PDB-5lfq: Crystal Structure of the Bacterial Proteasome Activator Bpa of My...

ID or keywords:

Entry

Database: PDB / ID: 5lfq

Title

Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis (space group P3)

Components

Bacterial proteasome activator

Keywords

SIGNALING PROTEIN / Dodecamer / four-helix bundle

Function / homology

Bacterial proteasome activator / Bacterial proteasome activator / proteasome accessory complex / positive regulation of proteasomal protein catabolic process / proteasome binding / peptidoglycan-based cell wall / protein homooligomerization / plasma membrane / Bacterial proteasome activator

Function and homology information

Biological species

Mycobacterium tuberculosis H37Rv (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 3.503 Å

Authors

Bolten, M. / Delley, C.L. / Leibundgut, M. / Boehringer, D. / Ban, N. / Weber-Ban, E.

Citation

Journal: Structure / Year: 2016
Title: Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome.
Authors: Marcel Bolten / Cyrille L Delley / Marc Leibundgut / Daniel Boehringer / Nenad Ban / Eilika Weber-Ban /

Abstract: Mycobacterium tuberculosis harbors proteasomes that recruit substrates for degradation through an ubiquitin-like modification pathway. Recently, a non-ATPase activator termed Bpa (bacterial ...

History

Deposition	Jul 4, 2016	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Nov 23, 2016	Provider: repository / Type: Initial release
Revision 1.1	Dec 14, 2016	Group: Database references
Revision 1.2	Jan 10, 2024	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	5lfq.cif.gz	708.8 KB	Display	PDBx/mmCIF format
PDB format	pdb5lfq.ent.gz	599.1 KB	Display	PDB format
PDBx/mmJSON format	5lfq.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	5lfq_validation.pdf.gz	553.1 KB	Display	wwPDB validaton report
Full document	5lfq_full_validation.pdf.gz	572.4 KB	Display
Data in XML	5lfq_validation.xml.gz	55.7 KB	Display
Data in CIF	5lfq_validation.cif.gz	78.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/lf/5lfq ftp://data.pdbj.org/pub/pdb/validation_reports/lf/5lfq	HTTPS FTP

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Related structure data

Related structure data	4127C 4128C 5lfjC 5lfpSC 5lzpC C: citing same article (ref.) S: Starting model for refinement
Similar structure data	7649 7658 305 7673 2141 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: Bacterial proteasome activator

B: Bacterial proteasome activator

C: Bacterial proteasome activator

D: Bacterial proteasome activator

E: Bacterial proteasome activator

F: Bacterial proteasome activator

G: Bacterial proteasome activator

H: Bacterial proteasome activator

I: Bacterial proteasome activator

J: Bacterial proteasome activator

K: Bacterial proteasome activator

L: Bacterial proteasome activator

M: Bacterial proteasome activator

N: Bacterial proteasome activator

O: Bacterial proteasome activator

P: Bacterial proteasome activator

240 kDa, 16 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)	100.854, 100.854, 207.433
Angle α, β, γ (deg.)	90.000, 90.000, 120.000
Int Tables number	143
Space group name H-M	P3

Noncrystallographic symmetry (NCS)

NCS domain:
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	ASP	ASP	ARG	ARG	(chain A and (resseq 39:94 or resseq 96:105 or resseq 107:149))	A	A	39 - 94	11 - 66
1	2	GLU	GLU	ASN	ASN	(chain A and (resseq 39:94 or resseq 96:105 or resseq 107:149))	A	A	96 - 105	68 - 77
1	3	ASP	ASP	GLN	GLN	(chain A and (resseq 39:94 or resseq 96:105 or resseq 107:149))	A	A	107 - 149	79 - 121
2	1	ASP	ASP	ARG	ARG	(chain B and (resseq 39:94 or resseq 96:105 or resseq 107:149))	B	B	39 - 94	11 - 66
2	2	GLU	GLU	ASN	ASN	(chain B and (resseq 39:94 or resseq 96:105 or resseq 107:149))	B	B	96 - 105	68 - 77
2	3	ASP	ASP	GLN	GLN	(chain B and (resseq 39:94 or resseq 96:105 or resseq 107:149))	B	B	107 - 149	79 - 121
3	1	ASP	ASP	ARG	ARG	(chain C and (resseq 39:94 or resseq 96:105 or resseq 107:149))	C	C	39 - 94	11 - 66
3	2	GLU	GLU	ASN	ASN	(chain C and (resseq 39:94 or resseq 96:105 or resseq 107:149))	C	C	96 - 105	68 - 77
3	3	ASP	ASP	GLN	GLN	(chain C and (resseq 39:94 or resseq 96:105 or resseq 107:149))	C	C	107 - 149	79 - 121
4	1	ASP	ASP	ARG	ARG	(chain D and (resseq 39:94 or resseq 96:105 or resseq 107:149))	D	D	39 - 94	11 - 66
4	2	GLU	GLU	ASN	ASN	(chain D and (resseq 39:94 or resseq 96:105 or resseq 107:149))	D	D	96 - 105	68 - 77
4	3	ASP	ASP	GLN	GLN	(chain D and (resseq 39:94 or resseq 96:105 or resseq 107:149))	D	D	107 - 149	79 - 121
5	1	ASP	ASP	ARG	ARG	(chain E and (resseq 39:94 or resseq 96:105 or resseq 107:149))	E	E	39 - 94	11 - 66
5	2	GLU	GLU	ASN	ASN	(chain E and (resseq 39:94 or resseq 96:105 or resseq 107:149))	E	E	96 - 105	68 - 77
5	3	ASP	ASP	GLN	GLN	(chain E and (resseq 39:94 or resseq 96:105 or resseq 107:149))	E	E	107 - 149	79 - 121
6	1	ASP	ASP	ARG	ARG	(chain F and (resseq 39:94 or resseq 96:105 or resseq 107:149))	F	F	39 - 94	11 - 66
6	2	GLU	GLU	ASN	ASN	(chain F and (resseq 39:94 or resseq 96:105 or resseq 107:149))	F	F	96 - 105	68 - 77
6	3	ASP	ASP	GLN	GLN	(chain F and (resseq 39:94 or resseq 96:105 or resseq 107:149))	F	F	107 - 149	79 - 121
7	1	ASP	ASP	ARG	ARG	(chain G and (resseq 39:94 or resseq 96:105 or resseq 107:149))	G	G	39 - 94	11 - 66
7	2	GLU	GLU	ASN	ASN	(chain G and (resseq 39:94 or resseq 96:105 or resseq 107:149))	G	G	96 - 105	68 - 77
7	3	ASP	ASP	GLN	GLN	(chain G and (resseq 39:94 or resseq 96:105 or resseq 107:149))	G	G	107 - 149	79 - 121
8	1	ASP	ASP	ARG	ARG	(chain H and (resseq 39:94 or resseq 96:105 or resseq 107:149))	H	H	39 - 94	11 - 66
8	2	GLU	GLU	ASN	ASN	(chain H and (resseq 39:94 or resseq 96:105 or resseq 107:149))	H	H	96 - 105	68 - 77
8	3	ASP	ASP	GLN	GLN	(chain H and (resseq 39:94 or resseq 96:105 or resseq 107:149))	H	H	107 - 149	79 - 121
9	1	ASP	ASP	ARG	ARG	(chain I and (resseq 39:94 or resseq 96:105 or resseq 107:149))	I	I	39 - 94	11 - 66
9	2	GLU	GLU	ASN	ASN	(chain I and (resseq 39:94 or resseq 96:105 or resseq 107:149))	I	I	96 - 105	68 - 77
9	3	ASP	ASP	GLN	GLN	(chain I and (resseq 39:94 or resseq 96:105 or resseq 107:149))	I	I	107 - 149	79 - 121
10	1	ASP	ASP	ARG	ARG	(chain J and (resseq 39:94 or resseq 96:105 or resseq 107:149))	J	J	39 - 94	11 - 66
10	2	GLU	GLU	ASN	ASN	(chain J and (resseq 39:94 or resseq 96:105 or resseq 107:149))	J	J	96 - 105	68 - 77
10	3	ASP	ASP	GLN	GLN	(chain J and (resseq 39:94 or resseq 96:105 or resseq 107:149))	J	J	107 - 149	79 - 121
11	1	ASP	ASP	ARG	ARG	(chain K and (resseq 39:94 or resseq 96:105 or resseq 107:149))	K	K	39 - 94	11 - 66
11	2	GLU	GLU	ASN	ASN	(chain K and (resseq 39:94 or resseq 96:105 or resseq 107:149))	K	K	96 - 105	68 - 77
11	3	ASP	ASP	GLN	GLN	(chain K and (resseq 39:94 or resseq 96:105 or resseq 107:149))	K	K	107 - 149	79 - 121
12	1	ASP	ASP	ARG	ARG	(chain L and (resseq 39:94 or resseq 96:105 or resseq 107:149))	L	L	39 - 94	11 - 66
12	2	GLU	GLU	ASN	ASN	(chain L and (resseq 39:94 or resseq 96:105 or resseq 107:149))	L	L	96 - 105	68 - 77
12	3	ASP	ASP	GLN	GLN	(chain L and (resseq 39:94 or resseq 96:105 or resseq 107:149))	L	L	107 - 149	79 - 121
13	1	ASP	ASP	ARG	ARG	(chain M and (resseq 39:94 or resseq 96:105 or resseq 107:149))	M	M	39 - 94	11 - 66
13	2	GLU	GLU	ASN	ASN	(chain M and (resseq 39:94 or resseq 96:105 or resseq 107:149))	M	M	96 - 105	68 - 77
13	3	ASP	ASP	GLN	GLN	(chain M and (resseq 39:94 or resseq 96:105 or resseq 107:149))	M	M	107 - 149	79 - 121
14	1	ASP	ASP	ARG	ARG	(chain N and (resseq 39:94 or resseq 96:105 or resseq 107:149))	N	N	39 - 94	11 - 66
14	2	GLU	GLU	ASN	ASN	(chain N and (resseq 39:94 or resseq 96:105 or resseq 107:149))	N	N	96 - 105	68 - 77
14	3	ASP	ASP	GLN	GLN	(chain N and (resseq 39:94 or resseq 96:105 or resseq 107:149))	N	N	107 - 149	79 - 121
15	1	ASP	ASP	ARG	ARG	(chain O and (resseq 39:94 or resseq 96:105 or resseq 107:149))	O	O	39 - 94	11 - 66
15	2	GLU	GLU	ASN	ASN	(chain O and (resseq 39:94 or resseq 96:105 or resseq 107:149))	O	O	96 - 105	68 - 77
15	3	ASP	ASP	GLN	GLN	(chain O and (resseq 39:94 or resseq 96:105 or resseq 107:149))	O	O	107 - 149	79 - 121
16	1	ASP	ASP	ARG	ARG	(chain P and (resseq 39:94 or resseq 96:105 or resseq 107:149))	P	P	39 - 94	11 - 66
16	2	GLU	GLU	ASN	ASN	(chain P and (resseq 39:94 or resseq 96:105 or resseq 107:149))	P	P	96 - 105	68 - 77
16	3	ASP	ASP	GLN	GLN	(chain P and (resseq 39:94 or resseq 96:105 or resseq 107:149))	P	P	107 - 149	79 - 121

#1: Protein	Bacterial proteasome activator Mass: 15016.304 Da / Num. of mol.: 16 / Fragment: UNP residues 36-159 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium tuberculosis H37Rv (bacteria) Gene: bpa, Rv3780, MTCY13D12.14 / Plasmid: pET24 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta / References: UniProt: P9WKX3

#1: Protein

Bacterial proteasome activator

Mass: 15016.304 Da / Num. of mol.: 16 / Fragment: UNP residues 36-159
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Mycobacterium tuberculosis H37Rv (bacteria)
Gene: bpa, Rv3780, MTCY13D12.14 / Plasmid: pET24 / Production host:

Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta / References: UniProt: P9WKX3

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.58 Å³/Da / Density % sol: 52.31 %
Crystal grow	Temperature: 293.15 K / Method: evaporation Details: 5-7 % (v/v) propane-1,2-diol, 100 mM HEPES-NaOH pH 8.0 - 8.2, 200 mM MgCl2 PH range: 8.0 - 8.2

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9785 Å
Detector	Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Mar 6, 2015
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9785 Å / Relative weight: 1
Reflection	Resolution: 3.5→45.35 Å / Num. obs: 47926 / % possible obs: 81.44 % / Redundancy: 2.9 % / B_iso Wilson estimate: 93.3 Å² / CC_1/2: 0.997 / R_merge(I) obs: 0.0886 / R_sym value: 0.1047 / Net I/av σ(I): 6.75 / Net I/σ(I): 8.6
Reflection shell	Resolution: 3.5→3.549 Å / Redundancy: 2.4 % / R_merge(I) obs: 0.526 / Mean I/σ(I) obs: 1.41 / CC_1/2: 0.85 / % possible all: 78

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
XDS	May 1, 2016	data reduction
Aimless	0.5.26	data scaling
PHASER		phasing
PHENIX	1.10_2155	refinement
PDB_EXTRACT	3.2	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 5LFP

5lfp

Resolution: 3.503→45.35 Å / SU ML: 0.57 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 39.21

	R_factor	Num. reflection	% reflection
R_free	0.3013	3739	7.8 %
R_work	0.2423	-	-
obs	0.2469	47926	80.68 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å

Displacement parameters

B_iso max: 448.59 Å² / B_iso mean: 106.81 Å² / B_iso min: 37.24 Å²

Refinement step

Cycle: final / Resolution: 3.503→45.35 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13856	0	0	0	13856
Num. residues	-	-	-	-	1808

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.005	14032
X-RAY DIFFRACTION	f_angle_d	0.707	19040
X-RAY DIFFRACTION	f_chiral_restr	0.041	2256
X-RAY DIFFRACTION	f_plane_restr	0.005	2544
X-RAY DIFFRACTION	f_dihedral_angle_d	9.494	8720

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	2	B	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	3	C	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	4	D	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	5	E	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	6	F	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	7	G	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	8	H	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	9	I	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	10	J	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	11	K	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	12	L	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	13	M	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	14	N	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	15	O	8025	X-RAY DIFFRACTION	8.384	TORSIONAL
1	16	P	8025	X-RAY DIFFRACTION	8.384	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 27

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
3.5029-3.5472	0.3499	122	0.3665	1544	1666	76
3.5472-3.5939	0.4334	119	0.3423	1580	1699	76
3.5939-3.6431	0.3884	138	0.3499	1532	1670	77
3.6431-3.6951	0.447	139	0.3643	1542	1681	77
3.6951-3.7502	0.3865	123	0.3491	1477	1600	71
3.7502-3.8088	0.3512	133	0.2996	1522	1655	76
3.8088-3.8712	0.3869	137	0.3099	1615	1752	79
3.8712-3.9379	0.348	128	0.3118	1618	1746	81
3.9379-4.0095	0.3791	160	0.2958	1631	1791	82
4.0095-4.0866	0.3189	136	0.2619	1632	1768	80
4.0866-4.1699	0.3519	144	0.2728	1697	1841	83
4.1699-4.2605	0.3027	146	0.2437	1650	1796	81
4.2605-4.3596	0.2651	132	0.2404	1693	1825	83
4.3596-4.4685	0.2956	141	0.2418	1572	1713	80
4.4685-4.5892	0.3521	115	0.273	1673	1788	78
4.5892-4.7241	0.4349	131	0.2532	1558	1689	80
4.7241-4.8764	0.2974	153	0.2239	1650	1803	81
4.8764-5.0505	0.2614	132	0.2143	1704	1836	83
5.0505-5.2524	0.3282	147	0.2545	1778	1925	86
5.2524-5.4911	0.2892	129	0.2249	1709	1838	86
5.4911-5.7801	0.3881	142	0.2711	1766	1908	86
5.7801-6.1414	0.2895	137	0.2607	1640	1777	82
6.1414-6.6142	0.3297	140	0.221	1783	1923	86
6.6142-7.2774	0.2665	169	0.2091	1824	1993	90
7.2774-8.3248	0.2293	157	0.1669	1737	1894	87
8.3248-10.4671	0.1978	170	0.1486	1646	1816	82
10.4671-45.3546	0.2267	116	0.197	1417	1533	69

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	6.8143	-0.6369	-0.8203	4.2139	0.0243	3.0158	-0.3326	-0.1574	0.332	0.2325	0.0477	0.2756	0.1016	0.7407	-0.0053	0.5679	0.001	0.0397	0.7806	-0.0963	0.9145	-44.4522	64.6177	177.8825
2	3.2881	-1.311	1.8452	7.5831	0.1756	2.0196	-0.0138	-0.5167	-0.2326	0.5486	-0.1652	-0.4366	0.4476	-0.1749	0.0087	0.5017	-0.0865	-0.0455	0.7427	-0.0999	0.9075	-14.8933	23.1635	177.9946
3	4.3556	-1.321	-1.5171	4.7964	1.1824	1.4905	0.0617	-0.4206	-0.5397	0.6859	0.277	-0.0184	0.2171	0.0257	-0.0049	1.0185	-0.0552	0.0887	0.9837	-0.0046	0.8447	-33.7401	45.6632	74.1503
4	3.3004	0.0823	-1.4675	1.492	-1.9692	3.1211	-0.0794	-0.4889	-0.4757	0.9083	0.4964	0.0906	-0.7064	-0.4666	0.0017	1.1323	-0.0397	0.0053	1.0808	0.0888	0.6404	-22.9893	30.371	74.2024
5	4.4907	-1.5219	-1.7822	1.0182	-0.0619	2.679	-0.6313	-0.4748	-0.4984	0.2498	0.0554	-0.1328	-0.5391	-0.2669	-0.089	1.1131	0.0338	-0.1439	1.0953	0.1889	0.8367	-5.9739	22.7238	74.2181
6	0.9174	0.0962	-1.4906	5.2635	0.2506	3.5765	-0.2236	-0.5263	0.4824	0.3675	0.3711	0.6198	0.16	0.9747	0.0143	1.0142	0.0524	0.0281	1.2208	-0.0364	0.7837	-35.5094	64.1773	74.2625
7	3.0874	-1.4256	1.8236	6.2401	-1.8689	2.5334	-0.1556	-0.3087	0.2686	0.1794	0.4733	-0.0433	-0.0363	0.1679	-0.0056	0.4572	0.1144	-0.0459	0.6438	-0.0501	0.7104	-16.6849	41.6817	177.9024
8	5.8512	1.0908	1.151	3.4043	2.91	4.8979	-0.1527	-0.5375	0.2758	0.6706	0.2453	-0.5038	0.3091	1.0926	0.0111	0.6519	0.1227	-0.0208	0.4926	-0.1066	0.7261	-27.4543	56.9798	177.915
9	3.6042	-2.7709	-1.2873	3.3653	2.3908	2.0149	-0.007	0.1445	0.4141	-0.5249	-0.2005	0.6763	-0.0005	-0.3138	-0.0699	1.1109	-0.099	-0.0021	1.0573	-0.1051	0.78	-27.7625	35.3145	129.0787
10	2.3576	0.8897	2.6043	4.0681	-0.1061	3.184	0.4202	0.7017	-0.0592	-0.9307	-0.2167	0.5828	1.1637	0.431	-0.0131	1.0377	0.0855	-0.0464	1.1623	0.0997	0.6818	-35.615	52.2232	129.05
11	3.1048	0.3491	-0.7181	5.9575	0.7622	3.2571	0.0454	0.2067	-0.3712	-0.5907	-0.0615	-0.265	-0.3984	0.4207	-0.0083	0.6099	-0.0949	-0.004	0.7103	-0.0571	0.8256	-16.7063	16.5304	25.3307
12	5.4575	-1.4637	-1.9845	4.4435	-2.8103	4.4164	0.0096	0.4715	0.1934	-0.6764	-0.0592	0.0913	0.4019	-0.2117	0.0107	0.5241	-0.046	-0.1254	0.5749	0.0739	0.8687	-37.8281	62.868	25.2721
13	2.2614	0.7403	0.7248	4.9292	0.5524	3.6143	-0.1121	0.021	0.2876	-0.7682	-0.1753	0.1057	0.4977	0.2359	-0.063	1.2419	-0.0721	0.0206	1.1962	0.1216	0.7174	-33.7487	70.7823	129.0119
14	4.4696	-2.0598	-1.0019	2.7321	1.0623	3.3908	-0.0826	0.1001	-0.6055	-0.6603	0.1102	-0.0098	-1.1185	0.131	0.0021	1.1254	-0.1407	0.0599	1.0626	-0.0899	0.7033	-12.5922	24.4822	128.9345
15	6.4143	-2.2535	0.037	4.8836	-2.333	4.9094	-0.0885	0.3425	-0.1056	-0.2449	0.2447	-0.5883	-0.6799	0.4976	0.2858	0.618	0.0348	0.1059	0.4024	0.1076	0.7281	-22.6897	52.0051	25.3427
16	2.7094	1.1166	-3.5731	4.1558	-0.2238	5.0858	0.2892	0.5845	0.3352	-0.4137	0.0125	-1.1579	-1.3417	-0.3503	0.0408	0.6127	0.1185	0.1136	0.535	-0.0701	0.8153	-14.8394	35.0958	25.2905

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 37 through 149)	A	37 - 149
2	X-RAY DIFFRACTION	2	(chain 'B' and resid 37 through 149)	B	37 - 149
3	X-RAY DIFFRACTION	3	(chain 'C' and resid 37 through 149)	C	37 - 149
4	X-RAY DIFFRACTION	4	(chain 'D' and resid 37 through 149)	D	37 - 149
5	X-RAY DIFFRACTION	5	(chain 'E' and resid 37 through 149)	E	37 - 149
6	X-RAY DIFFRACTION	6	(chain 'F' and resid 37 through 149)	F	37 - 149
7	X-RAY DIFFRACTION	7	(chain 'G' and resid 37 through 149)	G	37 - 149
8	X-RAY DIFFRACTION	8	(chain 'H' and resid 37 through 149)	H	37 - 149
9	X-RAY DIFFRACTION	9	(chain 'I' and resid 37 through 149)	I	37 - 149
10	X-RAY DIFFRACTION	10	(chain 'J' and resid 37 through 149)	J	37 - 149
11	X-RAY DIFFRACTION	11	(chain 'K' and resid 37 through 149)	K	37 - 149
12	X-RAY DIFFRACTION	12	(chain 'L' and resid 37 through 149)	L	37 - 149
13	X-RAY DIFFRACTION	13	(chain 'M' and resid 37 through 149)	M	37 - 149
14	X-RAY DIFFRACTION	14	(chain 'N' and resid 37 through 149)	N	37 - 149
15	X-RAY DIFFRACTION	15	(chain 'O' and resid 37 through 149)	O	37 - 149
16	X-RAY DIFFRACTION	16	(chain 'P' and resid 37 through 149)	P	37 - 149

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