PDB-2wqu: Internalin domain of Listeria monocytogenes InlB: triclinic cryst...

ID or keywords:

Entry

Database: PDB / ID: 2wqu

Title

Internalin domain of Listeria monocytogenes InlB: triclinic crystal form

Components

INTERNALIN B

Keywords

CELL INVASION / HGF RECEPTOR LIGAND / LEUCINE RICH REPEAT / LRR / C-MET LIGAND / VIRULENCE FACTOR

Function / homology

Function and homology information

peptidoglycan-based cell wall / InlB-mediated entry of Listeria monocytogenes into host cell / heparin binding / lipid binding / cell surface / extracellular region / metal ion binding / plasma membrane / cytoplasm
Similarity search - Function

Biological species

LISTERIA MONOCYTOGENES (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.6 Å

Authors

Niemann, H.H. / Heinz, D.W.

Citation

Journal: J.Mol.Biol. / Year: 2010
Title: Ligand-Mediated Dimerization of the met Receptor Tyrosine Kinase by the Bacterial Invasion Protein Inlb.
Authors: Ferraris, D.M. / Gherardi, E. / Di, Y. / Heinz, D.W. / Niemann, H.H.

History

Deposition	Aug 27, 2009	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Nov 10, 2009	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.2	Mar 6, 2019	Group: Data collection / Experimental preparation / Other Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval
Revision 1.3	May 8, 2019	Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method
Revision 1.4	Dec 20, 2023	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_initial_refinement_model / struct_site 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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Remark 700

SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ...

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2wqu.cif.gz	332.6 KB	Display	PDBx/mmCIF format
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PDBx/mmJSON format	2wqu.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/wq/2wqu ftp://data.pdbj.org/pub/pdb/validation_reports/wq/2wqu	HTTPS FTP

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Related structure data

Related structure data	2wqvC 2wqwC 2wqxC 1h6tS 1d0b 1m9s 1otm 1otn 1oto 2uzx 2uzy S: Starting model for refinement C: citing same article (ref.)
Similar structure data	2wqv-2 2wqv-1 2i5v-d 6zzh-2 4qb7-d 4aw4-3 1all-d 2wqx-1 2wqx-2 5hno-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) Search similar-shape structures by Omokage search (details) 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

Related structure data

S: Starting model for refinement

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#143 - Nov 2011 Toll-like Receptors similarity (5) #248 - Aug 2020 Phytosulfokine Receptor similarity (5) #245 - May 2020 Spliceosomes similarity (3) #60 - Dec 2004 Ubiquitin similarity (1) #68 - Aug 2005 Neurotrophins similarity (2) #105 - Sep 2008 Ribonuclease A similarity (2) #234 - Jun 2019 MDM2 and Cancer similarity (1)

Deposited unit

A: INTERNALIN B

B: INTERNALIN B

C: INTERNALIN B

D: INTERNALIN B

E: INTERNALIN B

F: INTERNALIN B

hetero molecules

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

1

A: INTERNALIN B

hetero molecules

defined by author&software
32.6 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: INTERNALIN B

hetero molecules

defined by author&software
32.6 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: INTERNALIN B

hetero molecules

defined by author&software
32.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: INTERNALIN B

defined by author&software
32.2 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

5

E: INTERNALIN B

hetero molecules

defined by author&software
32.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

6

F: INTERNALIN B

hetero molecules

defined by author&software
32.8 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	59.660, 70.650, 124.660
Angle α, β, γ (deg.)	74.47, 83.13, 85.65
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS oper:

ID	Code	Matrix	Vector
1	given	(-0.83625, -0.52905, 0.14423), (-0.54805, 0.79762, -0.25189), (0.01822, -0.28969, -0.95695)	58.20268, 17.40254, -0.28812
2	given	(0.84201, 0.52067, -0.14113), (-0.52807, 0.74205, -0.41292), (-0.11026, 0.42221, 0.89977)	38.46272, 21.7145, -51.93545
3	given	(-0.99806, 0.0616, 0.00865), (0.06211, 0.99461, 0.08303), (-0.00349, 0.0834, -0.99651)	1.68736, 0.25157, -0.45215
4	given	(0.64842, -0.61765, -0.44504), (0.56733, 0.00224, 0.82349), (-0.50763, -0.78645, 0.35186)	53.24129, -29.90241, 67.21381
5	given	(-0.56188, 0.61861, 0.54919), (0.62709, -0.11444, 0.77049), (0.53949, 0.77732, -0.32362)	49.56183, 6.49988, 0.71027

#1: Protein	INTERNALIN B Mass: 32243.818 Da / Num. of mol.: 6 / Fragment: INTERNALIN DOMAIN, RESIDUES 36-321 Source method: isolated from a genetically manipulated source Source: (gene. exp.) LISTERIA MONOCYTOGENES (bacteria) / Strain: EGD-E / Plasmid: PETM30 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODONPLUS / References: UniProt: P25147, UniProt: P0DQD2*PLUS
#2: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: SO₄
#3: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₃H₈O₃
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 61 / 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: 2.6 Å³/Da / Density % sol: 52.7 % / Description: NONE
Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop Details: SITTING DROP AT 293K WITH 200 NL PROTEIN PLUS 100 NL RESERVOIR SOLUTION CONSISTING OF: 0.1 M LI2SO4, 0.1 M NA-CITRATE PH 5.6, 30% PEG400. THE PROTEIN WAS A COMPLEX CONSISTING OF MET741 AND ...Details: SITTING DROP AT 293K WITH 200 NL PROTEIN PLUS 100 NL RESERVOIR SOLUTION CONSISTING OF: 0.1 M LI2SO4, 0.1 M NA-CITRATE PH 5.6, 30% PEG400. THE PROTEIN WAS A COMPLEX CONSISTING OF MET741 AND INLB321 AT 5 MG/ML, I.E. INLB321 WAS AT 1.4 MG7ML. CRYSTAL GROWTH TIME WAS SEVERAL MONTHS.

Crystal

Density Matthews: 2.6 Å³/Da / Density % sol: 52.7 % / Description: NONE

Crystal grow

Temperature: 293 K / Method: vapor diffusion, sitting drop
Details: SITTING DROP AT 293K WITH 200 NL PROTEIN PLUS 100 NL RESERVOIR SOLUTION CONSISTING OF: 0.1 M LI2SO4, 0.1 M NA-CITRATE PH 5.6, 30% PEG400. THE PROTEIN WAS A COMPLEX CONSISTING OF MET741 AND ...

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.873
Detector	Type: MARRESEARCH / Detector: CCD / Date: May 19, 2006
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.873 Å / Relative weight: 1
Reflection	Resolution: 2.6→20 Å / Num. obs: 55139 / % possible obs: 92.1 % / Observed criterion σ(I): -3 / Redundancy: 4.96 % / R_merge(I) obs: 0.14 / Net I/σ(I): 10.13
Reflection shell	Resolution: 2.6→2.67 Å / Redundancy: 3.42 % / R_merge(I) obs: 0.7 / Mean I/σ(I) obs: 2.59 / % possible all: 74.8

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Processing

Software

Name	Version	Classification
REFMAC	5.5.0102	refinement
XDS		data reduction
XSCALE		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1H6T

1h6t

Resolution: 2.6→20 Å / Cor.coef. F_o:F_c: 0.935 / Cor.coef. F_o:F_c free: 0.887 / SU B: 25.185 / SU ML: 0.242 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.342 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.249	2746	5 %	RANDOM
R_work	0.191	-	-	-
obs	0.194	52393	92.4 %	-

Solvent computation

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

Displacement parameters

B_iso mean: 30.64 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.02 Å²	-0.41 Å²	-0.01 Å²
2-	-	2.07 Å²	-0.38 Å²
3-	-	-	-1.78 Å²

Refinement step

Cycle: LAST / Resolution: 2.6→20 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13226	0	103	61	13390

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.006	0.022	13534
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	8974
X-RAY DIFFRACTION	r_angle_refined_deg	0.978	1.992	18376
X-RAY DIFFRACTION	r_angle_other_deg	0.812	3	22379
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.465	5	1683
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	42.214	26.951	574
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	13.333	15	2555
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	15.2	15	24
X-RAY DIFFRACTION	r_chiral_restr	0.054	0.2	2218
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.021	14555
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	2202
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
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
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
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	0.141	1.5	8421
X-RAY DIFFRACTION	r_mcbond_other	0.023	1.5	3359
X-RAY DIFFRACTION	r_mcangle_it	0.28	2	13761
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	0.484	3	5113
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	0.837	4.5	4610
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

LS refinement shell

Resolution: 2.6→2.67 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.311	160	-
R_work	0.255	3070	-
obs	-	-	74.92 %

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	5.2809	-0.025	5.057	3.2855	0.5335	9.0421	0.0938	-0.65	0.0817	0.631	0.0512	-0.0457	0.2325	-0.4831	-0.145	0.2379	0.0143	0.0193	0.2053	0.0828	0.1341	19.222	10.9506	44.7411
2	2.1253	-1.433	-0.1081	4.37	-2.4407	8.3352	-0.051	-0.0253	0.1822	0.1364	0.0264	-0.5176	-0.212	0.5399	0.0246	0.0893	0.0179	-0.0006	0.1439	0.0008	0.1623	22.6478	14.601	30.1473
3	1.6516	-0.8596	1.097	1.1921	-0.7149	3.6638	0.0272	-0.0098	-0.0701	-0.073	0.0481	0.1169	0.1035	0.1135	-0.0753	0.0263	-0.008	0.0186	0.0066	0.032	0.1178	16.858	18.0199	4.8349
4	15.6971	-3.9487	-1.5962	8.9299	-4.622	2.3955	0.5017	0.637	0.5078	-1.3118	-0.4164	0.4485	-0.1299	-0.6693	-0.0853	0.257	0.1547	-0.0988	0.2811	0.0317	0.1278	1.3186	31.4617	-12.9935
5	8.0439	-9.0139	2.36	14.7733	-2.1129	2.3578	0.1392	0.5098	-0.7913	0.8817	-0.4877	0.9045	0.3324	-0.1428	0.3485	0.1232	0.0076	0.0429	0.1819	0.0088	0.0703	7.9931	17.4359	-4.0357
6	5.0108	3.3213	-0.206	6.2981	0.7003	3.9066	-0.0961	0.1725	-0.3077	-0.2719	0.1686	-0.2074	0.2597	0.4417	-0.0725	0.1735	0.0262	0.0427	0.1041	-0.0386	0.1935	42.9951	2.4649	-46.4148
7	4.2364	0.7693	1.6316	5.8906	2.6488	5.8884	-0.1474	-0.2461	-0.047	0.0786	0.0333	0.0759	-0.1724	0.0291	0.1141	0.0533	-0.0065	0.0459	0.1557	0.0461	0.0364	37.4223	10.444	-34.3323
8	1.1184	0.2149	0.2659	1.5493	1.529	7.3428	-0.0052	0.1749	-0.1154	-0.029	-0.0434	0.0681	0.059	-0.0517	0.0486	-0.0157	0.0196	-0.0006	0.1209	0.0392	0.0779	34.0262	14.6749	-14.9278
9	1.2731	0.0556	-1.012	8.9665	-0.7301	4.953	0.4058	-0.3942	0.6419	0.0026	-0.0851	0.687	-1.4586	0.0238	-0.3208	0.3914	-0.062	0.1052	0.2365	-0.12	0.3208	36.8783	35.7568	-0.1002
10	3.9899	0.23	0.2905	10.0698	1.9532	5.461	0.1579	-0.4953	0.5547	0.9951	-0.1491	-0.1407	-1.0712	0.589	-0.0088	0.3683	-0.1692	0.1147	0.2477	-0.0888	0.103	40.4414	32.9395	0.7737
11	8.3036	-2.7173	-1.3054	13.0151	-0.3718	4.6702	-0.3208	-0.6356	-0.509	0.6005	0.1981	0.1251	0.4731	-0.2028	0.1227	0.1707	-0.043	0.0554	0.1683	0.0306	0.1418	53.726	-0.7622	-6.9606
12	2.8607	-0.9161	-0.2663	7.7991	-1.2391	6.2512	0.1141	0.2044	-0.1744	-0.1524	-0.1317	0.1431	-0.0871	0.0445	0.0176	0.0262	0.0318	0.0395	0.2338	0.0047	0.0645	58.5193	8.3374	-19.5599
13	1.1381	0.049	-1.8461	3.7908	-2.1425	5.9991	-0.1161	-0.0733	-0.1477	0.0891	0.0243	-0.1815	0.1135	0.3307	0.0919	0.0123	0.0258	-0.0183	0.2108	0.0228	0.1385	64.3676	13.7576	-32.8464
14	1.6609	-0.0823	-0.2548	5.5593	-1.3571	6.196	0.0277	0.3245	0.4032	-0.0181	0.1199	0.0616	-0.6088	-0.2631	-0.1476	0.0616	0.035	0.0063	0.2551	0.0806	0.168	59.7864	27.3737	-46.7308
15	2.5939	-0.767	1.2056	12.04	1.0479	5.663	-0.0484	0.2748	0.3812	-0.5015	-0.1628	0.4603	-0.8732	-0.4114	0.2112	0.2881	0.0828	0.0485	0.3792	0.1399	0.241	55.3781	33.4981	-51.3241
16	10.3498	5.8346	4.8094	4.8036	2.0407	10.6977	-0.758	1.9311	-0.4517	-1.0188	0.73	0.0953	-0.0921	1.5101	0.028	0.4923	-0.1495	0.0284	0.829	-0.0394	0.2132	78.0429	19.472	-100.9288
17	8.1174	2.3014	2.9567	3.3567	2.5809	9.2622	-0.1791	-0.0186	0.2036	-0.4373	-0.0083	0.2302	-0.218	-0.0843	0.1873	0.1953	0.0156	0.0161	0.1872	0.0016	0.1256	74.8448	20.5896	-86.156
18	0.5771	0.3571	-0.0939	2.5022	-0.6109	5.7935	0.0058	0.0452	-0.0273	-0.1005	-0.0731	0.1664	0.0996	-0.5055	0.0673	0.0166	-0.0108	0.0062	0.1728	-0.0081	0.1424	74.9586	20.8955	-64.1645
19	2.1026	1.2348	1.3014	2.6406	0.7983	2.8353	-0.142	0.0088	0.1001	0.0049	0.0866	-0.1082	-0.1575	-0.1009	0.0554	0.0886	0.0514	-0.0113	0.1817	0.032	0.1174	87.2832	25.3719	-46.0932
20	3.2527	4.3887	2.5066	13.0076	3.8715	6.1859	-0.0917	-0.1398	-0.2139	0.1074	0.18	-0.7505	-0.0857	0.1274	-0.0883	0.0519	0.0645	0.0176	0.0867	0.0657	0.1035	91.6511	26.0019	-44.0998
21	7.9409	2.5896	0.1477	11.9846	-1.509	7.5524	-0.2122	-0.5739	0.7123	0.6537	-0.1088	0.3954	0.019	-0.1044	0.321	0.3421	0.0875	-0.058	0.1582	-0.0733	0.2783	36.7069	19.831	66.168
22	2.4043	-0.0515	-0.5964	5.8673	1.5424	2.247	-0.0786	0.1094	0.0196	-0.1065	-0.0436	-0.3034	-0.1307	-0.0256	0.1222	0.2343	0.0401	-0.0711	0.1003	0.0255	0.1375	43.6694	9.5208	57.8582
23	2.1134	-1.6433	0.2001	4.5017	1.1671	3.2213	0.0255	-0.1003	0.0137	0.2142	0.0546	-0.3965	-0.0177	0.1941	-0.0801	0.1104	-0.0485	-0.0123	0.0754	0.043	0.1702	53.3147	-8.2253	48.219
24	4.3956	1.9395	2.7468	6.5047	2.9488	3.8266	0.2444	0.318	-0.2151	0.6878	-0.3635	0.0017	0.4876	-0.1534	0.1191	0.2308	-0.0205	0.0693	0.153	0.0343	0.1557	45.9211	-32.3986	40.8309
25	7.0524	0.9678	3.5495	3.8113	2.1334	6.0332	0.3543	-0.5541	-0.1719	0.87	-0.3918	-0.0216	0.6414	-0.7589	0.0374	0.3943	-0.0069	0.0798	0.1403	0.0473	0.1655	45.3347	-32.8813	43.9307
26	1.8138	3.6175	0.4589	11.5468	-1.1778	4.6824	-0.2486	0.3959	0.3861	-0.4734	0.149	-0.4467	-0.3736	0.1303	0.0996	0.1912	0.001	0.0238	0.1917	0.1015	0.2338	69.944	51.8963	4.4475
27	4.8743	-0.8173	-0.1742	8.5591	-3.3048	2.8951	-0.0824	-0.28	0.1654	0.6437	0.0387	0.1672	-0.1597	-0.0181	0.0437	0.1386	0.0165	0.0168	0.1203	-0.0064	0.16	63.5451	42.1633	14.7005
28	3.0587	1.2654	0.2723	2.9257	-0.6679	2.1712	0.0573	-0.1667	0.2235	-0.1564	-0.013	0.0799	-0.0592	-0.1307	-0.0443	0.04	0.0226	0.0167	0.0914	-0.0034	0.1285	52.7592	25.5601	19.7046
29	5.1716	-1.3205	2.6589	4.435	-2.5444	4.3749	-0.0138	0.1797	-0.5088	-0.2571	0.0076	-0.1046	0.3289	0.1445	0.0062	0.123	-0.0542	0.03	0.0507	-0.0251	0.1672	56.1665	0.5062	26.2097
30	16.3581	-7.0668	11.9865	12.4947	-10.9804	12.9005	0.9026	1.6905	-0.0136	0.0015	-0.8669	-0.1793	-0.0418	1.6061	-0.0357	0.1464	-0.0062	0.1405	0.156	0.0261	0.0962	61.9816	4.3162	25.8097

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	36 - 89
2	X-RAY DIFFRACTION	2	A	90 - 144
3	X-RAY DIFFRACTION	3	A	145 - 275
4	X-RAY DIFFRACTION	4	A	276 - 294
5	X-RAY DIFFRACTION	5	A	295 - 320
6	X-RAY DIFFRACTION	6	B	36 - 84
7	X-RAY DIFFRACTION	7	B	85 - 138
8	X-RAY DIFFRACTION	8	B	139 - 236
9	X-RAY DIFFRACTION	9	B	237 - 275
10	X-RAY DIFFRACTION	10	B	276 - 320
11	X-RAY DIFFRACTION	11	C	37 - 76
12	X-RAY DIFFRACTION	12	C	77 - 138
13	X-RAY DIFFRACTION	13	C	139 - 193
14	X-RAY DIFFRACTION	14	C	194 - 276
15	X-RAY DIFFRACTION	15	C	277 - 318
16	X-RAY DIFFRACTION	16	D	37 - 68
17	X-RAY DIFFRACTION	17	D	69 - 141
18	X-RAY DIFFRACTION	18	D	142 - 228
19	X-RAY DIFFRACTION	19	D	229 - 276
20	X-RAY DIFFRACTION	20	D	277 - 320
21	X-RAY DIFFRACTION	21	E	37 - 69
22	X-RAY DIFFRACTION	22	E	70 - 138
23	X-RAY DIFFRACTION	23	E	139 - 235
24	X-RAY DIFFRACTION	24	E	236 - 278
25	X-RAY DIFFRACTION	25	E	279 - 320
26	X-RAY DIFFRACTION	26	F	37 - 89
27	X-RAY DIFFRACTION	27	F	90 - 141
28	X-RAY DIFFRACTION	28	F	142 - 240
29	X-RAY DIFFRACTION	29	F	241 - 310
30	X-RAY DIFFRACTION	30	F	311 - 320

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