PDB-5zg4: Crystal Structure of Triosephosphate isomerase SAD deletion mutan...

ID or keywords:

Entry

Database: PDB / ID: 5zg4

Title

Crystal Structure of Triosephosphate isomerase SAD deletion mutant from Opisthorchis viverrini

Components

Triosephosphate isomerase

Keywords

ISOMERASE / Tim-barrel / Triosephosphate isomerase

Function / homology

Function and homology information

triose-phosphate isomerase / triose-phosphate isomerase activity / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / glycolytic process / gluconeogenesis / metal ion binding / cytosol
Similarity search - Function

Biological species

Opisthorchis viverrini (Southeast Asian liver fluke)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.746 Å

Authors

Son, J. / Kim, S. / Kim, S.E. / Lee, H. / Lee, M.R. / Hwang, K.Y.

Citation

Journal: Sci Rep / Year: 2018
Title: Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini.
Authors: Son, J. / Kim, S. / Kim, S.E. / Lee, H. / Lee, M.R. / Hwang, K.Y.

History

Deposition	Mar 7, 2018	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Oct 24, 2018	Provider: repository / Type: Initial release
Revision 1.1	Nov 22, 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 / 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	5zg4.cif.gz	393.4 KB	Display	PDBx/mmCIF format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/zg/5zg4 ftp://data.pdbj.org/pub/pdb/validation_reports/zg/5zg4	HTTPS FTP

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Related structure data

Related structure data	5zfxSC 5zg5C 5zgaC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	5zga-1 2vom-2 5zga-2 1wyi-d 1su5-d 2vfh-d 3ypi-d 6nxw-2 1mo0-d 3bit-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) 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
Related items in Molecule of the Month	#50 - Feb 2004 Glycolytic Enzymes similarity (8)

Deposited unit

A: Triosephosphate isomerase

B: Triosephosphate isomerase

C: Triosephosphate isomerase

D: Triosephosphate isomerase

119 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Triosephosphate isomerase

B: Triosephosphate isomerase

defined by author&software
Evidence: gel filtration
59.5 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Triosephosphate isomerase

D: Triosephosphate isomerase

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

Unit cell

Length a, b, c (Å)	73.742, 91.924, 75.775
Angle α, β, γ (deg.)	90.000, 109.130, 90.000
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	(chain A and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))
2	1	(chain B and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))
3	1	(chain C and (resid 5 through 152 or resid 160 through 249))
4	1	(chain D and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))

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	ARG	ARG	ARG	ARG	(chain A and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))	A	A	5 - 152	25 - 172
1	2	HIS	HIS	ALA	ALA	(chain A and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))	A	A	160 - 170	180 - 190
1	3	LYS	LYS	ALA	ALA	(chain A and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))	A	A	175 - 249	195 - 269
2	1	ARG	ARG	ARG	ARG	(chain B and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))	B	B	5 - 152	25 - 172
2	2	HIS	HIS	ALA	ALA	(chain B and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))	B	B	160 - 170	180 - 190
2	3	LYS	LYS	ALA	ALA	(chain B and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))	B	B	175 - 249	195 - 269
3	1	ARG	ARG	ARG	ARG	(chain C and (resid 5 through 152 or resid 160 through 249))	C	C	5 - 152	25 - 172
3	2	HIS	HIS	ALA	ALA	(chain C and (resid 5 through 152 or resid 160 through 249))	C	C	160 - 249	180 - 269
4	1	ARG	ARG	ARG	ARG	(chain D and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))	D	D	5 - 152	25 - 172
4	2	HIS	HIS	ALA	ALA	(chain D and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))	D	D	160 - 170	180 - 190
4	3	LYS	LYS	ALA	ALA	(chain D and (resid 5 through 152 or resid 160 through 170 or resid 175 through 249))	D	D	175 - 249	195 - 269

#1: Protein	Triosephosphate isomerase Mass: 29735.094 Da / Num. of mol.: 4 / Mutation: SAD deletion Source method: isolated from a genetically manipulated source Source: (gene. exp.) Opisthorchis viverrini (Southeast Asian liver fluke) Gene: T265_10017 / Plasmid: pET17b / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: A0A074Z863, triose-phosphate isomerase
#2: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1190 / Source method: isolated from a natural source / Formula: H₂O
Sequence details	The sequence conflicts may be resulted from the difference of subspecies of the source organism.

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.04 Å³/Da / Density % sol: 39.71 %
Crystal grow	Temperature: 293 K / Method: evaporation / pH: 8.5 / Details: PEG 3350

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Data collection

Diffraction

Mean temperature: 293 K

Diffraction source

Source:

SYNCHROTRON / Site:

SPring-8

/ Beamline: BL44XU / Wavelength: 0.9 Å

Detector

Type: RAYONIX MX300HE / Detector: CCD / Date: Oct 26, 2016

Radiation

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

Radiation wavelength

Wavelength: 0.9 Å / Relative weight: 1

Reflection

Resolution: 1.75→45.96 Å / Num. obs: 96733 / % possible obs: 99.8 % / Redundancy: 4.2 % / B_iso Wilson estimate: 14.51 Å² / CC_1/2: 0.998 / R_merge(I) obs: 0.075 / R_pim(I) all: 0.041 / R_rim(I) all: 0.085 / Net I/σ(I): 14.1 / Num. measured all: 410025 / Scaling rejects: 1

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. measured all	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Net I/σ(I) obs	% possible all
1.75-1.78	4.1	0.495	19219	4711	0.84	0.276	0.568	2.8	97.8
9.56-45.96	3.9	0.023	2429	615	0.999	0.013	0.027	36.8	98.4

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Processing

Software

Name	Version	Classification
PHENIX	1.12_2829	refinement
autoXDS		data processing
Aimless		data scaling
PDB_EXTRACT	3.24	data extraction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 5ZFX

5zfx

Resolution: 1.746→36.36 Å / SU ML: 0.16 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 18.3 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1926	4776	4.94 %
R_work	0.1601	91905	-
obs	0.1616	96681	99.8 %

Solvent computation

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

Displacement parameters

B_iso max: 69.18 Å² / B_iso mean: 19.0053 Å² / B_iso min: 5.44 Å²

Refinement step

Cycle: final / Resolution: 1.746→36.36 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7530	0	0	1190	8720
B_iso mean	-	-	-	28.69	-
Num. residues	-	-	-	-	971

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	7675
X-RAY DIFFRACTION	f_angle_d	1.112	10375
X-RAY DIFFRACTION	f_chiral_restr	0.064	1163
X-RAY DIFFRACTION	f_plane_restr	0.007	1338
X-RAY DIFFRACTION	f_dihedral_angle_d	6.001	4655

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	4477	X-RAY DIFFRACTION	9.207	TORSIONAL
1	2	B	4477	X-RAY DIFFRACTION	9.207	TORSIONAL
1	3	C	4477	X-RAY DIFFRACTION	9.207	TORSIONAL
1	4	D	4477	X-RAY DIFFRACTION	9.207	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / 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 (%)
1.7459-1.7658	0.2716	167	0.2191	2984	3151	97
1.7658-1.7865	0.2835	156	0.2095	3037	3193	100
1.7865-1.8083	0.2277	169	0.2003	3070	3239	100
1.8083-1.8312	0.2565	133	0.188	3090	3223	100
1.8312-1.8553	0.2027	183	0.1851	3018	3201	100
1.8553-1.8807	0.2331	158	0.1815	3030	3188	100
1.8807-1.9076	0.2372	185	0.1754	3045	3230	100
1.9076-1.9361	0.1994	153	0.1739	3068	3221	100
1.9361-1.9663	0.1976	150	0.1665	3055	3205	100
1.9663-1.9985	0.2115	167	0.1647	3079	3246	100
1.9985-2.033	0.2175	141	0.1578	3038	3179	100
2.033-2.07	0.1906	178	0.1587	3047	3225	100
2.07-2.1098	0.188	177	0.1541	3054	3231	100
2.1098-2.1528	0.2076	148	0.1538	3033	3181	100
2.1528-2.1996	0.2116	174	0.1571	3046	3220	100
2.1996-2.2508	0.2119	179	0.1563	3064	3243	100
2.2508-2.3071	0.2203	159	0.158	3076	3235	100
2.3071-2.3695	0.1816	149	0.1604	3054	3203	100
2.3695-2.4392	0.1996	142	0.1623	3081	3223	100
2.4392-2.5179	0.2043	161	0.165	3054	3215	100
2.5179-2.6078	0.1868	142	0.1617	3081	3223	100
2.6078-2.7122	0.183	153	0.1647	3089	3242	100
2.7122-2.8356	0.1862	147	0.1667	3076	3223	100
2.8356-2.985	0.1959	165	0.1688	3055	3220	100
2.985-3.172	0.1857	147	0.1683	3093	3240	100
3.172-3.4167	0.1725	145	0.1539	3076	3221	100
3.4167-3.7602	0.1658	161	0.1466	3088	3249	100
3.7602-4.3036	0.1482	176	0.1354	3068	3244	100
4.3036-5.4192	0.1691	163	0.1364	3115	3278	100
5.4192-36.3682	0.1938	148	0.1596	3141	3289	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	0.0003	-0.0026	-0.0003	0.0027	-0.0033	-0.0008	0.0017	0.0082	0.001	0.0292	0.0287	-0.0362	0.0084	0.035	-0	0.0286	0.0368	-0.0132	0.0083	0.0502	0.0066	-10.8051	-35.2829	10.8737
2	0.0003	-0.0009	-0	0.0017	-0.0009	0.0006	-0.0167	-0.0021	0.0072	0.0052	0.0007	-0.0236	-0.0015	0.0191	-0	0.1152	0.041	0.0036	0.1315	0.0377	0.1088	0.9281	-41.904	6.4783
3	0.0001	-0.0067	-0.0009	0.002	-0.0012	0.0006	-0.0225	-0.0078	-0.0394	0.0075	0.0093	-0.03	0.0331	0.0056	0	0.0263	0.0888	-0.0497	-0.129	0.1475	-0.0722	-8.6186	-43.0703	7.6874
4	-0.0012	-0.0021	0.0006	0.0016	0.0036	0.0026	-0.0256	-0.0152	0.0107	-0.0067	-0.0028	0.0273	0.0229	0.0183	-0	-0.0192	0.1069	-0.0517	-0.1637	0.1042	-0.0383	-15.9957	-38.7224	1.5284
5	0.0106	-0.0076	0.0002	0.0118	-0.0248	0.0219	-0.0014	0.0294	0.0326	0.0357	0.0132	-0.0191	0.0351	-0.0132	0	0.0324	0.0041	0.0018	0.0128	-0.0057	0.025	-20.0752	-27.6515	2.7761
6	0.0006	0.0014	0.0002	0.0012	-0.0004	0.0013	0.007	0.0101	-0.0095	0.0071	0.0045	-0.0018	-0.0079	-0.0201	-0	0.0333	0.0071	-0	0.0333	-0.0015	0.0405	-28.3806	-21.2804	12.0265
7	0.0028	-0.0043	-0.0024	0.0046	0.0007	0.0033	-0.0084	-0.0141	-0.0038	-0.0197	0.0296	0.0081	-0.0054	-0.0192	0	0.0361	0.0019	-0.007	0.0362	-0.006	0.0432	-24.498	-29.7754	11.0999
8	0.0005	0.0032	0.005	0.002	-0.0024	0.0057	0.0049	-0.0148	0.0343	0.0806	0.0673	-0.0281	-0.0061	0.0462	0	0.0804	0.0323	0.0674	0.0799	-0.0188	-0.1365	-22.375	-24.8701	21.4556
9	-0.0002	-0.002	0.0043	0.0041	-0.002	0.0004	0.0041	-0.0219	0.0007	0.0865	0.0796	-0.03	-0.0081	0.0073	0	-0.0046	0.0394	-0.0575	-0.0106	0.0403	-0.0667	-21.0997	-32.4703	19.0514
10	-0.0009	-0.0072	0.0003	-0.0085	-0.0071	0.0002	-0.0151	-0.0183	-0.0028	0.1335	-0.0017	-0.0122	0.0087	0.017	0	-0.1551	0.175	-0.3412	-0.0418	0.2268	-0.4087	-10.2077	-34.8634	21.0321
11	0.001	-0.003	0.0002	0.0038	0.0028	0.002	-0.0087	0.042	-0.0023	-0.0005	0.0154	0.0031	0.0126	0.0509	0	0.043	-0.0058	0.0036	0.0755	0.0025	0.0256	-7.1856	-29.1693	-25.3955
12	0	0.0001	-0.0007	-0.0001	-0.0004	0.0008	-0.0067	-0.0058	-0.005	-0.0139	-0.0079	-0.0028	0.01	0.001	-0	0.1776	-0.0033	0.0424	0.0583	-0.0205	0.0638	-11.5298	-45.2203	-21.6658
13	0.0021	-0.0009	-0.002	0.0004	-0.0007	0.0004	0.0022	0.0374	-0.0233	-0.0104	-0.0004	-0.0113	0.0136	0.0269	-0	0.0162	0.0433	0.1047	0.0514	-0.032	-0.095	-4.927	-37.6502	-21.0211
14	0.0053	0.0055	-0.0046	-0.0001	-0.0079	0.0036	0.0429	-0.0316	0.0233	-0.074	-0.0034	0.0073	0.0451	0.0698	-0	-0.3676	0.2462	0.2214	-0.1204	-0.1229	-0.0899	-5.8552	-27.2043	-10.8964
15	0.0013	0	0.0002	0.0009	-0.0003	0.0003	-0.0252	0.0011	0.0189	0.001	-0.0179	0.0023	-0.0016	0.0202	-0	0.0348	-0.002	-0.0019	0.0259	0.002	0.0417	-1.7946	-17.5916	-9.6083
16	-0.0003	0.0038	-0.004	0.0064	-0.0037	0.0058	-0.0482	0.0007	0.0487	-0.0005	-0.0117	0.017	-0.0192	0.0491	0	-0.1356	0.1486	-0.0957	-0.1171	0.0795	0.0443	-9.1835	-12.2415	-20.3897
17	0.0006	0.0009	0.0006	0.003	0.005	0.0007	0.0049	-0.0007	0.0154	-0.0046	0.0266	-0.0097	-0.0002	0.0015	-0	0.0418	-0.0246	-0.0024	0.0639	0.0433	0.0827	-16.7447	-17.9862	-26.0054
18	0.0015	-0	-0.0011	0.0016	-0.0014	0.003	0.0113	0.0106	0.0113	-0.0119	0.0222	-0.0122	-0.0171	-0.0111	-0	0.0845	-0.0754	-0.0052	0.1207	0.0682	0.0816	-6.3708	-11.1087	-30.7613
19	0.0001	-0.0031	0.0014	0.0062	-0.008	0.0046	0.0095	0.0014	0.0001	-0.0477	0.0164	0.023	-0.0038	0.0158	-0	-0.0689	-0.0954	0.0169	0.0847	0.0122	0.045	-5.1789	-20.1031	-29.6092
20	-0.0018	-0.0018	-0.0005	-0.0001	0.0013	0.0012	-0.0068	0.0026	0.031	-0.053	0.0028	0.0172	0.0197	-0.0059	-0	0.0622	-0.0397	-0.0452	0.1414	0.005	-0.2686	-11.0318	-29.2622	-32.7363
21	0.0031	-0.0048	0.0017	0.0008	-0.0033	0.0006	0.0305	-0.0066	0.0016	0.0142	0.0453	-0.0153	0.0093	-0.0027	0	0.0059	0.0015	-0.0139	0.0502	0.0198	0.049	0.0023	8.5529	-46.4203
22	-0.0007	-0.0008	-0.0014	0.0015	-0.0004	0.0003	0.0129	0.0051	0.0034	0.0013	0.0089	-0.0123	0.0118	0.0118	0	0.1223	0.0231	-0.0275	0.0305	0.0109	0.1207	10.8424	-0.2081	-50.5467
23	0.0014	-0.0018	-0.0004	0.002	-0.0002	0.0003	-0.0082	0.0071	-0.0337	0.0156	0.0184	-0.0075	0.0194	0.0086	-0	0.0463	0.0194	0.0001	-0.0581	0.0549	0.0468	0.979	1.0351	-50.1918
24	0.0093	-0.0037	-0.0129	-0.0001	0.0024	0.0181	-0.0013	0.0384	0.0056	0.0209	0.0051	-0.0204	0.0211	-0.016	0	0.024	-0.0019	-0.0075	0.0135	0.0043	0.028	-7.761	12.2976	-57.6163
25	0.005	-0.0057	0.0039	0.0027	-0.0029	0.0069	0.0465	-0.0149	0.0006	-0.0051	0.0212	0.0126	-0.0348	-0.0129	0	0.0444	-0.0041	-0.002	0.0366	-0.0044	0.0399	-11.8083	23.863	-45.0243
26	0.0026	-0.0051	-0.0017	0.0038	-0.0024	0.0047	-0.0203	-0.0047	-0.0318	0.0264	-0.0289	0.017	-0.0209	0.0073	-0	0.0133	-0.0457	-0.0368	-0.0058	-0.0406	-0.0046	-10.7946	17.013	-44.1168
27	0.0012	0.0009	-0.0011	0.0006	0.0001	0.0013	0.0076	-0.0126	0.0079	0.0203	0.0167	-0.0115	-0.0309	-0.0066	0	0.0847	0.0089	0.0038	0.0928	-0.0013	0.0441	-14.7494	19.2699	-35.0393
28	0.0026	-0.0069	0.0065	0.0045	-0.003	0.0097	0.0237	-0.026	0.0283	0.1517	0.0075	-0.02	0.0345	-0.024	-0	0.0088	0.0118	-0.0816	0.0741	0.0217	-0.0318	-3.2812	9.9535	-37.0345
29	0.0041	-0.0008	0.0058	0.0016	0.0023	0.0046	-0.0248	0.038	0.0184	-0.0106	-0.0122	-0.0184	-0.0181	0.0318	0	0.0317	-0.0202	0.0154	0.0727	0.0125	0.0202	4.3317	15.0738	-82.5259
30	-0.0004	0.0003	-0.0005	0.001	0.0011	0.0008	0.003	-0.0022	-0.006	-0.0156	-0.0083	0.0128	0.0123	-0.0043	-0	0.1223	0.0065	-0.0036	0.0435	-0.0197	0.0603	-1.6584	-0.6167	-79.0434
31	-0.0013	-0.0032	-0.002	-0.0027	0.0021	0.0005	0.0112	0.0165	0.0041	-0.03	-0.0116	-0.0449	0.0271	0.0083	-0	-0.1179	0.0997	0.179	-0.0274	-0.1034	-0.1314	5.6606	6.2876	-78.2444
32	0.0062	0.0108	-0.0035	0.0086	-0.0123	0.0064	0.0361	-0.0089	0.0439	-0.0139	-0.0115	-0.0072	0.0369	0.0494	-0	0.0249	0.0018	0.0063	0.0301	-0.0042	0.0429	5.7276	16.5138	-68.0551
33	0.0017	0.0012	0.0006	0.0008	0.0003	0.0004	0.0111	0.0017	0.013	0.0137	0.014	0.0044	0.0119	0.0328	-0	-0.0058	-0.0352	0.0134	0.072	-0.0286	0.1071	10.5312	26.0046	-66.5693
34	0.0007	0.0041	0.0063	0.0051	0.0063	0.0044	0.0315	0.0145	0.0177	0.0079	0.06	-0.0016	-0.0097	0.0008	0	0.0473	0.0169	0.014	-0.0078	0.0369	0.1391	-0.7122	30.9629	-77.9057
35	0.0004	0.0017	0.0001	0.0012	-0.001	-0.0002	0.0173	-0.0038	-0.0034	0.003	0.011	-0.0042	-0.0074	0.0067	0	0.0905	-0.03	0.0051	-0.0027	0.0399	0.2744	5.8559	35.6694	-76.626
36	0.0013	0.0024	-0.0036	-0.0003	-0.0021	0.0015	-0.017	0.0026	0.0088	-0.0009	-0.0372	-0.0115	-0.023	0.0078	-0	-0.0714	-0.0949	0.0709	-0.0295	0.098	0.0248	-1.6716	26.8911	-81.657
37	0.0002	0.0021	-0.0004	-0.0006	-0.0019	0.0001	0.0233	-0.0017	0.0025	-0.0144	0.01	0.0057	-0.0175	0.0052	0	0.0341	-0.0745	0.0939	0.0776	0.1791	0.1801	6.8932	33.0793	-87.4816
38	0.003	-0.0044	-0.001	0.0053	0.0033	0.003	0.0247	0.0642	0.0325	-0.0884	-0.0022	0.0205	0.0286	-0.0269	-0	0.0363	-0.0177	0.0405	0.1073	0.0166	0.0194	3.0347	18.723	-88.5978

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 5 through 18 )	A	5 - 18
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 19 through 30 )	A	19 - 30
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 31 through 55 )	A	31 - 55
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 56 through 72 )	A	56 - 72
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 73 through 139 )	A	73 - 139
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 140 through 152 )	A	140 - 152
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 153 through 170 )	A	153 - 170
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 171 through 196 )	A	171 - 196
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 197 through 217 )	A	197 - 217
10	X-RAY DIFFRACTION	10	chain 'A' and (resid 218 through 249 )	A	218 - 249
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 2 through 18 )	B	2 - 18
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 19 through 31 )	B	19 - 31
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 32 through 55 )	B	32 - 55
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 56 through 106 )	B	56 - 106
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 107 through 120 )	B	107 - 120
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 121 through 160 )	B	121 - 160
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 161 through 178 )	B	161 - 178
18	X-RAY DIFFRACTION	18	chain 'B' and (resid 179 through 196 )	B	179 - 196
19	X-RAY DIFFRACTION	19	chain 'B' and (resid 197 through 217 )	B	197 - 217
20	X-RAY DIFFRACTION	20	chain 'B' and (resid 218 through 249 )	B	218 - 249
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 5 through 18 )	C	5 - 18
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 19 through 31 )	C	19 - 31
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 32 through 55 )	C	32 - 55
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 56 through 119 )	C	56 - 119
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 120 through 152 )	C	120 - 152
26	X-RAY DIFFRACTION	26	chain 'C' and (resid 153 through 178 )	C	153 - 178
27	X-RAY DIFFRACTION	27	chain 'C' and (resid 179 through 196 )	C	179 - 196
28	X-RAY DIFFRACTION	28	chain 'C' and (resid 197 through 249 )	C	197 - 249
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 2 through 18 )	D	2 - 18
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 19 through 31 )	D	19 - 31
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 32 through 55 )	D	32 - 55
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 56 through 106 )	D	56 - 106
33	X-RAY DIFFRACTION	33	chain 'D' and (resid 107 through 120 )	D	107 - 120
34	X-RAY DIFFRACTION	34	chain 'D' and (resid 121 through 139 )	D	121 - 139
35	X-RAY DIFFRACTION	35	chain 'D' and (resid 140 through 152 )	D	140 - 152
36	X-RAY DIFFRACTION	36	chain 'D' and (resid 153 through 178 )	D	153 - 178
37	X-RAY DIFFRACTION	37	chain 'D' and (resid 179 through 196 )	D	179 - 196
38	X-RAY DIFFRACTION	38	chain 'D' and (resid 197 through 249 )	D	197 - 249

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