PDB-5q01: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosph...

ID or keywords:

Entry

Database: PDB / ID: 5q01

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-[4-(4,5-dichloro-2-methylpyrazol-3-yl)oxyphenyl]sulfonylurea

Components

Fructose-1,6-bisphosphatase 1

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 / cellular response to magnesium ion / Gluconeogenesis / negative regulation of Ras protein signal transduction / fructose 6-phosphate metabolic process ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.603 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-[4-(4,5-dichloro-2- ...
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	5q01.cif.gz	961.3 KB	Display	PDBx/mmCIF format
PDB format	pdb5q01.ent.gz	804.1 KB	Display	PDB format
PDBx/mmJSON format	5q01.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	5q01_validation.pdf.gz	2.5 MB	Display	wwPDB validaton report
Full document	5q01_full_validation.pdf.gz	2.5 MB	Display
Data in XML	5q01_validation.xml.gz	91.2 KB	Display
Data in CIF	5q01_validation.cif.gz	123.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/q0/5q01 ftp://data.pdbj.org/pub/pdb/validation_reports/q0/5q01	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	5pzz-1 2fix-d 6lw2-d 5pzx-1 5q09-2 5pzx-2 1fta-d 5q07-1 4fbp-d 4mjo-2 1fpi-1 2wbd-2 3kbz-d 5q08-2 5pzu-d 5q0a-d 5pzv-d 5q0c-1 5q06-d 5pzr-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
150 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
150 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 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 / 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) / Strain (production host): E References: UniProt: Q2TU34, UniProt: P09467*PLUS, fructose-bisphosphatase
#2: Chemical	ChemComp-95G / N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-4-[(3,4-dichloro-1-methyl-1H-pyrazol-5-yl)oxy]benzene-1-sulfonamide Mass: 527.200 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₁₄H₁₀BrCl₂N₅O₄S₂
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 383 / 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 27, 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: 2.603→30.406 Å / Num. obs: 76273 / % possible obs: 78.85 %

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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: 2.603→30.406 Å / SU ML: 0.42 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 31.99 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2669	3777	4.95 %
R_work	0.1867	72496	-
obs	0.1908	76273	78.85 %

Solvent computation

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

Displacement parameters

B_iso max: 154.77 Å² / B_iso mean: 50.1744 Å² / B_iso min: 8.52 Å²

Refinement step

Cycle: final / Resolution: 2.603→30.406 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19440	0	224	383	20047
B_iso mean	-	-	51.48	38.07	-
Num. residues	-	-	-	-	2540

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	20057
X-RAY DIFFRACTION	f_angle_d	1.085	27113
X-RAY DIFFRACTION	f_chiral_restr	0.064	3054
X-RAY DIFFRACTION	f_plane_restr	0.007	3458
X-RAY DIFFRACTION	f_dihedral_angle_d	10.39	12145

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	12203	X-RAY DIFFRACTION	9.506	TORSIONAL
1	2	B	12203	X-RAY DIFFRACTION	9.506	TORSIONAL
1	3	C	12203	X-RAY DIFFRACTION	9.506	TORSIONAL
1	4	D	12203	X-RAY DIFFRACTION	9.506	TORSIONAL
1	5	E	12203	X-RAY DIFFRACTION	9.506	TORSIONAL
1	6	F	12203	X-RAY DIFFRACTION	9.506	TORSIONAL
1	7	G	12203	X-RAY DIFFRACTION	9.506	TORSIONAL
1	8	H	12203	X-RAY DIFFRACTION	9.506	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 27

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.603-2.636	0.3334	33	0.2215	659	692	19
2.636-2.6706	0.3261	78	0.2211	1561	1639	46
2.6706-2.7072	0.3434	113	0.2283	2323	2436	68
2.7072-2.7459	0.2984	143	0.2404	2749	2892	82
2.7459-2.7868	0.3467	161	0.2381	2884	3045	84
2.7868-2.8303	0.3471	125	0.2464	2878	3003	86
2.8303-2.8767	0.3876	160	0.227	2990	3150	87
2.8767-2.9263	0.337	175	0.2303	2883	3058	86
2.9263-2.9794	0.3414	149	0.2085	2921	3070	86
2.9794-3.0367	0.3183	169	0.205	2938	3107	86
3.0367-3.0986	0.3184	144	0.2002	2895	3039	85
3.0986-3.1659	0.3105	142	0.2079	2927	3069	85
3.1659-3.2395	0.2904	126	0.2069	2876	3002	85
3.2395-3.3204	0.2798	154	0.2001	2968	3122	85
3.3204-3.4101	0.2781	133	0.1934	2797	2930	84
3.4101-3.5103	0.3048	166	0.1889	2898	3064	84
3.5103-3.6234	0.2674	131	0.1861	2835	2966	84
3.6234-3.7527	0.2788	172	0.1865	2827	2999	83
3.7527-3.9026	0.2472	159	0.184	2802	2961	82
3.9026-4.0799	0.2562	147	0.164	2783	2930	83
4.0799-4.2944	0.1961	149	0.1559	2780	2929	82
4.2944-4.5626	0.2076	168	0.1486	2795	2963	82
4.5626-4.9136	0.216	130	0.1437	2781	2911	81
4.9136-5.4055	0.2359	133	0.1625	2719	2852	80
5.4055-6.182	0.2519	127	0.1878	2769	2896	80
6.182-7.7672	0.2585	153	0.2091	2675	2828	79
7.7672-30.4086	0.2282	137	0.1789	2583	2720	75

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	0.0616	0.0115	-0.0334	0.032	0.0257	0.0351	-0.0279	-0.0531	0.0782	-0.1039	-0.0893	-0.1132	-0.0406	0.0804	-0.0006	0.3331	-0.0526	-0.0259	0.2234	0.0521	0.2496	37.1462	16.4092	-5.8123
2	-0.0002	-0.0069	-0.0086	0.0418	0.0319	0.0165	-0.0329	0.039	0.1502	0.0527	0.0459	0.1246	-0.0702	0.065	0	0.4472	-0.0115	-0.0167	0.2725	0.0514	0.3249	30.0948	23.5426	-9.3079
3	0.0552	-0.0727	0.0066	0.1197	-0.0926	0.0513	-0.0475	0.1004	0.1058	-0.0975	-0.106	0.0546	-0.0586	-0.0189	-0.2368	0.2455	0.1514	-0.2049	-0.2081	0.1541	0.0953	11.7423	25.326	-5.9467
4	-0.0004	-0.0015	0.0037	0.0262	-0.0164	0.0088	0.083	-0.0974	0.0891	-0.017	0.0529	0.0552	-0.0708	-0.0572	0	0.4923	0.0253	-0.0914	0.2246	0.0379	0.3631	18.3943	33.4536	-12.8055
5	0.0014	-0.0012	0.0017	0.0081	-0.0018	0.0126	-0.0185	-0.0094	-0.0856	0.0076	0.0113	-0.0204	-0.0195	0.0175	0.0011	0.0974	0.02	0.0676	0.3375	0.0308	0.2297	21.3489	0.6456	31.0764
6	0.0052	-0.0003	0.0055	0.1178	0.0001	0.0016	-0.03	0.0392	-0.0676	-0.1518	0.0583	0.034	0.046	0.0251	-0.0076	0.1211	0.0027	0.0209	0.2074	0.0053	0.2231	15.1092	-3.5355	8.6131
7	0.0092	-0.0115	-0.0028	0.0107	0.0081	0.0032	0.1243	0.0391	-0.0904	-0.0911	0.0131	0.0043	0.0014	-0.067	0	0.272	0.048	0.0101	0.3209	0.032	0.455	4.2917	-1.8165	13.3051
8	0.0189	0.014	-0.0258	0.0133	-0.0048	0.0306	-0.0993	-0.0886	-0.0193	0.0912	-0.038	0.0536	0.043	-0.0859	-0.0821	-0.0841	0.1729	0.0467	0.058	-0.0772	0.3309	3.0068	2.5645	21.7477
9	0.0198	-0.021	-0.0187	0.044	0.0349	0.0262	0.0105	-0.0992	0.1015	0.0258	-0.0458	0.0494	-0.1008	-0.0906	-0.0384	0.0382	0.1312	-0.0014	0.1834	-0.0563	0.1701	17.7277	14.6899	19.7928
10	0.0348	0.0185	-0.0249	0.0116	-0.0115	0.0322	0.1287	-0.0313	-0.0257	0.0383	0.0934	0.1079	-0.0863	0.0326	0.0012	0.3009	0.092	0.0243	0.2315	0.0181	0.4993	2.4821	33.1344	9.5249
11	0.0432	-0.0148	-0.0273	0.0341	-0.0104	0.0202	-0.0208	-0.0838	0.0133	-0.0211	0.0125	0.004	-0.0069	-0.0816	0.0086	-0.0048	0.0976	-0.0421	0.2374	0.0178	0.4404	3.5858	17.3233	14.9926
12	0.0018	-0.0047	0.0019	0.0094	0.0299	0.0863	0.0945	0.0655	-0.0824	0.0216	0.0764	0.0067	-0.0512	-0.0009	0.0167	0.189	0.1778	0.0679	0.462	0.0219	0.5068	-3.0064	21.8249	20.1932
13	0.0525	-0.0382	-0.0227	0.0805	-0.0063	0.0806	-0.0129	0.0108	-0.0057	-0.1787	-0.035	0.0124	0.0602	0.0196	-0	0.2289	0.0392	0.0303	0.2236	-0.0019	0.192	39.3176	-9.3402	-11.8567
14	0.0867	0.0027	0.0279	0.1673	-0.0599	0.0287	-0.1195	0.1397	-0.0534	-0.19	0.0167	-0.087	0.1328	0.0389	-0.0448	0.1437	0.1182	0.0865	0.3067	0.0464	0.2876	57.4095	-24.2965	-4.4411
15	0.1033	-0.0516	0.061	0.125	0.005	0.0456	-0.0506	-0.081	0.0587	0.1084	0.0482	0.0848	0.0068	0.0245	-0.0025	0.0855	0.0082	0.0428	0.2172	-0.0048	0.1631	35.658	-9.1308	24.8168
16	0.011	0.0156	-0.0131	0.0128	-0.0227	0.0082	0.002	-0.1012	0.0369	0.0108	-0.0064	-0.0844	0.0002	0.0016	0	0.1471	0.029	-0.0152	0.221	0.0201	0.2331	48.1737	-30.4029	20.6613
17	0.0498	0.0001	-0.0307	0.0756	0.0365	0.0441	-0.0085	-0.0096	-0.1182	0.1187	0.0338	0.0729	-0.0255	0.1307	0.0018	0.3683	-0.0175	-0.004	0.1802	0.0539	0.2653	-3.6728	49.1391	44.2133
18	-0.0239	0.0281	-0.0272	-0.0022	-0.009	0.0958	-0.016	-0.1274	-0.1439	0.0333	0.0155	-0.1135	-0.0593	-0.0492	-0.0183	0.1632	-0.2166	0.05	-0.0708	-0.0176	0.199	-23.9829	40.7212	40.7356
19	0.0517	0.0572	0.0302	0.0316	0.0222	0.0141	0.0787	0.1076	-0.0663	-0.1206	-0.0367	0.0414	-0.1317	0.0472	0	0.3706	0.0842	-0.0471	0.3479	-0.0133	0.2505	-18.4685	72.4189	16.1151
20	0.0949	0.0579	-0.0139	0.0343	0.0018	0.0054	0.0441	-0.0175	-0.1408	-0.0228	-0.1093	0.0049	-0.0723	-0.0878	-0.0073	0.3065	0.0451	-0.065	0.2991	-0.0498	0.2362	-19.7465	63.0776	13.548
21	0.0035	0.0002	0.0014	-0.0038	0.008	0.0185	-0.0593	-0.0071	-0.0721	-0.0205	-0.0573	-0.0315	0.0139	-0.0823	0	0.3325	-0.1032	-0.0433	0.4054	-0.1753	0.6035	-27.9804	38.0814	18.5151
22	0.0188	0.01	-0.0151	0.0123	-0.0004	0.0265	-0.0546	0.0937	-0.0264	0.0485	-0.0675	-0.0169	-0.0076	-0.14	-0.0681	0.247	0.0177	-0.1108	0.3346	-0.2997	0.3749	-30.5634	49.8959	11.882
23	0.014	-0.0355	-0.0212	0.0472	0.0415	0.0429	0.0652	-0.1146	-0.0156	0.0964	-0.1089	0.1055	0.0084	0.0335	0	0.3693	-0.0237	0.0058	0.2521	-0.003	0.273	-3.5769	76.422	50.459
24	0.0457	0.0362	-0.0021	0.0259	-0.0336	0.0606	0.0973	-0.0274	0.0186	0.1592	-0.0771	0.0262	-0.0073	0.0726	-0	0.2709	-0.0233	-0.0041	0.2611	0.019	0.2103	14.7736	87.457	48.8052
25	0.1335	0.1094	-0.0449	0.0688	-0.026	0.0266	0.0114	0.1869	0.0058	-0.1209	0.0438	0.0372	0.1836	-0.0664	0.0018	0.4066	0.0454	-0.0169	0.3039	-0.0196	0.1676	6.3473	77.3917	14.0843
26	0.0142	0.0092	-0.013	0.0005	-0.0134	0.02	0.0535	0.0544	0.0523	0.0566	-0.0215	0.0143	-0.023	0.118	-0	0.3374	-0.043	0.0454	0.2492	0.0197	0.2566	17.3465	102.8989	28.9202
27	0.0224	0.0003	0.0261	0.0065	-0.0098	0.0257	-0.1249	0.143	0.0711	-0.0543	0.0586	0.0547	0.0019	0.0686	0	0.3922	-0.0052	0.0328	0.3471	0.0386	0.2767	17.6883	96.0236	17.1507

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 118 )	A	9 - 118
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 119 through 179 )	A	119 - 179
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 180 through 274 )	A	180 - 274
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 275 through 335 )	A	275 - 335
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 9 through 28 )	B	9 - 28
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 29 through 88 )	B	29 - 88
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 89 through 131 )	B	89 - 131
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 132 through 170 )	B	132 - 170
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 171 through 212 )	B	171 - 212
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 213 through 247 )	B	213 - 247
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 248 through 291 )	B	248 - 291
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 292 through 335 )	B	292 - 335
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 9 through 198 )	C	9 - 198
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 199 through 335 )	C	199 - 335
15	X-RAY DIFFRACTION	15	chain 'D' and (resid 9 through 198 )	D	9 - 198
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 199 through 335 )	D	199 - 335
17	X-RAY DIFFRACTION	17	chain 'E' and (resid 9 through 179 )	E	9 - 179
18	X-RAY DIFFRACTION	18	chain 'E' and (resid 180 through 335 )	E	180 - 335
19	X-RAY DIFFRACTION	19	chain 'F' and (resid 9 through 118 )	F	9 - 118
20	X-RAY DIFFRACTION	20	chain 'F' and (resid 119 through 198 )	F	119 - 198
21	X-RAY DIFFRACTION	21	chain 'F' and (resid 199 through 247 )	F	199 - 247
22	X-RAY DIFFRACTION	22	chain 'F' and (resid 248 through 335 )	F	248 - 335
23	X-RAY DIFFRACTION	23	chain 'G' and (resid 9 through 118 )	G	9 - 118
24	X-RAY DIFFRACTION	24	chain 'G' and (resid 119 through 335 )	G	119 - 335
25	X-RAY DIFFRACTION	25	chain 'H' and (resid 9 through 198 )	H	9 - 198
26	X-RAY DIFFRACTION	26	chain 'H' and (resid 199 through 247 )	H	199 - 247
27	X-RAY DIFFRACTION	27	chain 'H' and (resid 248 through 335 )	H	248 - 335

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