PDB-5kew: Vibrio parahaemolyticus VtrA/VtrC complex bound to the bile salt ...

ID or keywords:

Entry

Database: PDB / ID: 5kew

Title

Vibrio parahaemolyticus VtrA/VtrC complex bound to the bile salt taurodeoxycholate

Components

VtrA Protein
VtrC Protein

Keywords

SIGNALING PROTEIN / heterodimer / alpha/beta / calycin beta barrel superfamily / bile salt receptor / taurodeoxycholate

Function / homology

Function and homology information

phosphorelay signal transduction system / regulation of DNA-templated transcription / DNA binding / membrane / metal ion binding
Similarity search - Function

Biological species

Vibrio parahaemolyticus serotype O3:K6

Method

X-RAY DIFFRACTION /

SYNCHROTRON / Resolution: 2.103 Å

Model details

The C-terminal periplasmic domain of VtrA extends from residue 160 to 253. The C-terminal ...

Authors

Tomchick, D.R. / Orth, K. / Rivera-Cancel, G.

Citation

Journal: Elife / Year: 2016
Title: Bile salt receptor complex activates a pathogenic type III secretion system.
Authors: Li, P. / Rivera-Cancel, G. / Kinch, L.N. / Salomon, D. / Tomchick, D.R. / Grishin, N.V. / Orth, K.

History

Deposition	Jun 10, 2016	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jul 20, 2016	Provider: repository / Type: Initial release
Revision 1.1	Mar 6, 2024	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_oper_list Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5kew.cif.gz	404.7 KB	Display	PDBx/mmCIF format
PDB format	pdb5kew.ent.gz	341.2 KB	Display	PDB format
PDBx/mmJSON format	5kew.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	5kew_validation.pdf.gz	1.3 MB	Display	wwPDB validaton report
Full document	5kew_full_validation.pdf.gz	1.3 MB	Display
Data in XML	5kew_validation.xml.gz	29.2 KB	Display
Data in CIF	5kew_validation.cif.gz	37.8 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ke/5kew ftp://data.pdbj.org/pub/pdb/validation_reports/ke/5kew	HTTPS FTP

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Related structure data

Related structure data	5kevC C: citing same article (ref.)
Similar structure data	1oun-d 3up8-1 1ghi-d 1qma-1 6nzq-2 2p76-5 3b3d-2 5nju-1 2g3i-d 4cwm-2 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

5kevC

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	#190 - Oct 2015 Two-component Systems similarity (4)

Deposited unit

A: VtrA Protein

B: VtrC Protein

C: VtrA Protein

D: VtrC Protein

E: VtrA Protein

F: VtrC Protein

hetero molecules

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

1

A: VtrA Protein

B: VtrC Protein

hetero molecules

defined by author&software
29.2 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: VtrA Protein

D: VtrC Protein

hetero molecules

defined by author&software
28.7 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

E: VtrA Protein

F: VtrC Protein

hetero molecules

defined by author&software
28.5 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	55.385, 71.276, 203.726
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁

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Protein , 2 types, 6 molecules ACEBDF

#1: Protein	VtrA Protein Mass: 10982.484 Da / Num. of mol.: 3 Fragment: VtrA C-terminal periplasmic domain, UNP residues 161-253 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) (bacteria) Strain: RIMD 2210633 / Gene: VPA1332 / Plasmid: pACYCDuet1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q87GI4
#2: Protein	VtrC Protein Mass: 16918.775 Da / Num. of mol.: 3 Fragment: VtrC C-terminal periplasmic domain, UNP residues 31-161 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) (bacteria) Strain: RIMD 2210633 / Gene: VPA1333 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q87GI3

#1: Protein

VtrA Protein

Mass: 10982.484 Da / Num. of mol.: 3
Fragment: VtrA C-terminal periplasmic domain, UNP residues 161-253
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) (bacteria)
Strain: RIMD 2210633 / Gene: VPA1332 / Plasmid: pACYCDuet1 / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q87GI4

#2: Protein

VtrC Protein

Mass: 16918.775 Da / Num. of mol.: 3
Fragment: VtrC C-terminal periplasmic domain, UNP residues 31-161
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) (bacteria)
Strain: RIMD 2210633 / Gene: VPA1333 / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q87GI3

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Non-polymers , 5 types, 205 molecules

#3: Chemical	ChemComp-6SB / Taurodeoxycholate / 2-[[(4~{R})-4-[(3~{R},5~{R},8~{R},9~{S},10~{S},12~{S},13~{R},14~{S},17~{R})-10,13-dimethyl-3,12-bis(oxidanyl)-2,3,4,5,6 ,7,8,9,11,12,14,15,16,17-tetradecahydro-1~{H}-cyclopenta[a]phenanthren-17-yl]pentanoyl]amino]ethanesulfonic acid Mass: 499.704 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₂₆H₄₅NO₆S
#4: Chemical	ChemComp-ACT / ACETATE ION Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂H₃O₂
#5: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂H₆O₂
#6: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO₄
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 193 / 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: 2.4 Å³/Da / Density % sol: 48.79 % / Mosaicity: 0.385 °
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 2.0 M ammonium sulfate, 0.1 M sodium acetate, 0.5 mM taurodeoxycholine, 22.5% ethylene glycol

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 19-ID / Wavelength: 0.97926 Å

Detector

Type: DECTRIS PILATUS3 X 1M / Detector: PIXEL / Date: Feb 19, 2016 / Details: monochromator

Radiation

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

Radiation wavelength

Wavelength: 0.97926 Å / Relative weight: 1

Reflection

Resolution: 2.1→35.638 Å / Num. obs: 45762 / % possible obs: 95.6 % / Redundancy: 3.9 % / B_iso Wilson estimate: 24.18 Å² / R_merge(I) obs: 0.079 / R_pim(I) all: 0.043 / R_rim(I) all: 0.09 / Χ²: 0.9 / Net I/av σ(I): 15.889 / Net I/σ(I): 9.4 / Num. measured all: 176526

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Diffraction-ID	% possible all
2.1-2.14	2.8	0.362	1	79.4
2.14-2.18	2.6	0.353	1	82.3
2.18-2.22	2.9	0.312	1	87.2
2.22-2.26	3.1	0.304	1	90.8
2.26-2.31	3.2	0.306	1	93.4
2.31-2.37	3.4	0.313	1	94.6
2.37-2.42	3.5	0.339	1	98.3
2.42-2.49	3.8	0.345	1	99.1
2.49-2.56	3.9	0.312	1	98.8
2.56-2.65	3.8	0.289	1	97.8
2.65-2.74	4.4	0.239	1	99.5
2.74-2.85	4.5	0.186	1	99.9
2.85-2.98	4.4	0.147	1	99.8
2.98-3.14	4.4	0.111	1	99.9
3.14-3.33	4.3	0.083	1	99.2
3.33-3.59	4.2	0.065	1	97.2
3.59-3.95	4.5	0.059	1	99.5
3.95-4.52	4.4	0.052	1	99.7
4.52-5.7	4.1	0.047	1	97.6
5.7-50	4.1	0.037	1	97.7

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Processing

Software

Name	Version	Classification
HKL-3000		data collection
HKL-3000		data scaling
PHENIX	1.10.1_2155	refinement
PDB_EXTRACT	3.2	data extraction
HKL-3000		data reduction
PHENIX	1.10.1_2155	phasing

Refinement

Resolution: 2.103→35.638 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 23.33

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.231	2000	4.84 %	random
R_work	0.1965	-	-	-
obs	0.1982	41304	86.29 %	-

Solvent computation

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

Displacement parameters

B_iso max: 142.85 Å² / B_iso mean: 39.3728 Å² / B_iso min: 5.81 Å²

Refine analyze

Luzzati sigma a obs: 0.23 Å

Refinement step

Cycle: final / Resolution: 2.103→35.638 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	5411	0	361	193	5965
B_iso mean	-	-	44.28	35.32	-
Num. residues	-	-	-	-	651

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.002	5711
X-RAY DIFFRACTION	f_angle_d	0.487	7757
X-RAY DIFFRACTION	f_chiral_restr	0.048	860
X-RAY DIFFRACTION	f_plane_restr	0.002	953
X-RAY DIFFRACTION	f_dihedral_angle_d	11.389	3327

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.103-2.1555	0.2588	91	0.2142	1807	1898	57
2.1555-2.2137	0.2529	103	0.2186	2011	2114	62
2.2137-2.2789	0.2741	112	0.2018	2189	2301	69
2.2789-2.3524	0.2969	121	0.2014	2378	2499	74
2.3524-2.4365	0.2659	129	0.2016	2538	2667	79
2.4365-2.534	0.2205	140	0.2116	2750	2890	85
2.534-2.6493	0.2621	145	0.2165	2858	3003	88
2.6493-2.7889	0.2321	160	0.2142	3133	3293	98
2.7889-2.9636	0.2697	163	0.217	3225	3388	100
2.9636-3.1923	0.2394	166	0.2048	3240	3406	100
3.1923-3.5133	0.213	162	0.197	3194	3356	98
3.5133-4.021	0.2228	167	0.179	3272	3439	100
4.021-5.0638	0.1824	168	0.1552	3296	3464	99
5.0638-35.6431	0.2395	173	0.2178	3413	3586	98

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	0.0416	-0.0179	-0.052	0.0118	0.0348	0.1391	0.0839	-0.0225	-0.0078	0.0008	0.0538	-0.0932	0.0325	0.0967	0.1434	0.066	-0.0043	-0.0217	0.1686	-0.0431	0.1659	-13.415	10.4692	1.7426
2	0.0984	0.0512	-0.0028	0.0348	-0.0206	0.0749	0.0573	-0.0246	0.0152	-0.0018	0.0787	-0.0121	0.0459	-0.0025	0.2363	-0.1219	-0.1109	-0.1324	0.0833	-0.1104	0.1306	-22.0325	13.369	-2.2993
3	0.0066	-0.0007	-0.013	0.0358	-0.0232	0.1206	0.0089	-0.014	-0.0049	-0.0407	0.0113	-0.0096	0.1044	-0.0217	-0.0357	0.0226	-0.0416	-0.0981	0.0014	-0.1411	0.0425	-27.9022	6.647	-15.4563
4	0.0388	0.0193	-0.0082	0.0184	-0.0113	0.0083	0.0267	-0.0282	-0.0177	-0.0283	0.0115	-0.0114	0.0033	-0.0524	0.0218	0.1253	0.0892	-0.0211	0.2447	-0.0613	0.193	-32.6576	11.0596	-19.9325
5	0.0115	0.0191	-0.0111	0.0348	-0.0197	0.016	-0.0787	0.0137	-0.0567	-0.0555	0.0666	-0.0418	0.0488	-0.0149	0.0069	0.1452	0.0697	-0.0156	0.2469	-0.0665	0.1817	-22.3738	4.3238	-23.7142
6	0.0066	0.0097	0.0011	0.0187	-0.0063	0.0213	-0.0041	-0.0031	0.0156	-0.1163	0.0635	0.01	-0.0136	-0.0185	-0.0002	0.2106	0.0723	-0.0491	0.2118	-0.039	0.1795	-30.7083	9.4248	-27.4332
7	0.0021	-0.0077	-0.0088	0.026	0.0308	0.0377	0.0593	0.0989	-0.0008	-0.0554	0.0634	-0.0665	-0.0558	0.0259	0.0086	0.1592	0.0516	-0.0269	0.2367	-0.0444	0.2651	-17.3258	7.8717	-22.5298
8	0.1042	0.0145	-0.0471	0.0076	-0.0073	0.0614	0.0617	0.0545	-0.0516	-0.0122	0.0824	-0.0393	0.012	0.0865	0.0575	0.128	-0.0039	-0.0513	0.1425	-0.0441	0.1905	-19.3376	4.4539	-13.3258
9	0.0051	-0.0069	-0.0064	0.0285	0.0294	0.0301	0.0114	-0.0098	0.0226	0.0026	0.0129	-0.0142	0.0563	-0.028	0.0054	0.1215	-0.0414	-0.0666	0.0671	-0.07	0.1705	-23.1157	0.1818	-11.8174
10	0.0008	-0.0005	-0.0008	0.0007	0.0002	0.0007	0.0019	0.0016	-0.0035	0.0092	-0.0065	-0.0143	-0.0009	0.0102	-0	0.2367	0.1005	-0.0606	0.2592	-0.0582	0.2196	7.4869	-12.0643	-47.8132
11	0.0007	-0.0002	0	0.0001	0.0001	0.0054	0.0725	0.0303	0.0042	0.0165	0.0545	-0.0018	-0.016	-0.0121	-0	0.2562	0.0502	-0.0438	0.1839	-0.0185	0.1822	-4.2963	-4.0735	-49.703
12	0.0016	-0.0008	-0.0009	0.0017	-0.0015	0.0021	0.019	-0.0102	-0.0196	-0.0214	0.0298	0.0288	-0.0003	-0.0553	-0	0.2398	0.0496	-0.0433	0.2124	-0.0659	0.189	-12.1895	-5.2945	-46.6441
13	0.0094	0.0011	-0.0038	0.0004	-0.0007	0.0031	-0.003	0.0038	0.0126	-0.0039	-0.0145	0.0075	-0.0036	0.001	0	0.2635	0.0626	0.0126	0.3165	-0.0474	0.376	-10.5801	8.0892	-41.2237
14	0.0071	-0.0018	-0.0022	0.0013	0.0024	0.0037	-0.0034	-0.0012	-0.0117	-0.0006	-0.0082	-0.0024	0.0217	-0.0214	0	0.161	0.0365	-0.0219	0.1697	-0.0246	0.1381	-0.7067	-5.1911	-40.7698
15	0	0	-0	0.0007	-0.0001	0.0017	0.0002	-0.0012	0.0025	-0.0021	-0.0006	-0.008	-0.0044	-0.0018	-0	0.5947	0.0052	0.0056	0.5362	-0.0758	0.6466	-0.6179	12.0149	-39.6697
16	0.0381	0.0175	-0.0107	0.017	-0.0075	0.0061	0.0094	-0.0157	0.0306	-0.0036	0.0067	0.0051	-0.0263	0.0237	0.0014	0.1798	-0.0347	-0.0119	0.214	-0.0402	0.1284	-0.2795	-2.902	-33.4784
17	0.0003	-0.0003	0.0009	0.0002	-0.0005	0.001	0.0003	-0.0105	-0.013	0.004	0.001	-0.0035	-0.0025	0.0089	0	0.4503	-0.0834	-0.072	0.403	0.0632	0.4839	-7.9105	-17.1441	-35.5006
18	0.0027	0.0003	-0.0034	0.0024	-0.0028	0.0054	0.0744	-0.0313	0.0215	0.0041	0.0366	0.0468	0.0042	-0.0196	0.0001	0.1618	-0.0205	0.0535	0.2623	-0.0564	0.2417	-10.7688	-3.8786	-35.1889
19	0.0065	-0.004	-0.0001	0.0144	0.0178	0.0201	-0.0159	-0.0219	-0	0.0435	0.0416	-0.0264	0.0539	-0.0237	0	0.2265	-0.0625	0.0017	0.1928	-0.0153	0.1411	7.1307	-1.8724	-31.4826
20	0.0222	0.0048	0.0021	0.0127	-0.0138	0.0216	0.0256	0.0059	0.027	0.0944	0.0492	0.0324	0.0132	0.0488	0.001	0.2038	-0.0292	0.0134	0.2649	-0.0401	0.1212	12.4802	-1.569	-28.5368
21	0.0277	0.0015	0.0056	0.0417	0.0008	0.0024	0.06	0.0112	-0.0577	0.1128	0.0205	-0.1415	-0.0321	-0.0076	-0.0037	0.2265	0.0014	-0.0313	0.3222	-0.0594	0.1514	18.8484	-5.4555	-33.9683
22	0.006	-0.0065	0.0047	0.0046	-0.0037	0.0029	0.0189	-0.0183	-0.0209	-0.0048	0.0043	0.0242	-0.0115	-0.0047	-0	0.4121	0.011	-0.1012	0.298	-0.0002	0.2353	18.5215	-8.4288	-23.2681
23	0.0332	0.0245	-0.011	0.0243	-0.013	0.0082	0.021	0.0259	0.012	-0.008	0.0188	0.012	-0.0066	-0.0099	0.0049	0.2348	0.0138	-0.0074	0.2021	-0.0703	0.1324	11.2772	-3.0825	-46.5913
24	0.0106	-0.0042	0.0029	0.0063	0.0072	0.0118	0.0266	0.0338	0.0052	-0.018	0.0113	-0.0283	0.0009	0.0377	-0	0.2094	-0.0285	-0.0278	0.1592	-0.007	0.1207	8.9915	0.4628	-40.2923
25	0.0069	0.0057	0.0023	0.0043	0.0019	0.0015	0.0058	0.0137	0.0206	0.0622	0.0253	0.0146	-0.0398	-0.0218	0	0.3309	0.0303	0.057	0.1704	0.0135	0.249	8.663	36.7595	-15.9563
26	0.0042	0.0032	0	0.0041	0.0065	0.018	0.0433	-0.0138	-0.0064	0.051	-0.0042	-0.0042	-0.0108	-0.0198	0.0001	0.515	0.0312	-0.0038	0.1406	0.0198	0.2448	9.8297	45.7833	-11.5096
27	0.0146	0.0077	-0.0287	0.0242	-0.0016	0.0808	-0.0157	0.0501	0.0829	-0.006	0.0246	0.0791	-0.0664	-0.0674	-0.0049	0.2341	0.0129	0.0066	0.1046	0.0238	0.2077	8.0756	43.7309	-24.7552
28	0.0248	0.0031	-0.0237	0.0409	-0.0102	0.0236	0.0163	0.011	0.0175	-0.0053	0.0144	0.0104	-0.0453	0.011	0.0129	0.4358	-0.0684	-0.0994	0.1765	-0.0255	0.2805	16.4716	50.1194	-19.8262
29	0.0052	-0.0022	-0.0032	0.0049	-0.0033	0.0061	-0.0187	0.0014	0.0184	0.0252	-0.005	-0.0058	-0.0545	-0.0282	0	0.1811	-0.0539	-0.0142	0.2011	0.0474	0.2652	9.0828	36.7487	-37.4345
30	0.0178	-0.0149	-0.0045	0.0112	0.0003	0.0123	0.127	-0.0724	0.0471	-0.0253	0.0878	-0.0682	-0.0155	-0.0045	0.0004	0.2958	-0.0899	0.0124	0.2417	0.0128	0.2363	16.2681	37.7615	-39.0277
31	0.0881	-0.0522	0.0512	0.0371	-0.0238	0.0302	0.0682	0.0271	-0.0859	-0.0677	0.0902	0.0465	-0.0151	0.085	0.0131	0.2592	-0.0049	0.03	0.2026	-0.0145	0.2123	16.6825	28.8697	-39.3962
32	0.0045	-0.0005	-0.0056	0.0036	0.0007	0.006	-0.0366	-0.0032	-0.0407	-0.0072	-0.0259	-0.0058	-0.003	0.0369	0	0.3262	-0.0122	0.0785	0.324	0.0067	0.3415	25.6217	34.7787	-45.7027
33	0.0021	0.0004	-0.0018	0.0037	-0.0033	0.0031	0.029	-0.014	0.0008	0.0155	0.0409	0.0016	0.0186	-0.0338	0	0.2338	0.0337	0.018	0.1353	0.0297	0.2463	10.8526	27.0516	-28.3198
34	0.0047	0.0055	-0.0099	0.0106	-0.0126	0.0165	0.0384	-0.0055	-0.0115	0.0272	0.0368	0.0392	-0.0018	0.0335	-0	0.1673	0.0203	-0.0056	0.2277	0.0145	0.1371	7.9581	34.2292	-31.5782

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 165 through 205 )	A	165 - 205
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 206 through 253 )	A	206 - 253
3	X-RAY DIFFRACTION	3	chain 'B' and (resid 0 through 59 )	B	0 - 59
4	X-RAY DIFFRACTION	4	chain 'B' and (resid 60 through 78 )	B	60 - 78
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 79 through 95 )	B	79 - 95
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 96 through 121 )	B	96 - 121
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 122 through 139 )	B	122 - 139
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 140 through 153 )	B	140 - 153
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 154 through 161 )	B	154 - 161
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 164 through 168 )	C	164 - 168
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 169 through 182 )	C	169 - 182
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 183 through 199 )	C	183 - 199
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 200 through 205 )	C	200 - 205
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 206 through 221 )	C	206 - 221
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 222 through 226 )	C	222 - 226
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 227 through 233 )	C	227 - 233
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 234 through 239 )	C	234 - 239
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 240 through 253 )	C	240 - 253
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 31 through 48 )	D	31 - 48
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 49 through 76 )	D	49 - 76
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 77 through 109 )	D	77 - 109
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 110 through 131 )	D	110 - 131
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 132 through 139 )	D	132 - 139
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 140 through 161 )	D	140 - 161
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 166 through 182 )	E	166 - 182
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 183 through 199 )	E	183 - 199
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 200 through 233 )	E	200 - 233
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 234 through 253 )	E	234 - 253
29	X-RAY DIFFRACTION	29	chain 'F' and (resid 31 through 42 )	F	31 - 42
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 43 through 72 )	F	43 - 72
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 73 through 109 )	F	73 - 109
32	X-RAY DIFFRACTION	32	chain 'F' and (resid 110 through 129 )	F	110 - 129
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 130 through 139 )	F	130 - 139
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 140 through 161 )	F	140 - 161

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