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

ID or keywords:

Entry

Database: PDB / ID: 5pzz

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-(3,4-dichlorophenyl)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: 2.5 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-(3,4-dichlorophenyl)sulfonylurea
Authors: Ruf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G.

History

Deposition	Apr 28, 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: Advisory / Data collection ...Advisory / Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_unobs_or_zero_occ_atoms / 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	5pzz.cif.gz	966.3 KB	Display	PDBx/mmCIF format
PDB format	pdb5pzz.ent.gz	811.1 KB	Display	PDB format
PDBx/mmJSON format	5pzz.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/pz/5pzz ftp://data.pdbj.org/pub/pdb/validation_reports/pz/5pzz	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	5pzx-2 4mjo-2 1fta-d 5pzu-d 5q01-1 3kbz-d 5q07-1 4fbp-d 2fix-d 5q09-2 5pzy-2 2wbd-2 5pzw-d 2wbb-1 1fpi-1 5q0c-1 1fpe-1 5q02-d 5pzv-d 3kc0-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

298 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)	66.001, 283.850, 83.478
Angle α, β, γ (deg.)	90.000, 97.750, 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 61 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 61 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	GLY	GLY	(chain A and (resid 9 through 61 or resid 72 through 139 or resid 141 through 335))	A	A	9 - 61	10 - 62
1	2	LYS	LYS	TYR	TYR	(chain A and (resid 9 through 61 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 61 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	GLY	GLY	(chain E and (resid 9 through 61 or resid 72 through 139 or resid 141 through 335))	E	E	9 - 61	10 - 62
5	2	LYS	LYS	TYR	TYR	(chain E and (resid 9 through 61 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 61 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-94Y / N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3,4-dichlorobenzene-1-sulfonamide Mass: 431.113 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₁₀H₆BrCl₂N₃O₃S₂
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 265 / 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: 2.71 Å³/Da / Density % sol: 54.68 %
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: Oct 17, 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: 2.5→24.463 Å / Num. obs: 104007 / % possible obs: 99.55 %

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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: 2.5→24.463 Å / SU ML: 0.38 / Cross valid method: THROUGHOUT / σ(F): 1.37 / Phase error: 28.05 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.249	5192	4.99 %
R_work	0.1835	98815	-
obs	0.1869	104007	99.55 %

Solvent computation

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

Displacement parameters

B_iso max: 165.35 Å² / B_iso mean: 59.5827 Å² / B_iso min: 18.99 Å²

Refinement step

Cycle: final / Resolution: 2.5→24.463 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19440	0	160	265	19865
B_iso mean	-	-	68.2	48.24	-
Num. residues	-	-	-	-	2540

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	19993
X-RAY DIFFRACTION	f_angle_d	1.044	27017
X-RAY DIFFRACTION	f_chiral_restr	0.061	3054
X-RAY DIFFRACTION	f_plane_restr	0.007	3450
X-RAY DIFFRACTION	f_dihedral_angle_d	10.601	12137

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	12206	X-RAY DIFFRACTION	9.882	TORSIONAL
1	2	B	12206	X-RAY DIFFRACTION	9.882	TORSIONAL
1	3	C	12206	X-RAY DIFFRACTION	9.882	TORSIONAL
1	4	D	12206	X-RAY DIFFRACTION	9.882	TORSIONAL
1	5	E	12206	X-RAY DIFFRACTION	9.882	TORSIONAL
1	6	F	12206	X-RAY DIFFRACTION	9.882	TORSIONAL
1	7	G	12206	X-RAY DIFFRACTION	9.882	TORSIONAL
1	8	H	12206	X-RAY DIFFRACTION	9.882	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 (%)
2.5-2.5284	0.3672	174	0.2935	3393	3567	100
2.5284-2.5581	0.3557	155	0.2913	3262	3417	100
2.5581-2.5893	0.3785	137	0.282	3331	3468	100
2.5893-2.622	0.3558	178	0.2738	3337	3515	100
2.622-2.6565	0.3326	187	0.2719	3244	3431	100
2.6565-2.6928	0.3328	147	0.2678	3354	3501	100
2.6928-2.7313	0.3489	173	0.258	3258	3431	100
2.7313-2.772	0.3303	181	0.2464	3324	3505	100
2.772-2.8152	0.3475	173	0.2398	3285	3458	100
2.8152-2.8613	0.3295	176	0.2265	3319	3495	100
2.8613-2.9106	0.2947	162	0.2112	3314	3476	100
2.9106-2.9634	0.2763	168	0.2005	3281	3449	100
2.9634-3.0203	0.2625	180	0.2087	3311	3491	100
3.0203-3.0818	0.2986	183	0.2047	3267	3450	100
3.0818-3.1487	0.2763	192	0.2033	3308	3500	100
3.1487-3.2218	0.2827	185	0.1882	3272	3457	100
3.2218-3.3022	0.2822	155	0.1849	3380	3535	100
3.3022-3.3913	0.2435	189	0.1815	3228	3417	100
3.3913-3.4908	0.2378	174	0.1811	3324	3498	100
3.4908-3.6031	0.2564	183	0.1742	3274	3457	100
3.6031-3.7315	0.2457	165	0.1759	3307	3472	100
3.7315-3.8803	0.2302	188	0.1766	3323	3511	100
3.8803-4.0561	0.2322	180	0.1595	3267	3447	100
4.0561-4.2689	0.2129	189	0.1532	3284	3473	100
4.2689-4.5348	0.2171	181	0.1456	3319	3500	100
4.5348-4.8824	0.1789	164	0.1381	3318	3482	100
4.8824-5.369	0.2126	173	0.1512	3301	3474	100
5.369-6.1352	0.2286	183	0.1745	3321	3504	100
6.1352-7.6897	0.2288	159	0.1838	3337	3496	100
7.6897-24.4642	0.2054	158	0.1551	2972	3130	89

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	0.0599	0.0144	-0.1771	0.6632	0.1064	0.4054	-0.0474	0.0407	0.0551	-0.2962	-0.0794	-0.0903	-0.2449	0.1197	-0.0271	0.2098	-0.0312	-0.0051	0.323	0.0389	0.353	36.92	16.0098	-5.6221
2	0.4438	-0.3347	0.1707	0.1856	-0.0835	0.0944	-0.2031	-0.003	0.4802	-0.1408	0.2343	0.2221	0.044	-0.0192	0.0002	0.5321	0.0013	-0.038	0.4385	0.1258	0.5352	33.6931	26.3471	-8.8989
3	0.8591	-0.5163	-0.5919	0.4758	0.0695	0.3427	0.0201	0.0245	0.098	-0.394	-0.0333	0.1524	-0.2308	0.0032	0.0051	0.4316	0.0122	-0.1389	0.2215	0.0208	0.3521	15.8634	26.2981	-9.0286
4	0.8408	-0.3727	0.0409	0.9486	0.2252	0.4745	0.0536	-0.169	-0.1489	-0.0559	0.0384	0.206	0.0423	-0.0234	0.0238	0.1366	-0.0164	0.0124	0.3533	0.0663	0.3953	12.0632	-1.8898	14.5498
5	0.4319	0.7078	-0.3419	0.759	0.087	1.0812	-0.195	-0.2625	0.0952	0.4711	0.0755	0.5099	-0.4301	0.0458	-0.1847	-0.1643	0.1452	0.0608	0.3063	-0.0672	0.5542	4.8583	17.1859	17.3954
6	0.3288	-0.2651	-0.0209	0.0073	0.2264	0.8983	-0.0865	0.0819	-0.0929	-0.4199	0.0511	-0.0113	0.0697	-0.0262	0.0032	0.2932	0.0498	0.0449	0.292	0.045	0.215	38.5223	-10.0572	-12.9801
7	0.1471	-0.0843	0.1064	0.632	-0.3341	0.8598	0.028	0.0674	0.0314	-0.3377	-0.0794	-0.086	0.2628	0.1711	0.0006	0.248	0.0963	0.0865	0.4147	0.0448	0.3273	55.733	-20.6605	-4.226
8	0.6712	0.0447	0.0694	1.0169	-0.314	0.6693	-0.0651	-0.108	0.0669	0.1242	0.0522	0.0412	0.0699	-0.0299	-0.0001	0.183	0.0025	0.0528	0.2969	0.022	0.2478	36.5651	-8.1248	25.9672
9	0.237	-0.0815	0.2576	-0.1025	-0.3888	0.3769	-0.0385	-0.0724	0.0282	0.0681	-0.027	-0.0905	0.1883	0.1184	0	0.3256	0.0776	0.0141	0.3216	0.0479	0.3043	45.3688	-27.526	19.9173
10	0.0324	-0.0766	-0.054	0.0063	0.0277	0.022	0.0318	-0.2269	-0.0434	0.2318	-0.1397	0.2135	0.0436	0.1721	0.0001	0.8671	-0.0321	0.0341	0.4394	0.0118	0.4126	-8.8892	59.9159	56.8288
11	0.0096	0.0641	-0.0046	0.0628	-0.0215	0.0154	-0.0288	-0.0265	-0.1799	0.2132	-0.4041	-0.0004	0.0835	0.2623	-0.0007	0.4668	0.0108	-0.0516	0.3552	0.0337	0.4521	-2.7332	53.4898	43.9348
12	-0.0039	-0.0132	-0.0321	0.012	-0.0202	-0.0077	-0.0565	-0.341	0.0308	-0.334	-0.1901	0.1258	-0.0147	0.0207	-0	0.5102	0.0125	0.0057	0.6205	-0.0526	0.5623	1.6504	54.9866	21.897
13	0.0293	-0.0039	-0.0204	-0.0082	-0.0284	0.031	0.0688	-0.0862	-0.0988	0.0815	0.0047	-0.3653	-0.0653	0.2747	0.0002	0.5045	-0.0465	-0.0594	0.4294	0.0946	0.5073	2.5138	46.9513	39.0873
14	0.1426	0.0241	-0.07	0.1285	-0.0148	0.0223	-0.0203	-0.3486	-0.4327	0.1651	-0.0988	-0.1078	-0.07	0.0464	-0.0004	0.6336	0.0778	-0.0798	0.4196	0.0613	0.6009	2.6971	40.3746	47.1416
15	0.59	0.2336	-0.1669	0.5176	0.3804	0.2846	-0.0339	-0.0548	-0.226	0.1399	0.0879	-0.1037	0.1284	-0.0013	0.0001	0.6541	-0.0005	-0.0482	0.3328	0.0389	0.4436	-8.6198	43.2327	44.9129
16	0.1384	-0.0949	0.2919	0.1312	0.0567	0.2064	-0.0699	-0.3248	-0.0084	0.0966	-0.056	0.0988	-0.3271	-0.1464	0	0.5894	-0.0853	0.0642	0.4449	-0.0618	0.4233	-20.5564	53.7108	42.5839
17	0.3189	-0.181	-0.6107	0.2552	0.2744	1.1243	0.2096	0.0631	-0.2476	0.0128	0.0551	-0.2693	-0.1807	-0.5684	0.0806	0.1226	-0.3385	-0.2824	0.3761	0.0653	0.847	-31.4811	30.382	32.0551
18	0.0007	0.0497	0.0389	0.1677	0.1541	0.0874	0.115	0.0764	-0.1022	0.1901	-0.0537	0.0675	0.3162	-0.1395	-0.0001	0.5849	-0.0585	-0.0367	0.4442	-0.0438	0.6375	-26.7696	38.9885	35.3319
19	0.0294	0.2107	-0.1373	0.089	-0.2074	0.091	-0.0104	0.2006	-0.0747	0.2781	-0.13	-0.0925	0.2234	-0.2542	0	0.6617	-0.1051	0.0467	0.4428	0.0269	0.5699	-21.2219	34.0832	45.3074
20	0.6963	0.7314	-0.0733	0.2088	-0.5393	0.5069	-0.1205	0.1574	0.1014	-0.021	0.04	0.1895	-0.3558	0.1577	-0	0.6444	0.0772	-0.0739	0.4277	-0.0306	0.4111	-17.5182	69.4126	17.0083
21	0.4789	0.2014	0.0779	0.3736	0.2738	0.1491	-0.0827	-0.0412	0.0944	-0.1904	-0.0277	0.1879	-0.1114	-0.0399	0	0.5503	0.0461	-0.1299	0.4004	-0.0395	0.3752	-24.1048	63.8087	11.8539
22	0.3655	0.7247	-0.0994	0.1014	-0.008	0.7539	0.0255	0.1241	-0.1687	-0.021	-0.0254	-0.0168	-0.1901	-0.1614	0.0002	0.3677	0.0281	-0.0914	0.3811	-0.0962	0.5236	-26.7072	45.7298	14.0701
23	0.3791	0.179	0.2004	0.2352	0.3574	0.4171	0.1297	-0.0471	0.0322	-0.1008	-0.0485	0.0827	-0.0255	-0.0305	0.0001	0.5589	-0.0615	0.0409	0.3156	-0.0105	0.3031	-3.2134	74.9298	48.8165
24	0.3795	0.1639	-0.1031	0.4588	-0.3563	0.6714	0.1407	-0.2003	0.0336	0.1196	-0.1196	-0.0172	-0.1589	0.1536	-0	0.5468	-0.0689	-0.0027	0.3702	-0.0175	0.2845	15.179	84.1765	49.477
25	0.1268	0.0754	-0.4582	0.0373	-0.1584	0.6278	0.032	0.1145	-0.0463	-0.274	0.072	-0.0998	0.0127	-0.0526	0.2263	0.7453	-0.0472	-0.0062	0.3323	-0.0242	0.1939	7.5578	73.9995	13.1442
26	0.5671	0.4001	-0.0133	0.3506	-0.3503	0.3851	-0.0276	0.1565	0.0116	-0.2759	0.0829	-0.0254	-0.0306	0.1709	0	0.695	-0.0812	0.0927	0.384	-0.0231	0.3749	14.7666	93.2298	21.3753

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 122 )	A	9 - 122
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 123 through 155 )	A	123 - 155
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 156 through 335 )	A	156 - 335
4	X-RAY DIFFRACTION	4	chain 'B' and (resid 9 through 131 )	B	9 - 131
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 132 through 335 )	B	132 - 335
6	X-RAY DIFFRACTION	6	chain 'C' and (resid 9 through 179 )	C	9 - 179
7	X-RAY DIFFRACTION	7	chain 'C' and (resid 180 through 335 )	C	180 - 335
8	X-RAY DIFFRACTION	8	chain 'D' and (resid 9 through 179 )	D	9 - 179
9	X-RAY DIFFRACTION	9	chain 'D' and (resid 180 through 335 )	D	180 - 335
10	X-RAY DIFFRACTION	10	chain 'E' and (resid 9 through 28 )	E	9 - 28
11	X-RAY DIFFRACTION	11	chain 'E' and (resid 29 through 48 )	E	29 - 48
12	X-RAY DIFFRACTION	12	chain 'E' and (resid 49 through 72 )	E	49 - 72
13	X-RAY DIFFRACTION	13	chain 'E' and (resid 73 through 88 )	E	73 - 88
14	X-RAY DIFFRACTION	14	chain 'E' and (resid 89 through 118 )	E	89 - 118
15	X-RAY DIFFRACTION	15	chain 'E' and (resid 119 through 179 )	E	119 - 179
16	X-RAY DIFFRACTION	16	chain 'E' and (resid 180 through 212 )	E	180 - 212
17	X-RAY DIFFRACTION	17	chain 'E' and (resid 213 through 231 )	E	213 - 231
18	X-RAY DIFFRACTION	18	chain 'E' and (resid 232 through 274 )	E	232 - 274
19	X-RAY DIFFRACTION	19	chain 'E' and (resid 275 through 335 )	E	275 - 335
20	X-RAY DIFFRACTION	20	chain 'F' and (resid 9 through 106 )	F	9 - 106
21	X-RAY DIFFRACTION	21	chain 'F' and (resid 107 through 179 )	F	107 - 179
22	X-RAY DIFFRACTION	22	chain 'F' and (resid 180 through 335 )	F	180 - 335
23	X-RAY DIFFRACTION	23	chain 'G' and (resid 9 through 131 )	G	9 - 131
24	X-RAY DIFFRACTION	24	chain 'G' and (resid 132 through 335 )	G	132 - 335
25	X-RAY DIFFRACTION	25	chain 'H' and (resid 9 through 179 )	H	9 - 179
26	X-RAY DIFFRACTION	26	chain 'H' and (resid 180 through 335 )	H	180 - 335

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