PDB-5f78: Crystal structure of Mutant N87T of adenosine/Methylthioadenosine...

ID or keywords:

Entry

Database: PDB / ID: 5f78

Title

Crystal structure of Mutant N87T of adenosine/Methylthioadenosine phosphorylase from Schistosoma mansoni in APO form

Components

Methylthioadenosine phosphorylase

Keywords

TRANSFERASE

Function / homology

Function and homology information

S-methyl-5'-thioadenosine phosphorylase / S-methyl-5-thioadenosine phosphorylase activity / L-methionine salvage from methylthioadenosine / purine ribonucleoside salvage / nucleus / cytosol
Similarity search - Function

Biological species

Schistosoma mansoni (invertebrata)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.8518 Å

Authors

Torini, J.R.S. / Brandao-Neto, J. / DeMarco, R. / Pereira, H.M.

Funding support

Brazil, 2items

Citation

Journal: PLoS Negl Trop Dis / Year: 2016
Title: Crystal Structure of Schistosoma mansoni Adenosine Phosphorylase/5'-Methylthioadenosine Phosphorylase and Its Importance on Adenosine Salvage Pathway.
Authors: Torini, J.R. / Brandao-Neto, J. / DeMarco, R. / Pereira, H.D.

History

Deposition	Dec 7, 2015	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Dec 21, 2016	Provider: repository / Type: Initial release
Revision 1.1	Sep 27, 2017	Group: Author supporting evidence / Data collection / Category: diffrn_source / pdbx_audit_support Item: _diffrn_source.pdbx_synchrotron_site / _pdbx_audit_support.funding_organization
Revision 1.2	Nov 1, 2017	Group: Author supporting evidence / Category: pdbx_struct_assembly_auth_evidence
Revision 1.3	Apr 17, 2019	Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4	Jan 1, 2020	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5	Sep 27, 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 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.6	Oct 23, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5f78.cif.gz	698 KB	Display	PDBx/mmCIF format
PDB format	pdb5f78.ent.gz	574.2 KB	Display	PDB format
PDBx/mmJSON format	5f78.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	5f78_validation.pdf.gz	498.1 KB	Display	wwPDB validaton report
Full document	5f78_full_validation.pdf.gz	512.1 KB	Display
Data in XML	5f78_validation.xml.gz	79.5 KB	Display
Data in CIF	5f78_validation.cif.gz	116.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/f7/5f78 ftp://data.pdbj.org/pub/pdb/validation_reports/f7/5f78	HTTPS FTP

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Related structure data

Related structure data	4l5aC 4l5cC 4l5ySC 4l6iC 5f73C 5f76C 5f77C 5f7jC 5f7oC 5f7xC 5f7zC 5fakC C: citing same article (ref.) S: Starting model for refinement
Similar structure data	5f7z-1 5f7z-2 5f7o-d 5f73-1 4l5y-2 5f77-d 5f73-2 3sm4-d 5fak-2 5f76-d 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

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Methylthioadenosine phosphorylase

B: Methylthioadenosine phosphorylase

C: Methylthioadenosine phosphorylase

D: Methylthioadenosine phosphorylase

E: Methylthioadenosine phosphorylase

F: Methylthioadenosine phosphorylase

hetero molecules

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

1

A: Methylthioadenosine phosphorylase

B: Methylthioadenosine phosphorylase

C: Methylthioadenosine phosphorylase

hetero molecules

defined by author&software
Evidence: gel filtration
106 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: Methylthioadenosine phosphorylase

E: Methylthioadenosine phosphorylase

F: Methylthioadenosine phosphorylase

hetero molecules

defined by author&software
Evidence: gel filtration
106 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	81.193, 82.232, 150.746
Angle α, β, γ (deg.)	90.000, 101.550, 90.000
Int Tables number	4
Space group name H-M	P12₁1

Details

Trimer confirmed by gel filtration

#1: Protein	Methylthioadenosine phosphorylase Mass: 35246.484 Da / Num. of mol.: 6 / Fragment: Enzyme / Mutation: N87T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schistosoma mansoni (invertebrata) / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: I0B503, S-methyl-5'-thioadenosine phosphorylase
#2: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO₄
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1853 / Source method: isolated from a natural source / Formula: H₂O
Has protein modification	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.33 Å³/Da / Density % sol: 47.22 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: 100mM Bris-tris or Mes, 14-18% PEG3350, pH 6.5 / PH range: 6.1-6.7

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92 Å
Detector	Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: May 11, 2013
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.92 Å / Relative weight: 1
Reflection	Resolution: 1.85→28.05 Å / Num. all: 161035 / Num. obs: 161035 / % possible obs: 97.5 % / Redundancy: 5.4 % / R_merge(I) obs: 0.089 / Net I/σ(I): 11
Reflection shell	Resolution: 1.85→1.95 Å / Redundancy: 5.3 % / R_merge(I) obs: 0.566 / Mean I/σ(I) obs: 2.8 / % possible all: 97.7

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
PHASER		phasing
PHENIX		refinement
PDB_EXTRACT	3.15	data extraction
xia2		data reduction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 4L5Y

4l5y

Resolution: 1.8518→28.05 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 19.99 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.1995	8062	5.02 %	Random selection
R_work	0.1712	152613	-	-
obs	0.1726	160675	97.19 %	-

Solvent computation

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

Displacement parameters

B_iso max: 82.1 Å² / B_iso mean: 26.6607 Å² / B_iso min: 6.5 Å²

Refinement step

Cycle: final / Resolution: 1.8518→28.05 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13039	0	30	1853	14922
B_iso mean	-	-	15.15	36.18	-
Num. residues	-	-	-	-	1721

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.003	13328
X-RAY DIFFRACTION	f_angle_d	0.561	18098
X-RAY DIFFRACTION	f_chiral_restr	0.045	2103
X-RAY DIFFRACTION	f_plane_restr	0.004	2318
X-RAY DIFFRACTION	f_dihedral_angle_d	12.022	7990

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / 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 (%)
1.8518-1.8728	0.2885	249	0.2427	5088	5337	97
1.8728-1.8949	0.2482	241	0.2435	5125	5366	97
1.8949-1.918	0.2833	275	0.2482	5015	5290	97
1.918-1.9422	0.2763	275	0.2464	4981	5256	96
1.9422-1.9678	0.2368	272	0.2156	5035	5307	96
1.9678-1.9947	0.2503	255	0.2095	4841	5096	93
1.9947-2.0232	0.2055	251	0.1958	4816	5067	92
2.0232-2.0534	0.2211	283	0.1861	4946	5229	96
2.0534-2.0855	0.2236	284	0.2029	5206	5490	99
2.0855-2.1197	0.2081	264	0.178	5118	5382	99
2.1197-2.1562	0.2071	264	0.1764	5170	5434	99
2.1562-2.1954	0.2358	288	0.1776	5146	5434	99
2.1954-2.2376	0.2035	296	0.169	5123	5419	99
2.2376-2.2833	0.2134	283	0.191	5094	5377	98
2.2833-2.3329	0.2079	325	0.1748	5103	5428	99
2.3329-2.3871	0.2137	284	0.1684	5131	5415	98
2.3871-2.4468	0.195	279	0.1674	5092	5371	98
2.4468-2.5129	0.2039	275	0.1632	5150	5425	98
2.5129-2.5868	0.202	261	0.1662	5065	5326	97
2.5868-2.6702	0.1895	253	0.1642	5074	5327	96
2.6702-2.7656	0.1738	251	0.1609	5024	5275	96
2.7656-2.8762	0.2055	256	0.1636	4768	5024	92
2.8762-3.007	0.213	285	0.1745	5039	5324	96
3.007-3.1653	0.2002	260	0.1746	5227	5487	99
3.1653-3.3633	0.1988	271	0.1625	5219	5490	100
3.3633-3.6225	0.1777	270	0.1612	5247	5517	100
3.6225-3.9861	0.175	263	0.1468	5262	5525	99
3.9861-4.5608	0.1552	281	0.1343	5191	5472	99
4.5608-5.7381	0.1593	216	0.1487	4943	5159	92
5.7381-28.0561	0.1919	252	0.1724	5374	5626	99

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	3.6035	-1.3655	1.2724	3.0192	-0.0514	1.8248	0.1892	0.9206	-0.3289	-0.8815	-0.1751	-0.5318	0.3822	0.8221	-0.0384	0.31	0.0504	0.1665	0.36	-0.0191	0.4741	42.0697	-17.317	0.7083
2	1.9201	-1.2957	-0.2602	3.2282	-0.0239	3.769	-0.003	-0.0342	-0.2099	-0.1391	-0.2397	0.1056	0.5232	0.2121	0.1346	0.3355	0.0667	0.1548	0.1309	-0.0584	0.417	34.172	-29.215	2.0838
3	1.0104	-0.6497	0.107	1.051	0.4234	1.0706	-0.1285	0.0917	-0.1951	-0.2359	0.0429	-0.3753	0.1756	0.264	0.0486	0.1948	0.0329	0.1177	0.1711	-0.028	0.3841	36.3033	-20.2039	5.2106
4	1.6506	0.2037	-0.4205	1.5657	-0.1763	1.8199	-0.0453	-0.1926	-0.1184	-0.021	-0.0166	-0.2589	-0.014	0.2767	0.0587	0.1032	-0.0109	0.0254	0.1375	-0.0105	0.189	34.784	-9.211	15.8719
5	2.947	0.6022	-0.4541	1.594	-0.9846	1.2337	0.2439	-0.2788	0.1636	0.1374	-0.2346	-0.1831	-0.4224	0.3945	0.0347	0.2345	-0.0856	0.0523	0.1609	-0.0482	0.1989	35.8415	3.0908	11.9655
6	4.4035	1.1617	0.7935	1.9268	0.2229	3.9424	-0.0052	-0.0848	0.1022	-0.0774	0.0893	-0.2181	-0.2722	-0.0899	-0.0601	0.1104	-0.0099	0.0389	0.0732	-0.0025	0.1166	17.3404	-1.4993	11.0754
7	1.3434	0.6785	0.2908	1.8386	-0.2821	2.2018	0.0342	-0.0728	-0.1298	-0.0546	-0.0885	-0.1846	0.1043	0.1167	0.0495	0.1037	-0.0124	0.0367	0.1197	0.0001	0.2077	30.3008	-12.6956	14.9432
8	3.8982	-1.4562	1.9241	3.3179	-2.6967	5.0541	-0.1173	0.1021	-0.0447	-0.0255	0.4564	0.4585	-0.4918	-0.3908	-0.3694	0.2223	-0.0223	0.0623	0.1636	0.0405	0.2898	28.1887	-1.5074	2.8797
9	7.6729	-3.7914	3.7051	3.9221	-2.6495	5.2665	-0.0735	0.8216	0.0751	-0.3159	-0.0711	-0.3958	-0.2759	0.4879	0.0821	0.2579	-0.0679	0.1236	0.2576	-0.018	0.3349	39.6488	-4.281	-0.8298
10	4.453	0.0276	-0.3768	0.4356	0.7296	1.3021	-0.2018	-0.8714	-1.014	0.1423	-0.1006	-0.6605	0.5183	0.6594	0.192	0.3207	0.1389	-0.0765	0.4298	0.1025	0.5512	42.3058	-23.8503	24.9567
11	0.6417	1.5135	-0.1933	4.2273	-1.6244	2.5353	-0.2215	-0.4676	-0.5899	0.0946	-0.026	-0.4911	0.2861	0.27	0.2501	0.1454	0.0294	-0.0116	0.2515	0.0861	0.2231	11.4623	-32.2338	43.4042
12	2.7476	-1.2187	3.3813	5.9417	-5.4188	8.1223	0.1133	-0.0641	-0.5448	-0.2099	0.0705	0.1148	1.0471	-0.2067	-0.1672	0.315	-0.0091	0.0366	0.1469	0.0143	0.2873	8.107	-38.5565	30.64
13	1.2959	0.49	-0.8694	1.1328	-0.5785	2.7617	-0.0865	-0.1423	-0.287	-0.0392	-0.0808	-0.1182	0.2939	0.1249	0.1712	0.147	-0.0004	0.0115	0.1146	0.0562	0.1648	10.0747	-30.3871	36.1401
14	2.1585	0.1878	0.9245	0.9666	-0.2861	2.5401	0.0093	-0.0535	-0.0154	-0.0061	-0.0701	-0.0657	-0.0064	0.1102	0.0465	0.1592	0.0033	0.0192	0.0856	0.0289	0.0928	8.9308	-16.7215	29.6549
15	1.5334	-0.3947	-0.1757	0.4371	0.0328	1.8317	0.15	-0.4494	0.2883	0.3132	-0.0507	-0.1649	-0.6247	0.2997	-0.0374	0.341	-0.1173	-0.0184	0.2775	-0.0206	0.1658	13.4229	-10.8236	48.0543
16	4.7643	-1.8996	-1.4402	6.7912	1.5875	4.3093	0.0968	-0.1165	0.1434	0.2883	-0.1497	-0.1369	-0.15	0.3462	0.0578	0.1233	-0.0384	-0.0014	0.1447	0.0329	0.1006	25.3498	-9.6699	26.3877
17	0.5202	-0.2259	0.2104	0.6513	-0.0892	0.8044	0.078	-0.1126	-0.0236	-0.0132	-0.1837	-0.2997	-0.1212	0.3314	0.0069	0.1402	-0.0402	-0.0023	0.2152	0.0687	0.1741	17.5496	-17.1059	34.5525
18	6.1518	-0.1189	-1.5015	1.2049	0.0177	1.2508	-0.1176	-0.6814	-0.0648	0.205	-0.1306	-0.3865	0.0049	0.6946	0.2347	0.232	-0.0553	-0.0558	0.4885	0.1664	0.2599	22.5151	-23.5102	47.6651
19	1.7133	-0.4082	1.0686	1.0773	-0.7913	4.5373	0.0572	-0.1427	-0.0273	0.0366	0.1358	0.1823	0.0144	-1.0678	-0.1516	0.1214	-0.0165	0.0332	0.2444	0.0145	0.1744	-8.0212	-20.5051	35.6116
20	1.8868	-1.1624	1.9361	1.6867	0.1608	7.0264	0.1803	0.0862	-0.2276	-0.2196	-0.0065	0.4393	0.3238	-0.7218	-0.1367	0.2155	0.0023	-0.0338	0.1642	-0.0076	0.1826	-11.7836	-9.1698	0.2839
21	0.9733	-0.0957	-0.1226	1.689	0.2833	0.799	0.0434	0.0634	0.0325	-0.1052	-0.0241	-0.0073	-0.0729	-0.0761	-0.0161	0.1254	0.0097	0.0036	0.0828	0.0046	0.0689	-0.0717	-5.6052	5.5386
22	0.6724	0.0799	-0.2308	0.7222	-0.1585	3.1111	-0.0045	-0.0627	-0.0118	0.0332	-0.0157	-0.0931	-0.0452	0.0574	0.0343	0.1123	0.0032	-0.0049	0.0601	0.0064	0.1086	6.0897	-6.2743	16.3361
23	2.2683	0.0813	-0.6205	1.7413	-0.004	1.538	-0.0677	-0.072	-0.0341	-0.1396	-0.0054	0.0797	-0.0075	0.0022	0.0572	0.1849	0.0384	-0.001	0.0642	-0.0096	0.1116	-4.3497	-2.5917	6.9742
24	2.2137	0.5824	-0.0319	1.8083	-0.4447	1.4576	0.0126	-0.1869	-0.1863	0.1337	-0.0609	0.3129	0.1375	-0.1921	0.0599	0.1047	-0.0255	0.0207	0.1225	0.005	0.1851	30.0196	17.6811	70.2784
25	1.1929	-0.1524	-0.224	0.8444	0.1193	1.2201	0.0141	0.1109	0.0007	-0.0993	-0.0501	0.1286	-0.0808	-0.1742	0.0194	0.0871	0.0269	-0.0226	0.1043	0.0005	0.1121	33.2006	31.7008	58.8483
26	2.5807	-0.5945	-0.4814	1.7474	0.3345	1.8022	-0.0047	-0.1709	-0.0383	0.0852	0.0081	0.1712	-0.0027	-0.1809	0.0134	0.0857	0.0208	-0.0219	0.1248	0.0099	0.173	27.8871	28.687	65.3049
27	1.308	-2.0095	-1.3866	3.2462	1.679	2.8858	-0.0811	0.5662	-0.5724	-0.1945	-0.0371	0.3176	0.1434	-0.3915	0.3634	0.1994	0.0147	0.0198	0.3278	-0.1504	0.228	53.5553	7.7888	29.4515
28	0.9594	-0.0694	-0.6778	1.1594	0.6349	2.6702	-0.0382	0.1396	-0.2975	0.02	-0.0419	-0.0895	0.2347	0.0684	0.0702	0.163	0.036	0.0175	0.1533	-0.07	0.2108	55.9358	8.0604	37.7196
29	1.6842	-0.1711	0.2499	0.8773	0.5071	2.2152	0.1056	0.2912	0.0235	-0.25	-0.0889	-0.0671	-0.1729	-0.0687	-0.0102	0.2172	0.0285	0.0432	0.1476	-0.0129	0.1132	55.195	25.17	35.8902
30	1.1812	-0.0425	-0.6616	0.5555	0.3469	0.9753	0.1387	0.2714	0.042	-0.2466	-0.0824	-0.0285	-0.1815	-0.137	-0.0393	0.1847	0.0439	0.0043	0.1627	-0.0162	0.0994	47.1538	27.3508	39.2498
31	3.6862	0.6434	-1.3253	0.4798	-0.0621	0.5681	-0.1469	-0.197	0.1539	-0.0548	-0.0556	0.2769	-0.1483	-0.4697	0.0071	0.2209	0.094	-0.0201	0.525	-0.1585	0.2434	37.9537	22.2177	35.6071
32	0.8959	-0.3486	-0.7209	0.7375	0.3663	1.2333	-0.0084	0.6987	-0.2077	-0.6745	-0.3058	0.2703	0.0561	-0.7789	-0.1205	0.2929	0.1095	-0.1298	0.6199	-0.3538	0.0577	43.7676	16.015	24.9119
33	1.0481	0.1185	1.1064	1.2467	0.1021	5.2374	0.0291	0.2195	0.041	-0.1401	0.0298	-0.4569	-0.0634	1.1733	0.0073	0.1912	0.0092	0.0985	0.4106	-0.0343	0.358	73.1416	20.7508	36.9311
34	1.4201	-0.3624	-0.3998	2.1334	0.6598	2.6925	0.0992	-0.5001	-0.1819	0.3258	-0.047	-0.8184	0.5849	0.9912	-0.2429	0.1892	-0.0214	-0.1029	0.3724	0.0749	0.2911	76.8749	31.3875	71.2298
35	4.2784	2.499	-1.5602	1.8022	-0.924	0.5641	0.2927	-0.8449	-0.5413	0.4615	-0.361	-0.5891	-0.0067	0.6421	-0.0042	0.2292	0.0207	-0.0623	0.3048	0.1182	0.3464	70.5482	19.0904	74.2765
36	1.8492	0.3642	1.1	1.6065	0.4225	1.7189	0.0731	-0.2744	-0.2436	0.1842	-0.1941	-0.3887	0.2586	0.4915	-0.3106	0.1301	-0.0247	-0.0756	0.26	0.0736	0.2168	73.4388	27.3488	69.1721
37	1.507	0.3007	0.9503	2.4127	0.7719	3.3116	0.1018	-0.2458	-0.1454	0.352	-0.1073	-0.0448	0.0304	0.0594	0.0059	0.0979	-0.0208	-0.016	0.1422	0.0336	0.1248	66.4628	29.7371	72.7693
38	1.5853	0.4979	-0.4341	1.0523	-0.4902	1.0341	0.087	-0.0321	0.0751	-0.0121	-0.0478	-0.0579	-0.1126	0.0946	-0.053	0.1078	-0.0157	-0.0197	0.082	-0.0072	0.1087	62.1688	41.0991	63.5814
39	0.6607	0.172	-0.3415	1.0471	-0.0831	4.2784	-0.0147	0.0335	-0.0229	-0.0989	-0.0162	-0.0763	-0.044	-0.0324	0.0435	0.0807	-0.0112	-0.0107	0.0671	0.0017	0.1046	58.9838	34.1815	56.1873
40	1.9766	0.0342	0.5501	1.5665	-0.212	0.187	-0.0182	0.5967	-0.0389	-0.3365	0.0486	-0.1155	0.2139	-0.1667	0.053	0.2222	-0.0636	0.0397	0.2212	-0.0219	0.1453	69.994	37.1267	54.3108
41	3.6553	-0.3375	-3.1905	2.8064	2.388	8.0633	-0.0374	0.0764	0.0389	-0.12	-0.0661	-0.3756	-0.0225	0.2835	0.0139	0.111	-0.0373	-0.0148	0.129	0.0606	0.1976	79.2839	40.2874	61.112
42	6.5579	4.289	2.0864	4.8908	2.1402	1.84	0.4312	-0.7323	0.2331	0.5588	-0.4634	0.1841	-0.0549	-0.1353	0.0616	0.2555	-0.0571	0.0172	0.2179	-0.025	0.1039	55.9196	37.1057	82.3839

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 3 through 23 )	A
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 24 through 38 )	A
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 39 through 90 )	A
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 91 through 164 )	A
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 165 through 182 )	A
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 183 through 198 )	A
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 199 through 220 )	A
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 221 through 238 )	A
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 239 through 270 )	A
10	X-RAY DIFFRACTION	10	chain 'A' and (resid 271 through 291 )	A
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 3 through 23 )	B
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 24 through 38 )	B
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 39 through 90 )	B
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 91 through 139 )	B
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 140 through 182 )	B
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 183 through 198 )	B
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 199 through 238 )	B
18	X-RAY DIFFRACTION	18	chain 'B' and (resid 239 through 269 )	B
19	X-RAY DIFFRACTION	19	chain 'B' and (resid 270 through 291 )	B
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 3 through 23 )	C
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 24 through 182 )	C
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 183 through 220 )	C
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 221 through 291 )	C
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 3 through 90 )	D
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 91 through 220 )	D
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 221 through 291 )	D
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 3 through 23 )	E
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 24 through 90 )	E
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 91 through 164 )	E
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 165 through 220 )	E
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 221 through 240 )	E
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 241 through 270 )	E
33	X-RAY DIFFRACTION	33	chain 'E' and (resid 271 through 291 )	E
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 3 through 23 )	F
35	X-RAY DIFFRACTION	35	chain 'F' and (resid 24 through 38 )	F
36	X-RAY DIFFRACTION	36	chain 'F' and (resid 39 through 67 )	F
37	X-RAY DIFFRACTION	37	chain 'F' and (resid 68 through 89 )	F
38	X-RAY DIFFRACTION	38	chain 'F' and (resid 90 through 182 )	F
39	X-RAY DIFFRACTION	39	chain 'F' and (resid 183 through 220 )	F
40	X-RAY DIFFRACTION	40	chain 'F' and (resid 221 through 241 )	F
41	X-RAY DIFFRACTION	41	chain 'F' and (resid 242 through 269 )	F
42	X-RAY DIFFRACTION	42	chain 'F' and (resid 270 through 291 )	F

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