Source method: isolated from a natural source / Formula: H₂O
Compound details	ENGINEERED RESIDUE IN CHAIN A, LYS 410 TO LEU ENGINEERED RESIDUE IN CHAIN A, LYS 415 TO ALA ...ENGINEERED RESIDUE IN CHAIN A, LYS 410 TO LEU ENGINEERED RESIDUE IN CHAIN A, LYS 415 TO ALA ENGINEERED RESIDUE IN CHAIN B, LYS 410 TO LEU ENGINEERED RESIDUE IN CHAIN B, LYS 415 TO ALA ENGINEERED RESIDUE IN CHAIN C, LYS 410TO LEU ENGINEERED RESIDUE IN CHAIN C, LYS 415 TO ALA ENGINEERED RESIDUE IN CHAIN D, LYS 410 TO LEU ENGINEERED RESIDUE IN CHAIN D, LYS 415 TO ALA ENGINEERED RESIDUE IN CHAIN E, LYS 410 TO LEU ENGINEERED RESIDUE IN CHAIN E, LYS 415 TO ALA ENGINEERED RESIDUE IN CHAIN F, LYS 410 TO LEU ENGINEERED RESIDUE IN CHAIN F, LYS 415 TO ALA

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.8 Å³/Da / Density % sol: 54 %
Crystal grow	pH: 7 / Details: 30% PEG400, 0.2M CACL2, 0.1 M HEPES PH 7.5

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.976
Detector	Type: MARRESEARCH / Detector: CCD / Date: Nov 3, 2005
Radiation	Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.976 Å / Relative weight: 1
Reflection	Resolution: 2.44→40 Å / Num. obs: 120494 / % possible obs: 99.1 % / Observed criterion σ(I): 0 / Redundancy: 5.2 % / R_merge(I) obs: 0.06 / Net I/σ(I): 14.1
Reflection shell	Resolution: 2.44→2.51 Å / Redundancy: 5.2 % / R_merge(I) obs: 0.52 / Mean I/σ(I) obs: 2.9 / % possible all: 97.6

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0019	refinement
XDS		data reduction
XSCALE		data scaling
SHARP		phasing

Refinement

Method to determine structure:

MAD / Resolution: 2.44→25 Å / Cor.coef. F_o:F_c: 0.938 / Cor.coef. F_o:F_c free: 0.93 / SU B: 21.508 / SU ML: 0.242 / Cross valid method: THROUGHOUT / ESU R: 0.381 / ESU R Free: 0.268 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.269	1920	1.6 %	RANDOM
R_work	0.222	-	-	-
obs	0.223	118480	100 %	-

Solvent computation

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

Displacement parameters

B_iso mean: 26.93 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-1.36 Å²	0 Å²	0 Å²
2-	-	-1.36 Å²	0 Å²
3-	-	-	2.72 Å²

Refinement step

Cycle: LAST / Resolution: 2.44→25 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19191	0	174	199	19564

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.014	0.022	19659
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	13726
X-RAY DIFFRACTION	r_angle_refined_deg	1.017	1.997	26485
X-RAY DIFFRACTION	r_angle_other_deg	0.641	3	33467
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.218	5	2439
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	34.56	24.095	884
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	18.939	15	3603
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.618	15	175
X-RAY DIFFRACTION	r_chiral_restr	0.076	0.2	3038
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.02	21515
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	3780
X-RAY DIFFRACTION	r_nbd_refined	0.263	0.2	5151
X-RAY DIFFRACTION	r_nbd_other	0.255	0.2	14959
X-RAY DIFFRACTION	r_nbtor_refined	0.192	0.2	9802
X-RAY DIFFRACTION	r_nbtor_other	0.097	0.2	11109
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.253	0.2	503
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	0.199	0.2	45
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.311	0.2	177
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.198	0.2	25
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	1.733	3	15704
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	2.05	3.5	19699
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	3.02	4.5	8268
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	4.043	5	6786
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	899	tight positional	0.15	0.05
1	2	B	899	tight positional	0.15	0.05
1	3	C	899	tight positional	0.13	0.05
1	4	D	899	tight positional	0.17	0.05
1	5	E	899	tight positional	0.16	0.05
1	6	F	899	tight positional	0.1	0.05
2	1	A	442	tight positional	0.18	0.05
2	2	B	442	tight positional	0.15	0.05
2	3	C	442	tight positional	0.14	0.05
2	4	D	442	tight positional	0.15	0.05
2	5	E	442	tight positional	0.14	0.05
2	6	F	442	tight positional	0.12	0.05
3	1	A	828	tight positional	0.17	0.05
3	2	B	828	tight positional	0.2	0.05
3	3	C	828	tight positional	0.2	0.05
3	4	D	828	tight positional	0.2	0.05
3	5	E	828	tight positional	0.16	0.05
3	6	F	828	tight positional	0.17	0.05
1	1	A	1072	loose positional	0.76	5
1	2	B	1072	loose positional	0.78	5
1	3	C	1072	loose positional	0.83	5
1	4	D	1072	loose positional	0.88	5
1	5	E	1072	loose positional	0.74	5
1	6	F	1072	loose positional	0.8	5
2	1	A	567	loose positional	0.78	5
2	2	B	567	loose positional	0.94	5
2	3	C	567	loose positional	0.75	5
2	4	D	567	loose positional	0.77	5
2	5	E	567	loose positional	0.81	5
2	6	F	567	loose positional	0.94	5
3	1	A	1031	loose positional	0.66	5
3	2	B	1031	loose positional	0.78	5
3	3	C	1031	loose positional	0.73	5
3	4	D	1031	loose positional	0.76	5
3	5	E	1031	loose positional	0.65	5
3	6	F	1031	loose positional	0.84	5
1	1	A	899	tight thermal	0.63	0.5
1	2	B	899	tight thermal	0.5	0.5
1	3	C	899	tight thermal	0.34	0.5
1	4	D	899	tight thermal	0.52	0.5
1	5	E	899	tight thermal	0.54	0.5
1	6	F	899	tight thermal	0.31	0.5
2	1	A	442	tight thermal	0.67	0.5
2	2	B	442	tight thermal	0.58	0.5
2	3	C	442	tight thermal	0.44	0.5
2	4	D	442	tight thermal	0.5	0.5
2	5	E	442	tight thermal	0.52	0.5
2	6	F	442	tight thermal	0.52	0.5
3	1	A	828	tight thermal	0.67	0.5
3	2	B	828	tight thermal	0.64	0.5
3	3	C	828	tight thermal	0.67	0.5
3	4	D	828	tight thermal	0.61	0.5
3	5	E	828	tight thermal	0.66	0.5
3	6	F	828	tight thermal	0.72	0.5
1	1	A	1072	loose thermal	3.35	10
1	2	B	1072	loose thermal	2.11	10
1	3	C	1072	loose thermal	1.94	10
1	4	D	1072	loose thermal	2.05	10
1	5	E	1072	loose thermal	3.02	10
1	6	F	1072	loose thermal	2.47	10
2	1	A	567	loose thermal	3.09	10
2	2	B	567	loose thermal	3.12	10
2	3	C	567	loose thermal	2.25	10
2	4	D	567	loose thermal	2.86	10
2	5	E	567	loose thermal	2.47	10
2	6	F	567	loose thermal	3.8	10
3	1	A	1031	loose thermal	2.25	10
3	2	B	1031	loose thermal	2.42	10
3	3	C	1031	loose thermal	2.6	10
3	4	D	1031	loose thermal	2.25	10
3	5	E	1031	loose thermal	2.48	10
3	6	F	1031	loose thermal	2.84	10

LS refinement shell

Resolution: 2.44→2.5 Å / Total num. of bins used: 20 /

	R_factor	Num. reflection
R_free	0.343	213
R_work	0.296	8346

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°²)	L12 (°²)	L13 (°²)	L22 (°²)	L23 (°²)	L33 (°²)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å²)	T12 (Å²)	T13 (Å²)	T22 (Å²)	T23 (Å²)	T33 (Å²)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	2.939	-0.1889	-1.2092	2.895	0.7236	6.4328	0.0767	0.1909	0.1501	-0.1067	0.1145	-0.1064	-1.0506	0.2837	-0.1912	-0.1588	-0.0439	0.0169	-0.1905	0.0055	-0.2769	13.795	93.012	43.904
2	5.0739	1.0389	4.9664	3.7643	2.8326	9.2502	-0.1576	0.2659	0.1918	-0.4893	-0.0265	-0.0393	-0.3661	0.2431	0.1841	-0.3021	0.022	-0.0091	-0.2026	0.0419	-0.2797	23.2	79.403	16.588
3	6.918	-0.5469	-0.6574	6.8742	2.4933	3.8591	0.0347	0.0372	0.7464	-0.3014	0.2225	-0.926	-0.6222	0.5012	-0.2572	-0.1711	-0.1326	0.0537	-0.1807	0.0278	-0.0783	28.19	103.091	72.843
4	12.4183	2.1949	6.774	4.1955	1.9919	7.436	0.3196	-0.1548	-0.9244	0.0247	-0.045	0.0748	0.4859	-0.0129	-0.2746	-0.2912	-0.0252	0.0587	-0.3239	0.0841	-0.1454	17.172	74.098	65.349
5	15.4705	4.4274	-3.0871	7.7671	-3.3926	3.7571	-0.3537	0.1794	4.2639	-0.6122	0.1359	1.4259	-0.6229	-0.4193	0.2178	0.3515	0.0045	-0.4041	-0.0165	-0.0838	1.2393	56.404	122.756	89.405
6	33.5247	4.2708	1.641	4.5778	-2.5967	3.5349	0.0422	-3.9901	-0.7695	0.2194	-0.2654	-0.1541	0.4089	0.1685	0.2232	-0.0346	0.1079	-0.0305	0.7608	0.0941	-0.092	34.664	101.88	100.764
7	8.8017	-1.7199	-2.0968	7.3945	1.8075	3.1638	0.5879	0.0684	1.6322	-0.4303	-0.0491	-1.2946	-0.7115	0.6043	-0.5388	-0.1001	-0.21	0.2156	-0.1181	0.0389	0.2624	102.098	30.993	40.941
8	4.8486	2.9786	-1.8258	11.7692	-3.3888	4.5842	-0.0357	0.1662	0.135	-0.1078	0.2261	0.3751	-0.0407	-0.5038	-0.1905	-0.2803	-0.007	-0.0239	-0.2185	0.0092	-0.2598	73.978	18.407	48.526
9	2.919	0.5134	-1.7373	5.5851	2.6835	7.206	0.0635	-0.1343	0.1872	0.1384	0.3597	-1.0427	-0.3632	0.9581	-0.4232	-0.2536	-0.0442	-0.0503	-0.235	-0.0041	0.0727	91.913	16.637	70.8
10	5.3882	0.303	-3.129	5.1908	-4.5931	10.519	-0.1202	-0.57	0.2109	0.2317	0.0818	-0.3615	-0.082	0.368	0.0384	-0.1915	0.0458	-0.0542	-0.3094	-0.0272	-0.1256	76.193	23.416	97.542
11	18.5065	8.3269	1.687	5.9702	1.7459	2.8664	-1.3026	0.6743	-3.0398	-1.0234	1.2155	-1.2794	1.8102	0.3998	0.0871	1.099	-0.0786	0.4322	0.6913	-0.0545	1.3794	106.346	41.991	91.357
12	36.7098	3.3939	4.6083	26.5475	3.717	14.0052	0.5518	-3.6552	2.2731	2.0711	-1.9349	-0.5164	-1.8528	0.7736	1.3831	0.616	-0.3428	0.1694	1.0173	-0.2554	0.4529	126.456	63.267	103.79
13	3.9448	2.1006	3.6378	1.9439	2.2431	8.1824	0.0186	0.0197	0.0425	0.0306	-0.0866	0.4227	0.0522	-0.337	0.068	-0.3939	0.0164	-0.0121	-0.324	-0.0221	-0.2923	49.784	71.857	45.934
14	6.7012	4.6681	-0.2784	4.7676	-0.0456	2.2036	0.1007	-0.3181	0.1491	0.3371	-0.0196	0.5011	-0.061	-0.1885	-0.0811	-0.2879	0.0659	0.0841	-0.2882	0.0552	-0.3583	52.328	74.928	78.605
15	2.611	1.4787	-2.2279	3.1186	-2.0783	8.4194	0.033	-0.3543	0.2447	0.5026	0.0362	0.2329	-0.4631	-0.5041	-0.0693	-0.2042	0.0637	-0.0179	-0.1676	-0.0683	-0.4148	73.474	97.205	92.363
16	4.9904	4.4811	0.427	5.9159	0.9522	2.487	0.0515	0.4528	-0.609	-0.1661	0.0111	-0.2438	0.2314	0.1179	-0.0626	-0.2412	0.0943	-0.045	-0.2132	-0.1451	-0.3175	74.528	54.286	37.238
17	2.6794	2.274	-3.3961	4.7342	-3.8658	7.9157	-0.2002	0.128	-0.5993	0.1181	0.0836	0.1427	0.3824	-0.0625	0.1166	-0.2786	0.0379	0.015	-0.4214	-0.0004	-0.1356	69.702	50.561	69.008
18	2.4471	1.2699	2.5255	4.1046	1.0959	12.4997	0.0761	-0.3347	-0.1959	0.9381	-0.039	-0.3119	0.4521	0.5349	-0.037	-0.0669	0.0604	-0.0122	-0.2178	0.0549	-0.3291	87.788	67.799	91.895

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	153 - 325
2	X-RAY DIFFRACTION	2	A	330 - 400
3	X-RAY DIFFRACTION	3	B	153 - 325
4	X-RAY DIFFRACTION	4	B	330 - 400
5	X-RAY DIFFRACTION	5	C	153 - 325
6	X-RAY DIFFRACTION	6	C	330 - 400
7	X-RAY DIFFRACTION	7	D	153 - 325
8	X-RAY DIFFRACTION	8	D	330 - 400
9	X-RAY DIFFRACTION	9	E	153 - 325
10	X-RAY DIFFRACTION	10	E	330 - 400
11	X-RAY DIFFRACTION	11	F	153 - 325
12	X-RAY DIFFRACTION	12	F	330 - 400
13	X-RAY DIFFRACTION	13	A	411 - 600
14	X-RAY DIFFRACTION	14	B	411 - 600
15	X-RAY DIFFRACTION	15	C	411 - 600
16	X-RAY DIFFRACTION	16	D	411 - 600
17	X-RAY DIFFRACTION	17	E	411 - 600
18	X-RAY DIFFRACTION	18	F	411 - 600

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