PDB-3b8o: Structure of WzzE- Bacterial Polysaccharide Co-polymerase

ID or keywords:

Entry

Database: PDB / ID: 3b8o

Title

Structure of WzzE- Bacterial Polysaccharide Co-polymerase

Components

Lipopolysaccharide biosynthesis protein wzzE

Keywords

BIOSYNTHETIC PROTEIN / WZZ / WzzE / Bacterial Polysaccharide Co-polymerase / Inner membrane / Lipopolysaccharide biosynthesis /

Membrane /

Transmembrane /

MEMBRANE PROTEIN

Function / homology

Function and homology information

enterobacterial common antigen biosynthetic process / identical protein binding /

plasma membrane
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

SAD / Resolution: 2.4 Å

Authors

Tocilj, A. / Matte, A. / Cygler, M.

Citation

Journal: Nat.Struct.Mol.Biol. / Year: 2008
Title: Bacterial polysaccharide co-polymerases share a common framework for control of polymer length
Authors: Tocilj, A. / Munger, C. / Proteau, A. / Morona, R. / Purins, L. / Ajamian, E. / Wagner, J. / Papadopoulos, M. / Van Den Bosch, L. / Rubinstein, J.L. / Fethiere, J. / Matte, A. / Cygler, M.

History

Deposition	Nov 1, 2007	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jan 22, 2008	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Derived calculations ...Advisory / Derived calculations / Source and taxonomy / Version format compliance
Revision 1.2	Apr 18, 2012	Group: Derived calculations
Revision 1.3	Oct 25, 2017	Group: Refinement description / Category: software / Item: _software.name

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	3b8o.cif.gz	362.5 KB	Display	PDBx/mmCIF format
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Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/b8/3b8o ftp://data.pdbj.org/pub/pdb/validation_reports/b8/3b8o	HTTPS FTP

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Related structure data

Related structure data	3b8mC 3b8nC 3b8pC C: citing same article (ref.)
Similar structure data	4wl1-3 4wl1-2 4wl1-1 4wl1-4 6a7h-d 6a8j-d 7l6o-d 21111 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: Lipopolysaccharide biosynthesis protein wzzE

B: Lipopolysaccharide biosynthesis protein wzzE

C: Lipopolysaccharide biosynthesis protein wzzE

D: Lipopolysaccharide biosynthesis protein wzzE

E: Lipopolysaccharide biosynthesis protein wzzE

F: Lipopolysaccharide biosynthesis protein wzzE

G: Lipopolysaccharide biosynthesis protein wzzE

H: Lipopolysaccharide biosynthesis protein wzzE

247 kDa, 8 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)	107.438, 108.299, 122.569
Angle α, β, γ (deg.)	90.000, 102.150, 90.000
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	B
2	1	A
1	2	C
2	2	A
1	3	D
2	3	A
1	4	E
2	4	A
1	5	F
2	5	A
1	6	G
2	6	A
1	7	H
2	7	A

NCS domain segments:

Component-ID: 1 / Beg label comp-ID: GLU / End label comp-ID: ASP / Refine code: 4 / Auth seq-ID: 55 - 319 / Label seq-ID: 1 - 265

Dom-ID	Ens-ID	Auth asym-ID	Label asym-ID
1	1	B	B
2	1	A	A
1	2	C	C
2	2	A	A
1	3	D	D
2	3	A	A
1	4	E	E
2	4	A	A
1	5	F	F
2	5	A	A
1	6	G	G
2	6	A	A
1	7	H	H
2	7	A	A

NCS ensembles :

ID
1
2
3
4
5
6
7

#1: Protein	Lipopolysaccharide biosynthesis protein wzzE Mass: 30913.971 Da / Num. of mol.: 8 / Fragment: Periplasmic domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: O157:H7 / Gene: wzzE, wzz / Plasmid: pGEX-4T1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P0AG01
#2: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 395 / Source method: isolated from a natural source / Formula: H₂O

#1: Protein

Lipopolysaccharide biosynthesis protein wzzE

Mass: 30913.971 Da / Num. of mol.: 8 / Fragment: Periplasmic domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli) / Strain: O157:H7 / Gene: wzzE, wzz / Plasmid: pGEX-4T1 / Species (production host): Escherichia coli / Production host:

Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P0AG01

#2: Water

ChemComp-HOH / water /

Water

Mass: 18.015 Da / Num. of mol.: 395 / 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: 2.82 Å³/Da / Density % sol: 56.36 %
Crystal grow	Temperature: 298 K / pH: 7 Details: PEG 3350, pH 7.0, vapor diffusion, temperature 298K, pH 7.00

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.1
Detector	Type: ADSC QUANTUM 315 / Detector: CCD
Radiation	Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.1 Å / Relative weight: 1
Reflection	Resolution: 2.3→50 Å / Num. obs: 117899 / % possible obs: 96.8 % / Redundancy: 3.4 % / R_merge(I) obs: 0.083 / Net I/σ(I): 9.3
Reflection shell	Resolution: 2.3→2.38 Å / Redundancy: 2.4 % / R_merge(I) obs: 0.297 / % possible all: 78.8

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Phasing

Phasing

Method:

SAD

Phasing MAD set

ID	R cullis acentric	R cullis centric	Highest resolution (Å)	Lowest resolution (Å)	Reflection acentric	Reflection centric
ISO_1	0	0	2.39	39.41	96920	3205
ANO_1	0.759	0	2.39	39.41	94689	0

Phasing MAD set shell

ID	Resolution (Å)	R cullis acentric	Reflection acentric	Reflection centric
ISO_1	10.34-39.41	0	1200	165
ISO_1	7.44-10.34	0	2149	179
ISO_1	6.11-7.44	0	2752	173
ISO_1	5.31-6.11	0	3280	178
ISO_1	4.76-5.31	0	3711	173
ISO_1	4.35-4.76	0	4107	178
ISO_1	4.03-4.35	0	4469	175
ISO_1	3.77-4.03	0	4849	177
ISO_1	3.56-3.77	0	5044	171
ISO_1	3.37-3.56	0	5417	171
ISO_1	3.22-3.37	0	5686	180
ISO_1	3.08-3.22	0	5972	173
ISO_1	2.96-3.08	0	6219	179
ISO_1	2.86-2.96	0	6469	173
ISO_1	2.76-2.86	0	6655	177
ISO_1	2.67-2.76	0	6812	174
ISO_1	2.59-2.67	0	6708	138
ISO_1	2.52-2.59	0	5890	115
ISO_1	2.45-2.52	0	5180	87
ISO_1	2.39-2.45	0	4351	69
ANO_1	10.34-39.41	0.349	1187	0
ANO_1	7.44-10.34	0.33	2143	0
ANO_1	6.11-7.44	0.345	2746	0
ANO_1	5.31-6.11	0.374	3280	0
ANO_1	4.76-5.31	0.423	3706	0
ANO_1	4.35-4.76	0.46	4105	0
ANO_1	4.03-4.35	0.521	4468	0
ANO_1	3.77-4.03	0.582	4846	0
ANO_1	3.56-3.77	0.682	5026	0
ANO_1	3.37-3.56	0.683	5414	0
ANO_1	3.22-3.37	0.732	5680	0
ANO_1	3.08-3.22	0.781	5958	0
ANO_1	2.96-3.08	0.824	6197	0
ANO_1	2.86-2.96	0.861	6421	0
ANO_1	2.76-2.86	0.894	6558	0
ANO_1	2.67-2.76	0.919	6652	0
ANO_1	2.59-2.67	0.944	6384	0
ANO_1	2.52-2.59	0.958	5432	0
ANO_1	2.45-2.52	0.964	4646	0
ANO_1	2.39-2.45	0.971	3840	0

Phasing MAD set site

ID	Cartn x (Å)	Cartn y (Å)	Cartn z (Å)	Atom type symbol	B iso	Occupancy
1	36.551	97.063	71.671	SE	28.37	0.13
2	70.245	91.35	50.169	SE	27.57	0.12
3	90.996	112.026	50.033	SE	30.19	0.13
4	31.326	117.172	69.83	SE	44.61	0.13
5	61.653	130.764	114.64	SE	58.43	0.15
6	72.891	106.037	72.225	SE	27.27	0.12
7	99.392	96.693	28.414	SE	51.38	0.12
8	45.202	130.544	84.813	SE	51.13	0.12
9	93.423	132.041	70.052	SE	45.16	0.11
10	77.212	143.015	114.705	SE	58.8	0.13
11	78.112	85.851	70.087	SE	44	0.14
12	65.268	112.136	69.433	SE	31.03	0.1
13	70.974	135.057	96.646	SE	50.46	0.12
14	49.851	121.073	91.064	SE	49.48	0.12
15	102.622	132.899	73.133	SE	29.07	0.11
16	32.685	143.213	116.158	SE	55.67	0.12
17	51.347	129.353	96.578	SE	48.63	0.11
18	65.822	125.482	49.441	SE	30.16	0.1
19	85.276	119.899	48.087	SE	38.24	0.1
20	7.974	126.866	124.733	SE	62.01	0.14
21	-3.511	136.447	148.293	SE	45.78	0.1
22	79.49	149.447	116.065	SE	77.41	0.14
23	41.943	133.72	114.49	SE	51.41	0.12
24	107.743	97.998	22.953	SE	56.06	0.12
25	74.873	124.775	46.329	SE	26.97	0.09
26	28.315	159.201	96.77	SE	48.36	0.12
27	23.579	114.499	124.843	SE	56.17	0.14
28	77.528	95.169	73.648	SE	26.24	0.09
29	-8.405	126.857	154.576	SE	53.47	0.12
30	44.153	91.105	69.411	SE	33.26	0.09
31	27.643	136.722	90.43	SE	71.52	0.13
32	25.839	108.002	123.641	SE	59.92	0.11
33	32.101	107.864	73.291	SE	37.63	0.1
34	-25.952	120.456	148.897	SE	58.26	0.13
35	29.425	149.141	114.664	SE	65.64	0.14
36	13.901	123.63	123.296	SE	61.78	0.1
37	17.347	122.434	142.888	SE	51.38	0.1
38	-28.301	112.828	154.6	SE	29.02	0.07
39	-11.611	123.713	124.93	SE	63.78	0.12
40	-20.87	114.25	123.479	SE	59.56	0.11
41	25.348	144.503	84.764	SE	18.21	0.06
42	-2.116	128.109	142.821	SE	45.6	0.1
43	-24.138	108.281	124.85	SE	59.79	0.12
44	19.745	160.563	91.446	SE	54.59	0.1
45	67.523	133.869	116.133	SE	47.2	0.09
46	75.782	83.576	48.407	SE	21.44	0.07
47	48.302	131.602	116.011	SE	66.71	0.11
48	108.874	91.711	34.661	SE	64.26	0.1
49	73.501	128.258	91.041	SE	28.48	0.07
50	19.974	129.05	148.689	SE	78.22	0.11
51	-5.205	125.922	123.469	SE	78.9	0.11
52	109.454	121.783	85.793	SE	100.99	0.08
53	-27.647	139.11	141.162	SE	115.65	0.13
54	29.119	165.807	84.993	SE	60.85	0.09
55	21.589	100.917	85.722	SE	68.94	0.08
56	92.111	126.22	98.519	SE	106.17	0.1
57	81.577	135.721	33.802	SE	74	0.07
58	88.1	102.276	85.725	SE	107.5	0.11
59	66.245	126.37	84.872	SE	39.45	0.05
60	26.187	118.205	98.341	SE	105.02	0.12
61	79.246	106.833	98.226	SE	113.95	0.11
62	-18.978	117.22	143.669	SE	138.38	0.11
63	113.985	130.909	98.141	SE	93.11	0.1
64	30.533	96.311	98.379	SE	113.55	0.12
65	34.59	140.156	95.77	SE	109.35	0.1
66	86.327	126.42	21.49	SE	140.4	0.13
67	12.732	131.269	154.511	SE	34.54	0.06
68	65.891	22.024	85.602	SE	58.06	0.06
69	38.152	18.863	34.128	SE	56.53	0.04
70	64.221	22.436	21.466	SE	58.43	0.06
71	33.947	33.61	92.981	SE	54.76	0.03
72	9.558	11.24	96.635	SE	60.63	0.1

Phasing dm

FOM : 0.71 / FOM acentric: 0.71 / FOM centric: 0.61 / Reflection: 83750 / Reflection acentric: 80833 / Reflection centric: 2917

Phasing dm shell

Resolution (Å)	FOM	FOM acentric	FOM centric	Reflection	Reflection acentric	Reflection centric
7.4-29.924	0.93	0.94	0.83	3680	3341	339
4.6-7.4	0.89	0.89	0.72	11283	10712	571
3.7-4.6	0.88	0.89	0.75	14097	13578	519
3.3-3.7	0.83	0.83	0.71	14252	13806	446
2.8-3.3	0.62	0.62	0.45	25242	24550	692
2.6-2.8	0.4	0.41	0.24	15196	14846	350

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Processing

Software

Name	Version	Classification
SCALEPACK		data scaling
SHARP		phasing
RESOLVE	2.13	phasing
REFMAC	refmac_5.2.0019	refinement
PDB_EXTRACT	2	data extraction
DENZO		data reduction

Refinement

Method to determine structure:

SAD / Resolution: 2.4→47.89 Å / Cor.coef. F_o:F_c: 0.918 / Cor.coef. F_o:F_c free: 0.887 / SU B: 15.903 / SU ML: 0.186 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.324 / ESU R Free: 0.249 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.26562	5290	5 %	RANDOM
R_work	0.22333	-	-	-
obs	0.22546	101074	99.06 %	-

Solvent computation

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

Displacement parameters

B_iso mean: 54.193 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.09 Å²	0 Å²	0 Å²
2-	-	-0.16 Å²	0 Å²
3-	-	-	0.06 Å²

Refinement step

Cycle: LAST / Resolution: 2.4→47.89 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	14376	0	0	395	14771

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.017	0.022	14640
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.365	1.942	19800
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.735	5	1744
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.631	24.216	816
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	19.111	15	2536
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	17.462	15	144
X-RAY DIFFRACTION	r_chiral_restr	0.093	0.2	2128
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	11360
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.202	0.2	6843
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.295	0.2	10046
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.162	0.2	547
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	0.239	0.2	46
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.264	0.2	3
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	1.849	3	9098
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	2.765	6	14184
X-RAY DIFFRACTION	r_scbond_it	2.93	4	6379
X-RAY DIFFRACTION	r_scangle_it	4.459	8	5616
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Dom-ID: 1 / Number: 1797 / Refine-ID: X-RAY DIFFRACTION

Ens-ID	Auth asym-ID	Type	Rms dev position (Å)	Weight position
1	B	medium positional	0.39	0.5
2	C	medium positional	0.27	0.5
3	D	medium positional	0.32	0.5
4	E	medium positional	0.25	0.5
5	F	medium positional	0.39	0.5
6	G	medium positional	0.27	0.5
7	H	medium positional	0.36	0.5
1	B	medium thermal	0.85	2
2	C	medium thermal	0.7	2
3	D	medium thermal	0.76	2
4	E	medium thermal	0.78	2
5	F	medium thermal	0.79	2
6	G	medium thermal	0.7	2
7	H	medium thermal	0.72	2

LS refinement shell

Resolution: 2.4→2.462 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.295	343	-
R_work	0.241	7112	-
obs	-	-	93.97 %

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	5.3511	-2.8882	0.6997	2.7941	0.1546	3.6985	-0.0605	0.0125	-0.1877	0.1361	0.0599	0.3154	0.0369	-0.2252	0.0006	-0.2053	0.0102	-0.0265	-0.197	0.0115	-0.0939	56.145	16.406	44.018
2	0.128	0.6315	1.3623	3.1371	6.5087	16.5009	-0.2227	0.2343	0.1352	-0.5748	0.141	-0.0955	-0.291	-0.0413	0.0817	0.3191	-0.0356	-0.0145	0.2248	-0.0225	0.0328	53.299	2.267	4.859
3	2.4568	-0.3339	0.1036	4.5154	-0.7099	1.6532	-0.0653	-0.2343	-0.0126	-0.054	-0.0177	0.041	-0.2061	-0.1198	0.0829	-0.1898	0.0189	-0.0086	-0.1612	-0.0216	-0.1607	63.421	-10.583	44.285
4	2.9691	1.89	5.0412	1.8339	4.8034	12.5888	-0.0775	0.4503	-0.0817	-0.4127	0.0389	-0.0587	-0.3946	0.1601	0.0386	0.4204	-0.0023	-0.0583	0.0804	-0.022	-0.0394	52.062	-18.842	4.941
5	2.8465	1.9286	-0.5145	4.4249	-0.8462	2.8375	-0.0239	-0.0917	0.0491	0.0316	0.0132	-0.0434	-0.1438	-0.0334	0.0107	-0.2226	-0.0092	0.0152	-0.1646	-0.0077	-0.1191	49.387	-35.674	44.334
6	3.7369	-0.9504	6.1209	0.3918	-0.75	14.3636	0.1472	0.7185	-0.0536	-0.3096	-0.317	-0.0686	-0.0646	0.2951	0.1698	0.1342	-0.0136	0.0282	0.3476	-0.0136	0.0111	35.566	-32.63	5.038
7	3.0143	0.3853	-0.7451	1.8666	-0.6132	2.9142	-0.0418	0.0423	0.0212	0.2118	0.0543	-0.0085	-0.2442	0.1137	-0.0125	-0.1979	0.0337	0.0289	-0.1833	-0.0007	-0.1276	22.53	-43.454	44.181
8	1.7935	-1.9578	4.5187	3.1187	-4.8185	11.3979	0.0429	0.4325	-0.1969	-0.486	0.1076	0.1606	0.0942	0.2031	-0.1505	0.0699	-0.0753	0.0023	0.343	0.0366	-0.0039	14.505	-31.645	4.924
9	3.1333	-1.6665	-0.2965	2.7451	-0.2611	3.6284	-0.0295	-0.0459	0.0918	0.0093	0.0032	-0.1468	0.0068	0.2182	0.0263	-0.2363	0.0424	0.006	-0.1839	-0.0032	-0.1677	-2.269	-29.573	44.014
10	0.3492	0.797	-1.2822	2.8041	-5.9406	16.3228	-0.2105	0.3139	-0.0858	-0.6198	0.103	-0.0005	0.1572	-0.0344	0.1074	0.3049	-0.008	0.0202	0.1466	0.0111	-0.0441	0.464	-15.552	4.803
11	1.5895	-0.4509	-0.4549	3.1179	0.7824	1.7641	0.007	-0.1389	0.0616	-0.0818	-0.0245	-0.0157	0.1477	0.2149	0.0175	-0.2267	0.0123	-0.0015	-0.1519	-0.0125	-0.1631	-9.615	-2.606	44.197
12	2.8766	1.921	-4.9117	1.696	-4.4389	11.6369	0.0306	0.4596	0.1796	-0.3467	0.0446	0.0406	0.0798	-0.1584	-0.0751	0.4676	0.0742	0.092	0.1215	0.0536	-0.0083	1.784	5.536	4.84
13	2.6084	2.422	0.0647	3.1484	0.003	2.7731	0.0407	-0.0969	-0.0491	0.0765	-0.0539	-0.0487	0.1719	0.0776	0.0132	-0.2075	-0.0344	0.0005	-0.1178	-0.0121	-0.0814	4.474	22.22	44.011
14	4.4755	-1.1605	-5.7945	0.4394	0.664	12.5782	0.2827	0.8589	0.1739	-0.3373	-0.3855	0.0071	-0.1588	-0.1813	0.1028	0.1682	0.0024	0.0328	0.4111	0.0253	0.041	18.184	19.417	4.852
15	3.5813	0.5987	0.9578	2.5752	0.9432	2.6277	0.0142	0.0576	-0.0059	0.2495	-0.0297	-0.0682	0.2436	-0.2213	0.0155	-0.2069	-0.0008	-0.0041	-0.1431	0.0415	-0.1047	31.235	30.128	44.168
16	1.6416	-2.0206	-4.5824	3.4529	5.6072	12.7928	0.1119	0.3614	0.1842	-0.5541	0.1453	-0.2431	-0.2306	-0.3834	-0.2572	0.0711	-0.1022	0.0213	0.4073	-0.0207	0.0503	39.346	18.446	4.808

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	55 - 65	1 - 11
2	X-RAY DIFFRACTION	1	A	A	95 - 181	41 - 127
3	X-RAY DIFFRACTION	1	A	A	307 - 319	253 - 265
4	X-RAY DIFFRACTION	2	A	A	66 - 85	12 - 31
5	X-RAY DIFFRACTION	2	A	A	182 - 306	128 - 252
6	X-RAY DIFFRACTION	3	B	B	55 - 65	1 - 11
7	X-RAY DIFFRACTION	3	B	B	95 - 181	41 - 127
8	X-RAY DIFFRACTION	3	B	B	307 - 319	253 - 265
9	X-RAY DIFFRACTION	4	B	B	66 - 85	12 - 31
10	X-RAY DIFFRACTION	4	B	B	182 - 306	128 - 252
11	X-RAY DIFFRACTION	5	C	C	55 - 65	1 - 11
12	X-RAY DIFFRACTION	5	C	C	95 - 181	41 - 127
13	X-RAY DIFFRACTION	5	C	C	307 - 319	253 - 265
14	X-RAY DIFFRACTION	6	C	C	66 - 85	12 - 31
15	X-RAY DIFFRACTION	6	C	C	182 - 306	128 - 252
16	X-RAY DIFFRACTION	7	D	D	55 - 65	1 - 11
17	X-RAY DIFFRACTION	7	D	D	95 - 181	41 - 127
18	X-RAY DIFFRACTION	7	D	D	307 - 319	253 - 265
19	X-RAY DIFFRACTION	8	D	D	66 - 85	12 - 31
20	X-RAY DIFFRACTION	8	D	D	182 - 306	128 - 252
21	X-RAY DIFFRACTION	9	E	E	55 - 65	1 - 11
22	X-RAY DIFFRACTION	9	E	E	95 - 181	41 - 127
23	X-RAY DIFFRACTION	9	E	E	307 - 319	253 - 265
24	X-RAY DIFFRACTION	10	E	E	66 - 85	12 - 31
25	X-RAY DIFFRACTION	10	E	E	182 - 306	128 - 252
26	X-RAY DIFFRACTION	11	F	F	55 - 65	1 - 11
27	X-RAY DIFFRACTION	11	F	F	95 - 181	41 - 127
28	X-RAY DIFFRACTION	11	F	F	307 - 319	253 - 265
29	X-RAY DIFFRACTION	12	F	F	66 - 85	12 - 31
30	X-RAY DIFFRACTION	12	F	F	182 - 306	128 - 252
31	X-RAY DIFFRACTION	13	G	G	55 - 65	1 - 11
32	X-RAY DIFFRACTION	13	G	G	95 - 181	41 - 127
33	X-RAY DIFFRACTION	13	G	G	307 - 319	253 - 265
34	X-RAY DIFFRACTION	14	G	G	66 - 85	12 - 31
35	X-RAY DIFFRACTION	14	G	G	182 - 306	128 - 252
36	X-RAY DIFFRACTION	15	H	H	55 - 65	1 - 11
37	X-RAY DIFFRACTION	15	H	H	95 - 181	41 - 127
38	X-RAY DIFFRACTION	15	H	H	307 - 319	253 - 265
39	X-RAY DIFFRACTION	16	H	H	66 - 85	12 - 31
40	X-RAY DIFFRACTION	16	H	H	182 - 306	128 - 252

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