PDB-7m1l: Crystal structure of Pseudomonas aeruginosa ClpP2

ID or keywords:

Entry

Database: PDB / ID: 7m1l

Title

Crystal structure of Pseudomonas aeruginosa ClpP2

Components

ATP-dependent Clp protease proteolytic subunit

Keywords

HYDROLASE / Petidase

Function / homology

Function and homology information

endopeptidase Clp / ATP-dependent peptidase activity / serine-type endopeptidase activity / cytoplasm
Similarity search - Function

Biological species

Pseudomonas aeruginosa (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2 Å

Authors

Hall, B.M. / Grant, R.A. / Baker, T.A. / Sauer, R.T.

Funding support

United States, 2items

Organization	Grant number	Country
Howard Hughes Medical Institute (HHMI)		United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)	AI016892	United States

Citation

Journal: Mol.Microbiol. / Year: 2021
Title: ClpP1P2 peptidase activity promotes biofilm formation in Pseudomonas aeruginosa.
Authors: Mawla, G.D. / Hall, B.M. / Carcamo-Oyarce, G. / Grant, R.A. / Zhang, J.J. / Kardon, J.R. / Ribbeck, K. / Sauer, R.T. / Baker, T.A.

History

Deposition	Mar 13, 2021	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 24, 2021	Provider: repository / Type: Initial release
Revision 1.1	Jun 30, 2021	Group: Database references / Category: citation Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.2	Oct 18, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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	7m1l.cif.gz	727.8 KB	Display	PDBx/mmCIF format
PDB format	pdb7m1l.ent.gz	618.9 KB	Display	PDB format
PDBx/mmJSON format	7m1l.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/m1/7m1l ftp://data.pdbj.org/pub/pdb/validation_reports/m1/7m1l	HTTPS FTP

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Related structure data

Related structure data	7m1mC 1yg6S S: Starting model for refinement C: citing same article (ref.)
Similar structure data	5c3c-1 6pbu-d 4u0h-d 1fcf-2 4gm2-d 7bug-d 3vcp-1 6jx2-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

Deposited unit

A: ATP-dependent Clp protease proteolytic subunit

B: ATP-dependent Clp protease proteolytic subunit

C: ATP-dependent Clp protease proteolytic subunit

D: ATP-dependent Clp protease proteolytic subunit

E: ATP-dependent Clp protease proteolytic subunit

F: ATP-dependent Clp protease proteolytic subunit

G: ATP-dependent Clp protease proteolytic subunit

hetero molecules

164 kDa, 7 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	124.372, 147.439, 99.338
Angle α, β, γ (deg.)	90.000, 121.730, 90.000
Int Tables number	5
Space group name H-M	C121

Components on special symmetry positions

ID	Model	Components
1	1	A-349- HOH

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	(chain A and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))
2	1	(chain B and (resid 14 through 92 or resid 94 through 199))
3	1	(chain C and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))
4	1	(chain D and (resid 14 through 92 or resid 94 through 199))
5	1	(chain E and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))
6	1	(chain F and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))
7	1	(chain G and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))

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	Selection details	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	HIS	HIS	GLY	GLY	(chain A and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	A	A	14 - 92	14 - 92
1	2	GLY	GLY	PRO	PRO	(chain A and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	A	A	94 - 125	94 - 125
1	3	SER	SER	PRO	PRO	(chain A and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	A	A	134 - 199	134 - 199
2	1	HIS	HIS	GLY	GLY	(chain B and (resid 14 through 92 or resid 94 through 199))	B	B	14 - 92	14 - 92
2	2	GLY	GLY	PRO	PRO	(chain B and (resid 14 through 92 or resid 94 through 199))	B	B	94 - 199	94 - 199
3	1	HIS	HIS	GLY	GLY	(chain C and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	C	C	14 - 92	14 - 92
3	2	GLY	GLY	PRO	PRO	(chain C and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	C	C	94 - 125	94 - 125
3	3	SER	SER	PRO	PRO	(chain C and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	C	C	134 - 199	134 - 199
4	1	HIS	HIS	GLY	GLY	(chain D and (resid 14 through 92 or resid 94 through 199))	D	D	14 - 92	14 - 92
4	2	GLY	GLY	PRO	PRO	(chain D and (resid 14 through 92 or resid 94 through 199))	D	D	94 - 199	94 - 199
5	1	HIS	HIS	GLY	GLY	(chain E and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	E	E	14 - 92	14 - 92
5	2	GLY	GLY	PRO	PRO	(chain E and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	E	E	94 - 125	94 - 125
5	3	SER	SER	PRO	PRO	(chain E and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	E	E	134 - 199	134 - 199
6	1	HIS	HIS	GLY	GLY	(chain F and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	F	F	14 - 92	14 - 92
6	2	GLY	GLY	PRO	PRO	(chain F and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	F	F	94 - 125	94 - 125
6	3	SER	SER	PRO	PRO	(chain F and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	F	F	134 - 199	134 - 199
7	1	HIS	HIS	GLY	GLY	(chain G and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	G	G	14 - 92	14 - 92
7	2	GLY	GLY	PRO	PRO	(chain G and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	G	G	94 - 125	94 - 125
7	3	SER	SER	PRO	PRO	(chain G and (resid 14 through 92 or resid 94 through 125 or resid 134 through 199))	G	G	134 - 199	134 - 199

NCS ensembles :

ID
1
2

#1: Protein	ATP-dependent Clp protease proteolytic subunit / Endopeptidase Clp Mass: 23356.494 Da / Num. of mol.: 7 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Gene: clpP2, clpP, PAMH19_1747 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0A8RGC1, endopeptidase Clp
#2: Chemical	ChemComp-PO4 / PHOSPHATE ION Mass: 94.971 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: PO₄
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 247 / Source method: isolated from a natural source / Formula: H₂O
Has ligand of interest	N

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.37 Å³/Da / Density % sol: 48.08 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.9 Details: 1.8 M sodium phosphate monobasic monohydrate, potassium phosphate dibasic, pH 6.9

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 24-ID-E / Wavelength: 0.97918 Å

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 14, 2014

Radiation

Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.97918 Å / Relative weight: 1

Reflection

Resolution: 2→100 Å / Num. obs: 102184 / % possible obs: 99.6 % / Redundancy: 3.7 % / R_merge(I) obs: 0.073 / R_pim(I) all: 0.044 / R_rim(I) all: 0.085 / Χ²: 0.979 / Net I/σ(I): 7.3 / Num. measured all: 383187

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Χ²	% possible all
2-2.03	3.7	0.931	5097	0.624	0.566	1.092	0.592	100
2.03-2.07	3.7	0.766	5110	0.722	0.462	0.897	0.655	100
2.07-2.11	3.7	0.647	5131	0.774	0.389	0.756	0.648	100
2.11-2.15	3.8	0.529	5102	0.852	0.317	0.617	0.626	100
2.15-2.2	3.8	0.421	5133	0.9	0.252	0.491	0.639	100
2.2-2.25	3.8	0.354	5135	0.92	0.212	0.413	0.744	100
2.25-2.31	3.8	0.301	5117	0.949	0.18	0.351	0.693	100
2.31-2.37	3.8	0.239	5086	0.966	0.142	0.278	0.684	100
2.37-2.44	3.8	0.201	5114	0.975	0.119	0.234	0.694	100
2.44-2.52	3.8	0.16	5099	0.984	0.095	0.186	0.705	99.9
2.52-2.61	3.8	0.133	5171	0.99	0.079	0.155	0.72	100
2.61-2.71	3.8	0.12	5080	0.988	0.071	0.139	0.769	100
2.71-2.84	3.8	0.092	5157	0.992	0.055	0.108	0.767	100
2.84-2.99	3.8	0.076	5089	0.994	0.046	0.089	0.848	100
2.99-3.17	3.8	0.067	5134	0.994	0.04	0.079	1.101	100
3.17-3.42	3.8	0.063	5151	0.993	0.038	0.073	1.602	100
3.42-3.76	3.7	0.059	5139	0.994	0.036	0.069	2.27	100
3.76-4.31	3.7	0.047	5130	0.996	0.029	0.055	1.849	99.9
4.31-5.43	3.7	0.039	5160	0.997	0.024	0.046	1.461	99.9
5.43-100	3.6	0.042	4849	0.996	0.026	0.05	1.627	92.9

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
SCALEPACK		data scaling
PHASER		phasing
PHENIX	1.17.1	refinement
PDB_EXTRACT	3.25	data extraction
HKL-2000		data reduction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1YG6

1yg6

Resolution: 2→19.97 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 24.6 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2175	5036	4.93 %
R_work	0.1969	97126	-
obs	0.198	102162	99.54 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL

Displacement parameters

B_iso max: 170.88 Å² / B_iso mean: 60.3289 Å² / B_iso min: 24.57 Å²

Refinement step

Cycle: final / Resolution: 2→19.97 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9924	0	15	247	10186
B_iso mean	-	-	101.81	43	-
Num. residues	-	-	-	-	1272

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	6087	X-RAY DIFFRACTION	10.703	TORSIONAL
1	2	B	6087	X-RAY DIFFRACTION	10.703	TORSIONAL
1	3	C	6087	X-RAY DIFFRACTION	10.703	TORSIONAL
1	4	D	6087	X-RAY DIFFRACTION	10.703	TORSIONAL
1	5	E	6087	X-RAY DIFFRACTION	10.703	TORSIONAL
1	6	F	6087	X-RAY DIFFRACTION	10.703	TORSIONAL
1	7	G	6087	X-RAY DIFFRACTION	10.703	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 30

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2-2.02	0.38	172	0.329	3078	3250	95
2.02-2.04	0.3846	171	0.3112	3252	3423	100
2.04-2.07	0.2955	140	0.2923	3237	3377	100
2.07-2.1	0.2843	161	0.2761	3284	3445	100
2.1-2.12	0.2887	167	0.2654	3238	3405	100
2.12-2.15	0.2765	158	0.2571	3244	3402	100
2.15-2.18	0.2721	145	0.2411	3244	3389	100
2.18-2.22	0.2356	192	0.2358	3222	3414	100
2.22-2.25	0.2765	187	0.2282	3284	3471	100
2.25-2.29	0.2724	157	0.2244	3195	3352	100
2.29-2.33	0.2353	164	0.2144	3242	3406	100
2.33-2.37	0.2329	143	0.2085	3303	3446	100
2.37-2.41	0.2338	188	0.2102	3204	3392	100
2.41-2.46	0.2431	182	0.2053	3249	3431	100
2.46-2.52	0.2252	162	0.2024	3228	3390	100
2.52-2.58	0.2398	169	0.1896	3247	3416	100
2.58-2.64	0.2206	171	0.2	3249	3420	100
2.64-2.71	0.23	168	0.2045	3229	3397	100
2.71-2.79	0.212	183	0.2038	3243	3426	100
2.79-2.88	0.267	180	0.2134	3240	3420	100
2.88-2.98	0.2353	153	0.2125	3270	3423	100
2.98-3.1	0.2578	161	0.2206	3275	3436	100
3.1-3.24	0.2443	167	0.2097	3235	3402	100
3.24-3.41	0.2401	167	0.2062	3283	3450	100
3.41-3.62	0.236	169	0.1917	3227	3396	100
3.62-3.9	0.1881	176	0.1825	3264	3440	100
3.9-4.29	0.1559	190	0.1614	3238	3428	100
4.29-4.91	0.1605	160	0.1398	3276	3436	100
4.91-6.15	0.1915	166	0.1825	3290	3456	100
6.15-19.97	0.2025	167	0.1874	3056	3223	92

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	9.3427	1.9784	2.2645	6.106	1.0532	2.1394	-0.7397	-0.0884	0.3313	-0.479	0.0661	0.6975	-0.964	-0.4477	0.6243	0.3752	-0.043	-0.0621	0.3775	-0.0083	0.6407	0.9244	49.2178	32.9407
2	4.0798	-0.3026	-0.3801	4.0139	0.3289	1.949	-0.022	0.3428	0.1974	-0.1231	-0.0644	-0.0235	-0.2648	0.1124	0.0683	0.2973	-0.0437	-0.0692	0.336	0.0705	0.2982	17.2131	52.4547	34.6098
3	1.4207	-1.2761	0.4089	1.5892	-1.012	1.4663	-0.0584	0.2405	-0.099	-0.1352	-0.1801	-0.2049	-0.0658	0.2852	0.2617	0.3337	-0.0825	-0.0691	0.4135	0.0616	0.4034	27.227	45.0911	31.9001
4	2.5488	-0.425	0.8094	3.7958	-4.3358	5.9066	-0.0146	0.3411	0.535	0.0917	-0.2528	-0.6723	-1.1234	0.0142	0.4378	0.6128	-0.0072	0.021	0.545	0.1162	0.5013	34.9493	61.1983	24.4657
5	4.9505	2.0733	-0.4347	3.8666	-0.761	1.9969	-0.0405	0.1896	-0.5773	0.1307	-0.1178	-0.7153	-0.0696	0.3609	0.1567	0.286	-0.0007	-0.0613	0.3627	0.0683	0.4055	31.0798	41.7577	34.889
6	7.5892	2.4186	-1.6272	4.3541	-5.6045	7.6935	-0.1656	-0.3578	0.6192	0.3133	-0.5535	-0.9451	-0.8753	0.4802	0.4947	0.5023	0.0154	-0.0579	0.3019	-0.0745	0.8138	-17.9106	46.0786	27.1676
7	4.1824	0.9784	1.5858	3.8983	0.8214	3.8833	-0.0022	0.1826	0.1934	-0.3528	0.1357	-0.0553	-0.0643	0.1599	-0.1342	0.2949	-0.0457	0.0623	0.2472	-0.02	0.4183	-16.3729	30.5182	22.9223
8	4.9366	0.2294	-0.2602	1.8601	0.2178	2.5017	-0.0973	0.7066	0.2985	-0.4088	0.1041	0.109	0.0576	-0.2682	-0.0439	0.4315	-0.0665	-0.0745	0.3636	0.0734	0.5611	-22.4291	23.9984	14.5092
9	4.8815	-1.5367	-6.3543	4.1329	0.0589	9.4585	-0.6948	-0.9144	-0.1575	0.1803	0.1758	-0.5055	0.5085	1.9646	0.3564	0.6038	-0.1115	-0.0263	0.8061	-0.0774	0.4825	-7.6592	15.5177	10.5841
10	5.7624	1.7042	-4.6456	6.562	-0.6603	4.2787	-0.4363	1.6243	-0.4343	-0.8222	0.521	0.0803	-0.3932	-0.3497	0.0842	0.9617	-0.3333	0.0863	0.8425	-0.3594	0.6137	-19.7373	13.5592	6.5884
11	5.1981	0.5032	-1.2612	5.4787	1.0145	4.9459	-0.3427	0.8591	0.2859	-0.3852	0.217	0.732	0.2902	-0.6252	0.102	0.3594	-0.1342	-0.1595	0.4469	0.0797	0.5797	-31.8044	24.2646	17.1295
12	4.2359	2.7052	3.7356	5.6189	5.937	6.5259	-0.2609	-0.1173	-0.2605	-0.5547	-0.7698	1.0276	-0.2876	-0.7457	0.7297	0.419	-0.0775	-0.0725	0.4153	0.064	0.667	1.7677	60.0508	33.1072
13	6.406	0.6629	-0.4274	3.1867	-0.151	2.0182	0.0478	0.0701	-0.6615	-0.1169	-0.1336	-0.371	-0.0196	-0.1467	0.0709	0.3603	-0.0759	-0.0311	0.3035	-0.0181	0.3934	12.683	74.439	33.1568
14	4.4319	-1.3691	3.5694	2.5206	-2.0909	3.4012	0.0122	0.5657	0.2381	-0.2486	-0.1086	-0.1276	-0.0847	-0.7261	0.0786	0.3829	-0.0477	0.0279	0.644	0.018	0.4503	16.7933	88.4543	18.2966
15	3.2918	1.5081	-0.6068	4.6934	-1.6247	2.5477	0.0486	-0.2134	-0.6414	0.3708	-0.218	-0.9274	-0.0987	0.1733	0.1508	0.334	-0.0609	-0.1159	0.3596	0.031	0.6686	27.2713	78.0143	35.1134
16	4.1205	-3.1697	-4.0214	2.6742	2.3225	6.3753	0.0355	-0.0372	-1.7631	0.2899	-0.2704	-0.2724	0.3001	0.7266	0.2591	0.447	0.0849	-0.0898	0.5106	-0.0756	0.5277	-15.8118	65.9043	26.6755
17	3.1616	0.3375	0.9465	4.6477	-0.9804	1.922	0.1667	0.3207	-0.1682	-0.3102	0.0445	0.0829	0.3612	0.2472	-0.1667	0.3723	0.1195	0.0053	0.3094	-0.025	0.2873	-29.535	69.6729	18.1779
18	1.9277	0.6296	0.5282	3.5091	1.0592	1.9771	-0.272	0.594	0.0239	-0.503	0.241	0.3277	-0.1079	0.0578	-0.0541	0.4595	0.0269	-0.0227	0.4249	0.0229	0.386	-31.8316	79.8329	10.853
19	4.3863	-1.1862	-1.8493	7.4417	6.6192	8.3238	-0.043	0.7507	-0.3532	0.1365	-0.4177	0.4512	0.8333	-1.0882	0.2943	0.6279	-0.0161	-0.08	0.6767	0.0618	0.4609	-40.4036	68.314	-0.3339
20	4.0394	0.1101	-0.726	3.3326	0.631	4.3995	0.161	1.1764	0.3633	-1.0657	-0.0776	0.289	-0.797	-0.4508	-0.1498	0.7094	0.1362	-0.0669	0.6168	0.0964	0.449	-39.302	80.9024	-0.5459
21	5.5342	-1.1884	1.5414	4.5795	0.8348	7.0648	-0.0362	0.1264	0.6036	-0.3051	0.0114	0.3569	-0.4737	-0.042	-0.0437	0.3803	0.0499	0.0249	0.2541	0.0435	0.4855	-31.8344	86.8353	16.7247
22	4.3379	-4.1849	-1.6496	5.4946	4.7337	7.4301	0.557	-0.1458	-1.2191	-0.3197	-0.4085	0.6958	0.1413	0.2134	-0.1921	0.5201	-0.0266	-0.1071	0.4244	0.0024	0.5712	-5.5749	67.5021	30.1345
23	5.8495	1.2478	0.1945	3.2435	-0.4408	1.8201	0.1151	0.4346	0.0089	-0.1571	-0.1492	0.0651	-0.0473	-0.0243	0.0335	0.2969	0.0332	0.0383	0.3556	-0.0778	0.2411	-8.8478	84.2713	24.8435
24	3.8469	-0.183	2.7652	1.6652	2.7393	8.8127	-0.1762	0.7276	0.5352	0.1163	-0.3589	0.333	0.064	-0.403	0.3773	0.5068	-0.0055	-0.0251	0.7038	0.1396	0.4792	-13.7675	94.6824	7.3979
25	4.5119	0.9417	1.8375	5.3527	-0.7058	5.6232	-0.1149	0.199	0.4592	-0.0661	-0.1084	0.0607	-0.6312	0.3151	0.2086	0.3373	-0.0638	0.0053	0.3704	-0.0593	0.4344	0.1198	95.8057	26.0288
26	4.5695	-2.1345	0.4948	5.472	0.814	2.411	0.1488	0.2494	-0.095	-0.2463	-0.3314	0.5997	-0.104	0.1357	0.1139	0.2566	-0.0088	-0.0158	0.2487	0.0089	0.3375	3.4453	32.8781	30.9619
27	5.9316	1.109	-1.8704	4.6861	0.3907	4.3119	0.1903	0.5144	0.0503	-0.6726	-0.1051	-0.1878	-0.6244	0.4363	-0.0463	0.508	0.0725	0.0059	0.3781	-0.0367	0.3731	18.9044	25.553	20.797
28	6.8294	-0.8788	-0.1136	3.9205	0.0811	1.6799	0.1821	0.332	-0.9767	-0.0106	-0.3042	0.7343	0.1987	0.0139	0.0835	0.3687	0.0214	-0.0239	0.2612	-0.0527	0.6528	6.0701	15.2651	27.2079
29	8.3638	0.8107	1.6913	4.0412	0.1977	2.1673	-0.6111	0.4599	-0.0153	-0.4757	0.2186	0.1382	-0.3297	0.0486	0.3256	0.4213	-0.0213	-0.066	0.3168	0.0336	0.514	-32.4088	48.7179	19.2015
30	4.1814	-2.1604	-1.4106	1.3079	0.2562	2.3261	-0.3958	1.2216	0.6765	-0.506	0.026	-0.2065	-0.4299	0.2174	0.3977	1.0145	-0.2321	-0.3481	0.914	0.0498	0.8737	-37.9537	48.2902	3.042
31	6.6098	-2.0109	-3.9208	5.3029	1.7221	2.382	-0.3005	0.0337	-0.9148	0.4676	-0.4861	0.5464	1.5495	0.3521	0.7112	0.9492	-0.0095	-0.0969	1.0769	-0.1039	0.6981	-37.9771	33.9775	1.9398
32	4.017	0.1527	-0.6304	5.0209	0.3628	1.0386	-0.7774	0.7598	0.6875	-0.6087	0.3426	1.0376	-0.2455	-0.0268	0.3362	0.6622	-0.0649	-0.386	0.7938	-0.0279	0.9699	-47.9284	50.9882	9.7137

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 14 through 27 )	A	14 - 27
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 28 through 106 )	A	28 - 106
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 107 through 132 )	A	107 - 132
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 133 through 158 )	A	133 - 158
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 159 through 200 )	A	159 - 200
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 14 through 28 )	B	14 - 28
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 29 through 106 )	B	29 - 106
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 107 through 135 )	B	107 - 135
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 136 through 158 )	B	136 - 158
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 159 through 172 )	B	159 - 172
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 173 through 198 )	B	173 - 198
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 14 through 27 )	C	14 - 27
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 28 through 121 )	C	28 - 121
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 122 through 158 )	C	122 - 158
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 159 through 199 )	C	159 - 199
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 14 through 27 )	D	14 - 27
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 28 through 106 )	D	28 - 106
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 107 through 135 )	D	107 - 135
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 136 through 158 )	D	136 - 158
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 159 through 172 )	D	159 - 172
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 173 through 199 )	D	173 - 199
22	X-RAY DIFFRACTION	22	chain 'E' and (resid 14 through 27 )	E	14 - 27
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 28 through 121 )	E	28 - 121
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 122 through 168 )	E	122 - 168
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 169 through 199 )	E	169 - 199
26	X-RAY DIFFRACTION	26	chain 'F' and (resid 14 through 114 )	F	14 - 114
27	X-RAY DIFFRACTION	27	chain 'F' and (resid 115 through 158 )	F	115 - 158
28	X-RAY DIFFRACTION	28	chain 'F' and (resid 159 through 199 )	F	159 - 199
29	X-RAY DIFFRACTION	29	chain 'G' and (resid 14 through 114 )	G	14 - 114
30	X-RAY DIFFRACTION	30	chain 'G' and (resid 115 through 135 )	G	115 - 135
31	X-RAY DIFFRACTION	31	chain 'G' and (resid 136 through 158 )	G	136 - 158
32	X-RAY DIFFRACTION	32	chain 'G' and (resid 159 through 199 )	G	159 - 199

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