PDB-5pzt: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosph...

ID or keywords:

Entry

Database: PDB / ID: 5pzt

Title

Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-(3-ethyl-4-phenylphenyl)sulfonylurea

Components

Fructose-1,6-bisphosphatase 1

Fructose 1,6-bisphosphatase

Keywords

HYDROLASE/HYDROLASE INHIBITOR / D3R docking / HYDROLASE-HYDROLASE INHIBITOR complex

Function / homology

Function and homology information

cellular response to raffinose / sucrose biosynthetic process / cellular hypotonic salinity response / cellular response to phorbol 13-acetate 12-myristate / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / negative regulation of Ras protein signal transduction / fructose 1,6-bisphosphate metabolic process / cellular response to magnesium ion / fructose 6-phosphate metabolic process ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.8 Å

Model details

For D3R project

Authors

Ruf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G. / Yang, H. / Shao, C. / Burley, S.K.

Citation

Journal: To be published
Title: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-(3-ethyl-4-phenylphenyl)sulfonylurea
Authors: Ruf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G.

History

Deposition	Apr 18, 2017	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jan 9, 2019	Provider: repository / Type: Initial release
Revision 1.1	Jan 16, 2019	Group: Data collection / Category: diffrn_radiation / Item: _diffrn_radiation.pdbx_diffrn_protocol
Revision 1.2	Feb 6, 2019	Group: Data collection / Database references / Structure summary Category: audit_author / citation_author / Item: _audit_author.name / _citation_author.name
Revision 1.3	Feb 10, 2021	Group: Structure summary / Category: audit_author / Item: _audit_author.identifier_ORCID
Revision 1.4	Mar 6, 2024	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / 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	5pzt.cif.gz	942.7 KB	Display	PDBx/mmCIF format
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Validation report

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

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Group deposition

ID	G_1002030 (23 entries) 5pzq 5pzr 5pzs 5pzt 5pzu 5pzv 5pzw 5pzx 5pzy 5pzz
Title	Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with allosteric inhibitors
Type	undefined
Description	Fructose-1,6-bisphosphatase 1 with inhibitors

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Related structure data

Similar structure data	2y5l-1 5pzx-2 5q04-2 4mjo-1 5pzr-d 3kc0-d 4fbp-d 5pzu-d 2y5l-2 4kxp-1 5q02-d 5pzy-2 5q07-1 5pzw-d 5pzv-d 5pzz-1 2wbd-2 5q04-1 5q0b-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

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#50 - Feb 2004 Glycolytic Enzymes similarity (1)

Deposited unit

A: Fructose-1,6-bisphosphatase 1

B: Fructose-1,6-bisphosphatase 1

C: Fructose-1,6-bisphosphatase 1

D: Fructose-1,6-bisphosphatase 1

E: Fructose-1,6-bisphosphatase 1

F: Fructose-1,6-bisphosphatase 1

G: Fructose-1,6-bisphosphatase 1

H: Fructose-1,6-bisphosphatase 1

hetero molecules

299 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Fructose-1,6-bisphosphatase 1

B: Fructose-1,6-bisphosphatase 1

C: Fructose-1,6-bisphosphatase 1

D: Fructose-1,6-bisphosphatase 1

hetero molecules

defined by author&software
149 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: Fructose-1,6-bisphosphatase 1

F: Fructose-1,6-bisphosphatase 1

G: Fructose-1,6-bisphosphatase 1

H: Fructose-1,6-bisphosphatase 1

hetero molecules

defined by author&software
149 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	66.435, 294.192, 83.569
Angle α, β, γ (deg.)	90.000, 97.560, 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 9 through 54 or resid 72 through 139 or resid 141 through 335))
2	1	(chain B and (resid 9 through 139 or resid 141 through 335))
3	1	(chain C and (resid 9 through 139 or resid 141 through 335))
4	1	(chain D and (resid 9 through 139 or resid 141 through 335))
5	1	(chain E and (resid 9 through 54 or resid 72 through 139 or resid 141 through 335))
6	1	(chain F and (resid 9 through 139 or resid 141 through 335))
7	1	(chain G and (resid 9 through 139 or resid 141 through 335))
8	1	(chain H and (resid 9 through 139 or resid 141 through 335))

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	ASP	ASP	ALA	ALA	(chain A and (resid 9 through 54 or resid 72 through 139 or resid 141 through 335))	A	A	9 - 54	10 - 55
1	2	LYS	LYS	TYR	TYR	(chain A and (resid 9 through 54 or resid 72 through 139 or resid 141 through 335))	A	A	72 - 139	73 - 140
1	3	LYS	LYS	SER	SER	(chain A and (resid 9 through 54 or resid 72 through 139 or resid 141 through 335))	A	A	141 - 335	142 - 336
2	1	ASP	ASP	TYR	TYR	(chain B and (resid 9 through 139 or resid 141 through 335))	B	B	9 - 139	10 - 140
2	2	LYS	LYS	SER	SER	(chain B and (resid 9 through 139 or resid 141 through 335))	B	B	141 - 335	142 - 336
3	1	ASP	ASP	TYR	TYR	(chain C and (resid 9 through 139 or resid 141 through 335))	C	C	9 - 139	10 - 140
3	2	LYS	LYS	SER	SER	(chain C and (resid 9 through 139 or resid 141 through 335))	C	C	141 - 335	142 - 336
4	1	ASP	ASP	TYR	TYR	(chain D and (resid 9 through 139 or resid 141 through 335))	D	D	9 - 139	10 - 140
4	2	LYS	LYS	SER	SER	(chain D and (resid 9 through 139 or resid 141 through 335))	D	D	141 - 335	142 - 336
5	1	ASP	ASP	ALA	ALA	(chain E and (resid 9 through 54 or resid 72 through 139 or resid 141 through 335))	E	E	9 - 54	10 - 55
5	2	LYS	LYS	TYR	TYR	(chain E and (resid 9 through 54 or resid 72 through 139 or resid 141 through 335))	E	E	72 - 139	73 - 140
5	3	LYS	LYS	SER	SER	(chain E and (resid 9 through 54 or resid 72 through 139 or resid 141 through 335))	E	E	141 - 335	142 - 336
6	1	ASP	ASP	TYR	TYR	(chain F and (resid 9 through 139 or resid 141 through 335))	F	F	9 - 139	10 - 140
6	2	LYS	LYS	SER	SER	(chain F and (resid 9 through 139 or resid 141 through 335))	F	F	141 - 335	142 - 336
7	1	ASP	ASP	TYR	TYR	(chain G and (resid 9 through 139 or resid 141 through 335))	G	G	9 - 139	10 - 140
7	2	LYS	LYS	SER	SER	(chain G and (resid 9 through 139 or resid 141 through 335))	G	G	141 - 335	142 - 336
8	1	ASP	ASP	TYR	TYR	(chain H and (resid 9 through 139 or resid 141 through 335))	H	H	9 - 139	10 - 140
8	2	LYS	LYS	SER	SER	(chain H and (resid 9 through 139 or resid 141 through 335))	H	H	141 - 335	142 - 336

#1: Protein	Fructose-1,6-bisphosphatase 1 / Fructose 1,6-bisphosphatase / Growth-inhibiting protein 17 / cDNA FLJ75786 / highly similar to Homo sapiens fructose-1 / 6- ...Growth-inhibiting protein 17 / cDNA FLJ75786 / highly similar to Homo sapiens fructose-1 / 6-bisphosphatase 1 (FBP1) / mRNA Mass: 36859.418 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FBP1, hCG_1640493 / Production host: Escherichia coli (E. coli) References: UniProt: Q2TU34, UniProt: P09467*PLUS, fructose-bisphosphatase
#2: Chemical	ChemComp-947 / N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-2-ethyl[1,1'-biphenyl]-4-sulfonamide Mass: 466.372 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₁₈H₁₆BrN₃O₃S₂
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 79 / 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: 2.84 Å³/Da / Density % sol: 56.63 %
Crystal grow	Temperature: 300 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 0.1M HEPES pH 7.0, 0.1M AMMONIUM ACETATE, 12%-25% PEG 3350

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.987 Å
Detector	Type: MAR CCD 165 mm / Detector: CCD / Date: Dec 6, 2005
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.987 Å / Relative weight: 1
Reflection	Resolution: 2.8→29.501 Å / Num. obs: 77696 / % possible obs: 99.92 %

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification	NB
PHENIX	1.11.1_2575	refinement
PDB_EXTRACT	3.23	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.8→29.501 Å / SU ML: 0.42 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 28.73 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2612	3891	5.01 %
R_work	0.1925	73805	-
obs	0.196	77696	99.92 %

Solvent computation

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

Displacement parameters

B_iso max: 156.63 Å² / B_iso mean: 64.7461 Å² / B_iso min: 16.23 Å²

Refinement step

Cycle: final / Resolution: 2.8→29.501 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19032	0	216	79	19327
B_iso mean	-	-	64.97	42.06	-
Num. residues	-	-	-	-	2484

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.009	19625
X-RAY DIFFRACTION	f_angle_d	1.099	26513
X-RAY DIFFRACTION	f_chiral_restr	0.063	2998
X-RAY DIFFRACTION	f_plane_restr	0.007	3386
X-RAY DIFFRACTION	f_dihedral_angle_d	12.528	11945

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	11980	X-RAY DIFFRACTION	12.181	TORSIONAL
1	2	B	11980	X-RAY DIFFRACTION	12.181	TORSIONAL
1	3	C	11980	X-RAY DIFFRACTION	12.181	TORSIONAL
1	4	D	11980	X-RAY DIFFRACTION	12.181	TORSIONAL
1	5	E	11980	X-RAY DIFFRACTION	12.181	TORSIONAL
1	6	F	11980	X-RAY DIFFRACTION	12.181	TORSIONAL
1	7	G	11980	X-RAY DIFFRACTION	12.181	TORSIONAL
1	8	H	11980	X-RAY DIFFRACTION	12.181	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 28

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.8-2.8341	0.3585	127	0.2745	2664	2791	100
2.8341-2.87	0.3667	140	0.2597	2628	2768	100
2.87-2.9077	0.3315	166	0.2443	2653	2819	100
2.9077-2.9475	0.3408	146	0.2488	2559	2705	100
2.9475-2.9896	0.3653	135	0.2462	2671	2806	100
2.9896-3.0342	0.339	147	0.2593	2597	2744	100
3.0342-3.0815	0.3512	130	0.251	2632	2762	100
3.0815-3.132	0.4011	127	0.241	2652	2779	100
3.132-3.1859	0.3186	144	0.2322	2624	2768	100
3.1859-3.2438	0.2917	111	0.2183	2629	2740	100
3.2438-3.3061	0.266	140	0.2063	2656	2796	100
3.3061-3.3735	0.2905	113	0.1993	2624	2737	100
3.3735-3.4467	0.2864	146	0.2083	2645	2791	100
3.4467-3.5268	0.2707	147	0.2095	2640	2787	100
3.5268-3.6148	0.2987	123	0.2083	2638	2761	100
3.6148-3.7124	0.2578	152	0.2052	2633	2785	100
3.7124-3.8214	0.281	154	0.1982	2619	2773	100
3.8214-3.9445	0.2667	139	0.192	2641	2780	100
3.9445-4.0851	0.2405	141	0.1775	2612	2753	100
4.0851-4.2482	0.2691	141	0.1723	2641	2782	100
4.2482-4.441	0.2324	143	0.1652	2655	2798	100
4.441-4.6742	0.2206	161	0.1573	2598	2759	100
4.6742-4.9658	0.2321	122	0.1558	2648	2770	100
4.9658-5.3471	0.233	131	0.1636	2638	2769	100
5.3471-5.8814	0.2396	130	0.1807	2672	2802	100
5.8814-6.7236	0.2375	148	0.187	2646	2794	100
6.7236-8.4381	0.214	138	0.181	2647	2785	100
8.4381-29.5027	0.2094	149	0.1754	2643	2792	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	0.0398	-0.0217	0.0021	0.0238	-0.0139	0.0141	-0.0757	-0.059	0.0918	-0.2229	0.0586	-0.1643	-0.0092	-0.0324	-0.002	0.424	-0.0727	0.0296	0.2732	0.0322	0.3316	36.8573	11.6008	-5.9446
2	0.0179	-0.0084	0.0184	0.0102	-0.014	0.0158	-0.0287	-0.0628	0.0448	-0.2706	0.0517	-0.1895	-0.0824	0.0344	-0.0001	0.5743	0.0189	0.0366	0.3505	0.0807	0.3985	37.6204	23.1158	-4.8538
3	0.0479	-0.0558	-0.0237	0.1184	-0.0802	0.0563	-0.0399	0.1051	-0.0696	-0.6916	0.0473	-0.0316	-0.2443	0.1658	-0.0659	0.6706	0.1069	-0.2378	0.0745	0.1697	0.2589	19.3498	26.0695	-8.7884
4	0.0737	0.061	0.0437	0.1885	0.109	0.1063	-0.0527	-0.0258	-0.1133	-0.1804	0.0509	0.1192	0.0465	0.1013	-0.0034	0.1593	0.0759	-0.0093	0.2095	0.053	0.3675	12.3436	-1.4815	17.8841
5	0.0569	0.0193	-0.01	0.0723	0.0595	0.1582	-0.0508	-0.1722	-0.0562	0.0328	-0.0422	0.3496	-0.1979	0.1078	-0.0829	0.1772	0.1389	-0.0142	0.2239	-0.0251	0.4978	6.2446	17.6742	18.3952
6	0.1083	-0.0816	-0.0115	0.0576	0.0007	0.0309	0.0223	0.0933	-0.1156	-0.1383	0.034	0.1999	-0.1121	0.1783	0.0079	0.3768	0.0283	0.0209	0.3289	0.0626	0.2202	38.3059	-9.9211	-11.2885
7	0.0019	-0.0572	0.0146	0.0654	-0.0008	0.0682	0.0583	0.0717	0.0444	-0.1815	-0.1061	-0.0605	0.081	0.202	-0	0.338	0.077	0.0954	0.3599	0.0442	0.2915	54.7872	-19.8448	-5.7193
8	0.0058	-0.0026	-0.0038	0.0015	0.0013	0.001	0.0172	0.009	-0.0006	0.0017	0.0572	0.0396	-0.0642	-0.0288	0	0.3129	0.0703	0.0611	0.4109	0.0483	0.3715	20.5436	-13.6525	27.8211
9	0.0348	0.0298	0.0391	0.089	0.0342	0.0226	0.0372	-0.0265	0.1031	0.1604	0.0297	0.1076	-0.0812	0.1704	-0	0.2574	-0.0282	0.0187	0.2981	-0.0157	0.1822	41.7049	-7.0759	29.3697
10	0.0322	0.004	0.0096	0.0139	0.033	0.0105	0.0899	0.0342	-0.0034	-0.0521	-0.0884	0.0677	0.0178	0.1469	-0	0.3003	0.0261	-0.0102	0.2165	0.0498	0.3028	34.6623	-20.4448	19.4097
11	0.0027	-0.0024	0.0071	0	-0.0042	0.0063	-0.0992	-0.0085	-0.0924	-0.0003	0.025	-0.0291	0.0403	0.0146	0	0.4588	0.1051	-0.0169	0.4875	-0.0234	0.424	58.4641	-35.1968	17.0534
12	0.0158	0.0008	-0.0081	0.0036	-0.0054	0.0058	0.0287	0.0236	-0.0297	-0.0183	0.0369	-0.0331	0.0915	0.0126	-0	0.4883	0.0693	0.0901	0.3477	0.0655	0.3594	49.5922	-36.1247	10.1983
13	0.0061	-0.0308	-0.0184	0.0031	0.0105	0.0166	0.0326	-0.0043	0.1051	0.1042	-0.0967	0.0931	0.1138	0.1005	0	0.3111	0.0633	-0.0038	0.3193	0.0064	0.3197	48.4277	-27.7331	26.2038
14	-0.0014	0.0027	0.0009	0.004	0.0066	0.0027	-0.0109	-0.0667	0.0115	-0.0292	-0.0094	-0.0563	-0.0151	-0.0487	0	0.5092	0.0653	0.043	0.3581	0.0667	0.3669	-7.7102	63.5312	55.9343
15	0.0282	0.0321	-0.0026	0.0262	-0.0125	0.0118	0.059	0.132	-0.107	0.2162	0.0885	-0.0231	0.1854	-0.0235	-0	0.4806	-0.0062	-0.0777	0.2644	0.0124	0.3104	0.1397	49.0899	40.5192
16	0.0521	0.0129	-0.0449	0.0202	0.0255	0.0397	-0.0342	-0.1269	-0.1072	0.1285	-0.1385	0.103	0.2806	-0.1668	-0.0011	0.4118	-0.1205	0.0689	0.2843	0.0055	0.4878	-18.9536	46.081	41.3905
17	0.0117	0.0079	-0.0013	0.0072	-0.013	-0.0018	0.0341	-0.249	0.0821	0.1224	-0.0985	0.0758	0.1551	-0.0035	-0.0001	0.6221	-0.1674	0.0887	0.2815	-0.0045	0.5569	-19.6141	37.8652	42.7395
18	0.0124	0.01	0.0001	0.0329	0.0036	-0	0.0041	0.1061	0.0477	0.072	0.0403	0.0217	0.0019	0.0537	-0	0.3115	0.1075	0.0086	0.4434	-0.0671	0.3997	-9.5533	68.9423	10.3559
19	0.0487	0.0581	-0.0047	0.0334	-0.0066	0.0609	0.2889	0.0902	-0.0014	-0.0881	-0.1257	0.0576	-0.1444	-0.172	0.0486	0.0259	0.2192	-0.2376	0.4888	-0.084	0.323	-24.6168	70.3029	16.3906
20	0.18	0.0134	0.0679	0.0383	0.0032	0.1185	-0.1483	0.1312	-0.0133	0.0405	-0.0941	0.1876	0.4199	-0.137	-0.2605	-0.1158	0.0841	-0.1425	0.3563	-0.1967	0.4514	-24.8803	50.5588	12.4453
21	0.0193	0.0215	0.0279	0.0312	0.0571	0.0768	0.0128	-0.1066	0.0647	0.1798	-0.0365	0.1663	0.1938	0.0153	0	0.3138	-0.0278	0.0475	0.3455	-0.0041	0.2296	-1.3199	79.671	51.7478
22	0.0336	0.0382	0.0068	0.0337	0.0153	0.0514	0.0964	0.0307	-0.0024	0.0874	-0.0512	0.0259	-0.1493	0.1145	0	0.2894	-0.0823	-0.0229	0.3632	0	0.2344	17.199	89.0176	46.5529
23	0.0124	0.0021	-0.0015	0.0053	-0.022	0.034	0.0828	0.0952	-0.1014	-0.0886	-0.0139	0.0652	-0.0377	0.1054	0	0.426	0.0928	-0.0186	0.3952	-0.0314	0.2384	7.5729	76.1561	12.3463
24	0.0332	0.093	0.0629	0.0547	-0.0618	0.0594	0.0121	0.0521	0.0503	-0.1418	-0.0271	0.0422	-0.1954	0.1649	-0.0004	0.369	-0.0389	0.0595	0.3679	0.0176	0.2666	13.6906	94.6432	17.7055

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 9 through 88 )	A	9 - 88
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 89 through 140 )	A	89 - 140
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 141 through 335 )	A	141 - 335
4	X-RAY DIFFRACTION	4	chain 'B' and (resid 9 through 140 )	B	9 - 140
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 141 through 335 )	B	141 - 335
6	X-RAY DIFFRACTION	6	chain 'C' and (resid 9 through 131 )	C	9 - 131
7	X-RAY DIFFRACTION	7	chain 'C' and (resid 132 through 335 )	C	132 - 335
8	X-RAY DIFFRACTION	8	chain 'D' and (resid 9 through 28 )	D	9 - 28
9	X-RAY DIFFRACTION	9	chain 'D' and (resid 29 through 155 )	D	29 - 155
10	X-RAY DIFFRACTION	10	chain 'D' and (resid 156 through 212 )	D	156 - 212
11	X-RAY DIFFRACTION	11	chain 'D' and (resid 213 through 231 )	D	213 - 231
12	X-RAY DIFFRACTION	12	chain 'D' and (resid 232 through 247 )	D	232 - 247
13	X-RAY DIFFRACTION	13	chain 'D' and (resid 248 through 335 )	D	248 - 335
14	X-RAY DIFFRACTION	14	chain 'E' and (resid 9 through 28 )	E	9 - 28
15	X-RAY DIFFRACTION	15	chain 'E' and (resid 29 through 140 )	E	29 - 140
16	X-RAY DIFFRACTION	16	chain 'E' and (resid 141 through 247 )	E	141 - 247
17	X-RAY DIFFRACTION	17	chain 'E' and (resid 248 through 335 )	E	248 - 335
18	X-RAY DIFFRACTION	18	chain 'F' and (resid 9 through 50 )	F	9 - 50
19	X-RAY DIFFRACTION	19	chain 'F' and (resid 51 through 140 )	F	51 - 140
20	X-RAY DIFFRACTION	20	chain 'F' and (resid 141 through 335 )	F	141 - 335
21	X-RAY DIFFRACTION	21	chain 'G' and (resid 9 through 155 )	G	9 - 155
22	X-RAY DIFFRACTION	22	chain 'G' and (resid 156 through 335 )	G	156 - 335
23	X-RAY DIFFRACTION	23	chain 'H' and (resid 9 through 140 )	H	9 - 140
24	X-RAY DIFFRACTION	24	chain 'H' and (resid 141 through 335 )	H	141 - 335

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