PDB-2cea: CELL DIVISION PROTEIN FTSH

ID or keywords:

Entry

Database: PDB / ID: 2cea

Title

CELL DIVISION PROTEIN FTSH

Components

CELL DIVISION PROTEIN FTSH

Keywords

HYDROLASE / CELL DIVISION / METALLOPROTEASE

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: 2.75 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	Jul 13, 2011	Group: Advisory / Refinement description / Version format compliance
Revision 1.2	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 1.3	Jul 24, 2019	Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
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	2cea.cif.gz	482.8 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	2cea_validation.pdf.gz	2.9 MB	Display	wwPDB validaton report
Full document	2cea_full_validation.pdf.gz	3 MB	Display
Data in XML	2cea_validation.xml.gz	98.9 KB	Display
Data in CIF	2cea_validation.cif.gz	132 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ce/2cea ftp://data.pdbj.org/pub/pdb/validation_reports/ce/2cea	HTTPS FTP

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Related structure data

Related structure data	2ce7C C: citing same article (ref.)
Similar structure data	2ce7-1 2ce7-2 4ww0-1 6oab-d 10216 5858 9677 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)	165.316, 165.316, 234.749
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	SER	SER	A	A	416 - 444	271 - 299
2	3	GLU	GLU	SER	SER	B	B	416 - 444	271 - 299
3	3	GLU	GLU	SER	SER	C	C	416 - 444	271 - 299
4	3	GLU	GLU	SER	SER	D	D	416 - 444	271 - 299
5	3	GLU	GLU	SER	SER	E	E	416 - 444	271 - 299
6	3	GLU	GLU	SER	SER	F	F	416 - 444	271 - 299
1	4	LEU	LEU	GLU	GLU	A	A	466 - 588	321 - 443
2	4	LEU	LEU	GLU	GLU	B	B	466 - 588	321 - 443
3	4	LEU	LEU	GLU	GLU	C	C	466 - 588	321 - 443
4	4	LEU	LEU	GLU	GLU	D	D	466 - 588	321 - 443
5	4	LEU	LEU	GLU	GLU	E	E	466 - 588	321 - 443
6	4	LEU	LEU	GLU	GLU	F	F	466 - 588	321 - 443

NCS ensembles :

ID
1
2
3
4

#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: GERMAN COLLECTION OF MICROORGANISMS (DSMZ) / Plasmid: PET28 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta References: UniProt: Q9WZ49, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases
#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

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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: 7.5 Details: 30% PEG400, O.2 M CACL2, 0.1M HEPES, PH7.5, pH 7.50

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 1
Detector	Type: MARRESEARCH / Detector: CCD / Date: Sep 19, 2005
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1 Å / Relative weight: 1
Reflection	Resolution: 2.7→40 Å / Num. obs: 86996 / % possible obs: 97.1 % / Observed criterion σ(I): 0 / Redundancy: 5.3 % / R_merge(I) obs: 0.08 / Net I/σ(I): 18.3
Reflection shell	Resolution: 2.7→2.75 Å / Redundancy: 4.6 % / R_merge(I) obs: 0.54 / Mean I/σ(I) obs: 2.6 / % possible all: 79

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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: 2.75→25 Å / Cor.coef. F_o:F_c: 0.931 / Cor.coef. F_o:F_c free: 0.916 / SU B: 30.018 / SU ML: 0.3 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 1.458 / ESU R Free: 0.354 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.262	1284	1.6 %	RANDOM
R_work	0.216	-	-	-
obs	0.216	81531	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: 38.02 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.96 Å²	0 Å²	0 Å²
2-	-	-0.96 Å²	0 Å²
3-	-	-	1.92 Å²

Refinement step

Cycle: LAST / Resolution: 2.75→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	1.009	1.997	26485
X-RAY DIFFRACTION	r_angle_other_deg	0.627	3	33467
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.116	5	2439
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	33.992	24.095	884
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	19.429	15	3603
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.616	15	175
X-RAY DIFFRACTION	r_chiral_restr	0.073	0.2	3038
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.02	21515
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	3780
X-RAY DIFFRACTION	r_nbd_refined	0.286	0.2	5491
X-RAY DIFFRACTION	r_nbd_other	0.258	0.2	14846
X-RAY DIFFRACTION	r_nbtor_refined	0.206	0.2	9930
X-RAY DIFFRACTION	r_nbtor_other	0.097	0.2	11615
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.269	0.2	566
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	0.211	0.2	60
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.334	0.2	180
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.259	0.2	24
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	1.998	3.5	15508
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	2.301	3.5	19699
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	3.223	4	8233
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	4.709	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	0.16	0.05
1	2	B	899	tight positional	0.16	0.05
1	3	C	899	tight positional	0.15	0.05
1	4	D	899	tight positional	0.18	0.05
1	5	E	899	tight positional	0.16	0.05
1	6	F	899	tight positional	0.15	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	0.15	0.05
2	4	D	442	tight positional	0.17	0.05
2	5	E	442	tight positional	0.15	0.05
2	6	F	442	tight positional	0.15	0.05
3	1	A	170	tight positional	0.13	0.05
3	2	B	170	tight positional	0.13	0.05
3	3	C	170	tight positional	0.14	0.05
3	4	D	170	tight positional	0.16	0.05
3	5	E	170	tight positional	0.14	0.05
3	6	F	170	tight positional	0.14	0.05
4	1	A	640	tight positional	0.16	0.05
4	2	B	640	tight positional	0.17	0.05
4	3	C	640	tight positional	0.15	0.05
4	4	D	640	tight positional	0.15	0.05
4	5	E	640	tight positional	0.14	0.05
4	6	F	640	tight positional	0.14	0.05
1	1	A	1072	loose positional	0.77	5
1	2	B	1072	loose positional	0.8	5
1	3	C	1072	loose positional	0.81	5
1	4	D	1072	loose positional	0.86	5
1	5	E	1072	loose positional	0.73	5
1	6	F	1072	loose positional	0.84	5
2	1	A	567	loose positional	0.78	5
2	2	B	567	loose positional	0.97	5
2	3	C	567	loose positional	0.75	5
2	4	D	567	loose positional	0.79	5
2	5	E	567	loose positional	0.81	5
2	6	F	567	loose positional	0.94	5
3	1	A	206	loose positional	0.67	5
3	2	B	206	loose positional	0.75	5
3	3	C	206	loose positional	0.93	5
3	4	D	206	loose positional	0.83	5
3	5	E	206	loose positional	0.79	5
3	6	F	206	loose positional	0.79	5
4	1	A	797	loose positional	0.56	5
4	2	B	797	loose positional	0.71	5
4	3	C	797	loose positional	0.6	5
4	4	D	797	loose positional	0.6	5
4	5	E	797	loose positional	0.54	5
4	6	F	797	loose positional	0.57	5
1	1	A	899	tight thermal	0.52	0.5
1	2	B	899	tight thermal	0.48	0.5
1	3	C	899	tight thermal	0.3	0.5
1	4	D	899	tight thermal	0.42	0.5
1	5	E	899	tight thermal	0.47	0.5
1	6	F	899	tight thermal	0.29	0.5
2	1	A	442	tight thermal	0.56	0.5
2	2	B	442	tight thermal	0.57	0.5
2	3	C	442	tight thermal	0.4	0.5
2	4	D	442	tight thermal	0.53	0.5
2	5	E	442	tight thermal	0.52	0.5
2	6	F	442	tight thermal	0.48	0.5
3	1	A	170	tight thermal	0.58	0.5
3	2	B	170	tight thermal	0.52	0.5
3	3	C	170	tight thermal	0.52	0.5
3	4	D	170	tight thermal	0.51	0.5
3	5	E	170	tight thermal	0.49	0.5
3	6	F	170	tight thermal	0.51	0.5
4	1	A	640	tight thermal	0.66	0.5
4	2	B	640	tight thermal	0.66	0.5
4	3	C	640	tight thermal	0.64	0.5
4	4	D	640	tight thermal	0.62	0.5
4	5	E	640	tight thermal	0.63	0.5
4	6	F	640	tight thermal	0.59	0.5
1	1	A	1072	loose thermal	3.41	10
1	2	B	1072	loose thermal	2.41	10
1	3	C	1072	loose thermal	2.42	10
1	4	D	1072	loose thermal	2.19	10
1	5	E	1072	loose thermal	3.31	10
1	6	F	1072	loose thermal	3.35	10
2	1	A	567	loose thermal	3.47	10
2	2	B	567	loose thermal	2.81	10
2	3	C	567	loose thermal	2.5	10
2	4	D	567	loose thermal	2.99	10
2	5	E	567	loose thermal	2.92	10
2	6	F	567	loose thermal	4.12	10
3	1	A	206	loose thermal	2.77	10
3	2	B	206	loose thermal	2.37	10
3	3	C	206	loose thermal	3.01	10
3	4	D	206	loose thermal	2.8	10
3	5	E	206	loose thermal	2.17	10
3	6	F	206	loose thermal	2.16	10
4	1	A	797	loose thermal	2.75	10
4	2	B	797	loose thermal	2.6	10
4	3	C	797	loose thermal	2.44	10
4	4	D	797	loose thermal	2.39	10
4	5	E	797	loose thermal	2.72	10
4	6	F	797	loose thermal	2.72	10

LS refinement shell

Resolution: 2.75→2.82 Å / Total num. of bins used: 20 /

	R_factor	Num. reflection
R_free	0.368	70
R_work	0.324	5012

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	3.9495	-0.2793	-1.8868	3.111	0.4442	5.8506	0.0867	0.0899	0.2132	-0.0914	0.0757	-0.0331	-0.8742	0.1519	-0.1624	-0.2054	-0.0207	-0.0061	-0.2266	-0.0031	-0.2181	13.795	93.012	43.904
2	5.6645	0.6483	5.167	4.2927	2.3214	9.3621	-0.0916	0.2868	0.1782	-0.4811	0.0746	-0.1029	-0.0508	0.2604	0.017	-0.3182	0.0163	0.0006	-0.254	0.0283	-0.2452	23.2	79.403	16.588
3	5.9407	-0.4799	-0.7464	6.9997	2.425	3.371	0.0244	0.1961	0.4697	-0.2876	0.2117	-0.7268	-0.3896	0.4492	-0.2361	-0.2588	-0.0864	0.0469	-0.2086	-0.0012	-0.1263	28.19	103.091	72.843
4	14.2794	2.8701	6.9762	3.4318	2.0929	8.0982	0.5875	-0.0996	-0.8949	0.0138	-0.1263	-0.0278	0.6948	-0.1255	-0.4611	-0.2932	-0.02	0.07	-0.3618	0.0431	-0.0958	17.172	74.098	65.349
5	8.9614	2.3565	-2.5223	7.2606	-2.888	3.2496	-0.1214	0.3021	2.3316	-0.4553	0.0988	0.5941	-0.3798	-0.1333	0.0226	0.1429	-0.0821	-0.1638	0.1051	-0.0216	0.9216	56.404	122.756	89.405
6	25.7931	3.7136	0.4232	6.1157	-1.529	3.9418	0.2017	-1.9531	-1.3836	0.7465	-0.3335	-0.3656	0.3494	0.2712	0.1318	-0.0343	0.0743	-0.0774	0.1198	0.1552	0.0408	34.664	101.88	100.764
7	7.8228	-0.5651	-1.5979	7.7103	1.6189	2.6081	0.5886	0.007	1.2587	-0.2346	-0.1689	-0.8682	-0.6497	0.5444	-0.4197	-0.0906	-0.165	0.201	-0.1575	0.016	0.1537	102.098	30.993	40.941
8	4.7304	3.9685	-1.211	14.1535	-4.5401	4.7153	-0.0996	0.1072	0.2544	-0.2355	0.3973	0.4807	0.0088	-0.4099	-0.2978	-0.2652	0.0434	-0.0012	-0.2319	-0.0263	-0.2386	73.978	18.407	48.526
9	3.5915	1.1429	-1.8376	5.8051	2.6193	6.5944	0.027	-0.2195	0.1849	0.0684	0.3418	-0.8925	-0.2669	0.9518	-0.3687	-0.2661	-0.0229	-0.0619	-0.2103	-0.009	0.0695	91.913	16.637	70.8
10	5.1779	-0.1629	-2.7223	7.9314	-5.6933	13.3326	-0.1648	-0.7601	0.1659	0.2323	0.3011	-0.3385	-0.0663	0.1007	-0.1363	-0.2462	0.0404	-0.0482	-0.3186	-0.0304	-0.057	76.193	23.416	97.542
11	13.2583	5.8574	-0.7373	4.5989	-1.4219	2.5806	-1.5998	0.8875	-2.176	-1.2393	1.2178	-0.9884	1.9875	-0.16	0.382	1.3056	-0.2497	0.3686	0.6433	-0.1711	1.6427	106.346	41.991	91.357
12	22.8184	2.8486	1.4799	18.5381	-2.1895	4.6318	1.6801	-3.198	1.6159	3.4676	-2.6505	1.8005	-1.3591	1.1849	0.9704	0.58	-0.5628	0.3056	1.5055	-0.341	0.5335	126.456	63.267	103.79
13	4.4382	2.1727	4.0569	2.047	2.6447	8.365	-0.0146	-0.0111	-0.0546	0.0362	-0.0707	0.3881	-0.0392	-0.2565	0.0853	-0.4013	0.0114	-0.0071	-0.3923	-0.0377	-0.2538	49.784	71.857	45.934
14	7.7908	5.4762	-0.5232	5.3564	-0.2347	2.4239	0.1496	-0.454	0.1108	0.3536	-0.0758	0.4628	-0.0917	-0.1713	-0.0738	-0.3374	0.0789	0.0761	-0.2966	0.0384	-0.3252	52.328	74.928	78.605
15	3.0304	1.6081	-2.8055	3.4579	-1.9595	10.7488	0.0178	-0.3587	0.2798	0.588	0.0093	0.2947	-0.418	-0.6363	-0.0271	-0.2143	0.0533	-0.0128	-0.1893	-0.0815	-0.3436	73.474	97.205	92.363
16	5.6332	5.2676	0.6767	6.7076	1.2904	2.8318	0.1413	0.3838	-0.6505	-0.118	-0.0235	-0.2595	0.2574	0.156	-0.1178	-0.2692	0.138	-0.0549	-0.256	-0.1507	-0.2732	74.528	54.286	37.238
17	2.6722	2.0327	-3.4015	4.4497	-3.9668	8.5346	-0.1887	0.0748	-0.5726	0.0737	0.0465	0.1785	0.4065	0.0108	0.1421	-0.3347	0.0296	0.0281	-0.4524	0.0015	-0.0617	69.702	50.561	69.008
18	2.5148	1.9248	3.0069	4.4208	1.3173	13.7645	0.1715	-0.3492	-0.295	0.9526	-0.1057	-0.3017	0.4393	0.5383	-0.0658	-0.0942	0.0253	-0.0136	-0.1796	0.0897	-0.2757	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	412 - 600

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