PDB-5q07: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosph...

ID or keywords:

Entry

Database: PDB / ID: 5q07

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-(4-bromo-6-morpholin-4-ylpyridin-2-yl)-3-[5-(2-methoxyethyl)-4-methylthiophen-2-yl]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: 2.424 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-(4-bromo-6-morpholin-4-ylpyridin-2-yl)-3-[5-(2- ...
Authors: Ruf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G.

History

Deposition	Apr 16, 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	5q07.cif.gz	968.6 KB	Display	PDBx/mmCIF format
PDB format	pdb5q07.ent.gz	809.4 KB	Display	PDB format
PDBx/mmJSON format	5q07.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/q0/5q07 ftp://data.pdbj.org/pub/pdb/validation_reports/q0/5q07	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	5pzu-d 5pzw-d 4mjo-2 2wbb-1 5pzx-2 2wbd-2 5pzz-1 5q00-1 2vt5-1 5q09-2 1fta-d 5q04-2 6lw2-d 4mjo-1 5q0b-d 5pzx-1 1fpe-1 5q06-d 5q0a-d 5pzv-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)	66.190, 284.507, 83.226
Angle α, β, γ (deg.)	90.000, 97.660, 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) / Strain (production host): E References: UniProt: Q2TU34, UniProt: P09467*PLUS, fructose-bisphosphatase
#2: Chemical	ChemComp-95Y / N-{[4-bromo-6-(morpholin-4-yl)pyridin-2-yl]carbamoyl}-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide Mass: 519.433 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₁₈H₂₃BrN₄O₅S₂
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 697 / 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: 2.72 Å³/Da / Density % sol: 54.79 %
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: Nov 1, 2006
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.987 Å / Relative weight: 1
Reflection	Resolution: 2.424→29.87 Å / Num. obs: 113819 / % possible obs: 99.06 %

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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: 2.424→29.87 Å / SU ML: 0.4 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 28.72 / Stereochemistry target values: ML
Details: INHIBITOR MORPHOLINE GROUP MAY HAVE MULTIPLE CONFORMATIONS

	R_factor	Num. reflection	% reflection
R_free	0.2634	5702	5.01 %
R_work	0.2001	108117	-
obs	0.2033	113819	99.06 %

Solvent computation

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

Displacement parameters

B_iso max: 142.98 Å² / B_iso mean: 43.5172 Å² / B_iso min: 8.01 Å²

Refinement step

Cycle: final / Resolution: 2.424→29.87 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19440	0	240	697	20377
B_iso mean	-	-	57.69	39.2	-
Num. residues	-	-	-	-	2540

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	20073
X-RAY DIFFRACTION	f_angle_d	1.043	27121
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	11.66	12209

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	12192	X-RAY DIFFRACTION	9.957	TORSIONAL
1	2	B	12192	X-RAY DIFFRACTION	9.957	TORSIONAL
1	3	C	12192	X-RAY DIFFRACTION	9.957	TORSIONAL
1	4	D	12192	X-RAY DIFFRACTION	9.957	TORSIONAL
1	5	E	12192	X-RAY DIFFRACTION	9.957	TORSIONAL
1	6	F	12192	X-RAY DIFFRACTION	9.957	TORSIONAL
1	7	G	12192	X-RAY DIFFRACTION	9.957	TORSIONAL
1	8	H	12192	X-RAY DIFFRACTION	9.957	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 (%)
2.4238-2.4514	0.3154	149	0.247	2851	3000	77
2.4514-2.4802	0.3458	194	0.2611	3550	3744	100
2.4802-2.5104	0.3528	201	0.2667	3653	3854	100
2.5104-2.5422	0.381	198	0.2687	3640	3838	100
2.5422-2.5756	0.3217	202	0.264	3559	3761	100
2.5756-2.6109	0.3109	185	0.2461	3669	3854	100
2.6109-2.6482	0.3116	188	0.2466	3622	3810	100
2.6482-2.6877	0.3386	178	0.2484	3675	3853	100
2.6877-2.7296	0.3647	190	0.254	3556	3746	100
2.7296-2.7744	0.302	181	0.2462	3719	3900	100
2.7744-2.8222	0.3244	181	0.2404	3585	3766	100
2.8222-2.8734	0.3351	213	0.2409	3657	3870	100
2.8734-2.9287	0.3053	206	0.2375	3567	3773	100
2.9287-2.9884	0.3318	199	0.2319	3656	3855	100
2.9884-3.0533	0.2766	185	0.2185	3637	3822	100
3.0533-3.1243	0.2786	167	0.2205	3651	3818	100
3.1243-3.2023	0.3068	190	0.2076	3634	3824	100
3.2023-3.2888	0.2704	168	0.2085	3628	3796	100
3.2888-3.3854	0.2563	192	0.2091	3612	3804	100
3.3854-3.4945	0.2828	189	0.2001	3675	3864	100
3.4945-3.6192	0.2288	180	0.1818	3628	3808	100
3.6192-3.7639	0.2536	218	0.1817	3594	3812	100
3.7639-3.9348	0.2334	200	0.1854	3634	3834	100
3.9348-4.1418	0.2511	192	0.1877	3653	3845	100
4.1418-4.4005	0.2543	190	0.1801	3616	3806	100
4.4005-4.739	0.2145	207	0.1613	3624	3831	100
4.739-5.2137	0.2162	184	0.1644	3623	3807	100
5.2137-5.9629	0.225	167	0.1772	3670	3837	100
5.9629-7.493	0.2467	210	0.177	3634	3844	100
7.493-29.8725	0.1734	198	0.1573	3645	3843	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	0.0386	-0.002	-0.0051	0.0458	0.0204	0.0349	-0.1478	-0.0203	0.0121	-0.1417	0.0405	-0.0254	0.0722	0.0291	-0.0085	0.1553	-0.0137	0.02	0.1394	0.0185	0.14	37.4552	16.1246	-5.5208
2	0.0321	-0.0386	-0.0273	0.0553	-0.0139	0.087	-0.2152	-0.0025	0.1264	-0.1575	0.0777	0.1794	-0.0602	0.1016	-0.1193	0.177	0.0541	-0.0856	0.1153	0.0443	0.261	19.8682	22.8594	-7.9514
3	0.0067	-0.0128	0.017	0.0124	-0.014	0.0091	-0.0687	0.0697	0.0957	-0.004	0.0603	0.0133	-0.0299	-0.0707	0	0.3618	0.0057	-0.098	0.1591	0.0208	0.2611	18.1508	31.2867	-10.3549
4	0.0518	0.0101	-0.002	0.0868	-0.0056	0.0378	-0.0072	-0.0891	-0.0988	0.008	-0.0632	0.0729	0.0958	0.0346	-0.0159	0.0705	0.0242	0.0369	0.1477	0.0399	0.1991	17.2897	-2.1451	15.2124
5	0.0503	-0.0284	-0.0095	0.066	0.0334	0.0305	-0.0532	0.052	-0.0382	-0.0402	-0.0288	0.0907	0.002	-0.0131	-0.0534	0.0688	-0.0268	0.1438	0.1748	0.0155	0.4094	3.0077	-4.8217	16.5202
6	0.0333	0.0022	0.0194	0.0149	0.0082	0.0119	-0.039	0.0292	0.0235	-0.0953	-0.1047	0.0592	0.0195	-0.0272	-0.0474	0.0968	0.1305	0.0526	0.279	-0.0806	0.2749	2.6962	2.0205	17.1878
7	0.065	-0.0433	-0.0448	0.0505	0.0435	0.0549	0.0562	-0.1584	-0.0185	0.0473	-0.0951	0.0479	-0.0584	0.0715	-0.003	0.1412	0.0423	0.0572	0.1879	-0.0359	0.1991	16.4989	12.8045	19.4927
8	0.0046	-0.0007	0.0002	-0.0014	0.0026	0.0011	-0.0383	-0.0017	0.0004	0.0655	-0.0309	0.0123	-0.0668	-0.0206	-0	0.2413	0.0728	-0.0037	0.2578	-0.0208	0.4852	-1.4147	31.295	8.6693
9	0.01	-0.007	0.0053	0.0074	-0.0129	0.06	-0.0069	-0.0236	0.0235	-0.0343	0.0047	0.096	-0.1756	0.0463	-0.0062	0.1741	0.1081	-0.0148	0.1879	-0.0464	0.3026	6.1362	24.8571	11.5026
10	0.0393	-0.0154	-0.0293	0.0476	-0.0246	0.0959	0.067	-0.0343	-0.0676	-0.0249	0.1196	0.1237	-0.1634	0.0284	0.0835	-0.2495	0.2414	0.1386	0.208	-0.115	0.293	-0.5811	18.4112	19.85
11	0.0162	-0.0628	-0.0522	0.2083	0.0744	0.0764	-0.0835	0.05	0.0307	-0.391	0.0079	0.1799	-0.0678	0.0747	0.0183	0.0431	0.127	0.0816	0.135	-0.0012	0.0486	38.9809	-10.0558	-13.0873
12	0.0533	-0.0448	-0.006	0.2224	0.0281	0.0295	0.0465	0.0343	-0.0182	-0.1679	-0.0387	0.0166	0.0874	0.1208	0.0189	0.1755	0.0587	0.0321	0.2073	0.0226	0.1695	56.1699	-20.6313	-4.2922
13	0.0324	-0.0012	-0.008	0.028	-0.0064	0.0092	0.0384	-0.0348	0.0499	0.1255	-0.0201	0.0523	0.0326	-0.004	0.0283	-0.1517	0.0469	0.1557	0.1697	0.0288	0.0899	35.7959	-4.8593	25.068
14	0.1428	-0.005	-0.0398	0.1403	-0.0047	0.0626	-0.0017	-0.0304	0.0786	0.0746	0.0169	-0.075	0.1337	0.053	0.0236	0.1667	0.0353	0.0168	0.1561	0.0442	0.1079	41.8685	-21.937	19.6719
15	0.0109	-0.0268	-0.0132	0.0017	-0.0039	0.0141	0.0112	-0.084	-0.0061	0.0134	0.0205	0.0668	0.0673	0.0348	-0	0.1761	0.0664	-0.0046	0.1923	0.0296	0.183	47.4417	-26.9583	24.6263
16	-0.003	-0.0021	-0.0054	-0.0009	0.0014	0.0078	0.0756	-0.039	-0.1213	0.1443	0.0296	-0.0141	-0.0624	0.0702	0	0.3436	-0.019	-0.041	0.1747	0.0176	0.2248	-5.3872	56.7501	50.6612
17	-0.0026	0.0095	0.0015	0.0127	0.007	0.0059	0.0954	-0.0597	-0.0727	-0.0142	0.119	-0.103	-0.0305	0.0414	0.0002	0.2177	-0.0125	-0.1011	0.174	0.0002	0.246	2.5032	51.017	30.7198
18	0.0663	-0.0005	-0.0479	0.0075	-0.0009	0.0408	-0.0871	-0.0055	-0.0705	-0.0313	-0.0185	0.0046	0.0267	0.0136	-0.0299	0.3491	0.0287	-0.1471	0.1898	0.0778	0.3384	2.1157	40.7108	45.6999
19	0.0185	-0.009	-0.0075	0.0065	0.0055	0.0036	0.0236	-0.0519	-0.1515	0.0847	-0.0792	0.0096	0.0649	-0.0264	-0.0002	0.2918	-0.0223	-0.0725	0.2043	0.0668	0.2622	-8.0938	43.2856	45.6248
20	0.0018	0.0133	0.0031	0.0053	0.0047	0.0038	0.0375	-0.0904	-0.1621	0.0078	0.079	0.0134	-0.0772	-0.0802	0.0003	0.2136	-0.0687	-0.0024	0.2491	0.0354	0.3811	-24.2786	44.8931	38.8181
21	0.0031	-0.0042	-0.0029	0.0149	0.0073	0.0008	0.0079	0.0165	0.0073	0.0374	0.0171	-0.0644	-0.0088	-0.0414	0	0.2232	-0.0237	0.0275	0.3536	-0.0054	0.5962	-34.7037	40.9581	33.2039
22	0.0112	0.006	0.0059	-0.0013	-0.0006	0.0002	0.0157	-0.0359	-0.0585	0.0756	-0.1005	0.0239	0.0243	0	-0	0.3221	-0.0251	-0.0672	0.1961	0.0303	0.3839	-18.8316	38.53	40.3302
23	0.003	-0.0021	-0.0022	0.0096	-0.0075	-0.0094	0.0273	-0.065	-0.0681	-0.0321	0.018	-0.0212	0.0532	-0.1299	-0	0.2703	-0.1122	-0.0141	0.2372	0.0507	0.3691	-23.1152	31.7657	45.4742
24	0.0216	0.0287	0.0119	0.0361	0.0098	0.0038	0.0162	0.1465	0.029	-0.0294	-0.0865	0.0299	-0.2228	0.0073	-0.0002	0.2262	0.0636	-0.0214	0.2103	-0.0165	0.1589	-18.7362	69.641	16.3688
25	0.0866	0.01	-0.0645	0.0422	0.0055	0.0488	0.0072	0.1276	-0.1873	-0.1306	-0.0768	0.0565	-0.1328	-0.0785	-0.0046	0.2255	0.0161	-0.0877	0.2832	-0.0982	0.2983	-22.5477	51.2061	15.121
26	0.007	0.0197	0.0018	0.0089	-0.0121	0.0018	-0.0994	0.0495	-0.0197	0.0481	0.0996	0.0132	-0.0392	-0.1052	-0	0.2583	-0.0257	-0.0822	0.2987	-0.0703	0.2867	-30.1604	48.0893	11.709
27	0.106	0.0246	-0.0619	0.0084	0.0001	0.0318	0.1383	-0.052	0.0407	0.0732	-0.0643	-0.0334	0.1061	-0.1174	0.0042	0.2518	-0.0503	-0.0041	0.1827	-0.0122	0.1537	-3.5595	74.1591	50.1421
28	0.079	0.0237	-0.0718	-0.0072	-0.037	0.1018	0.1026	-0.0546	0.0053	0.107	-0.1158	0.0078	0.0054	0.0465	-0.0004	0.221	-0.0324	-0.0205	0.1806	-0.008	0.1458	14.7073	84.6335	48.8651
29	0.0599	-0.001	-0.0252	0.01	-0.0419	0.0321	0.0276	0.0863	-0.0713	-0.0036	0.0843	-0.0743	0.0734	0.0704	0.003	0.3377	0.0089	-0.0157	0.2577	-0.0011	0.1777	8.1502	72.6827	12.8708
30	0.037	0.047	0.0201	0.0385	-0.0558	0.0411	0.0514	0.0602	0.0465	-0.0669	0.0318	0.0012	0.0924	0.0413	0	0.2666	0.0112	0.0457	0.2036	-0.0059	0.1603	13.397	92.3031	20.7375

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 247 )	A	123 - 247
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 248 through 335 )	A	248 - 335
4	X-RAY DIFFRACTION	4	chain 'B' and (resid 9 through 88 )	B	9 - 88
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 89 through 122 )	B	89 - 122
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 123 through 155 )	B	123 - 155
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 156 through 212 )	B	156 - 212
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 213 through 231 )	B	213 - 231
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 232 through 274 )	B	232 - 274
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 275 through 335 )	B	275 - 335
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 9 through 179 )	C	9 - 179
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 180 through 335 )	C	180 - 335
13	X-RAY DIFFRACTION	13	chain 'D' and (resid 9 through 122 )	D	9 - 122
14	X-RAY DIFFRACTION	14	chain 'D' and (resid 123 through 247 )	D	123 - 247
15	X-RAY DIFFRACTION	15	chain 'D' and (resid 248 through 335 )	D	248 - 335
16	X-RAY DIFFRACTION	16	chain 'E' and (resid 9 through 48 )	E	9 - 48
17	X-RAY DIFFRACTION	17	chain 'E' and (resid 49 through 88 )	E	49 - 88
18	X-RAY DIFFRACTION	18	chain 'E' and (resid 89 through 122 )	E	89 - 122
19	X-RAY DIFFRACTION	19	chain 'E' and (resid 123 through 179 )	E	123 - 179
20	X-RAY DIFFRACTION	20	chain 'E' and (resid 180 through 231 )	E	180 - 231
21	X-RAY DIFFRACTION	21	chain 'E' and (resid 232 through 247 )	E	232 - 247
22	X-RAY DIFFRACTION	22	chain 'E' and (resid 248 through 291 )	E	248 - 291
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 292 through 335 )	E	292 - 335
24	X-RAY DIFFRACTION	24	chain 'F' and (resid 9 through 122 )	F	9 - 122
25	X-RAY DIFFRACTION	25	chain 'F' and (resid 123 through 247 )	F	123 - 247
26	X-RAY DIFFRACTION	26	chain 'F' and (resid 248 through 335 )	F	248 - 335
27	X-RAY DIFFRACTION	27	chain 'G' and (resid 9 through 122 )	G	9 - 122
28	X-RAY DIFFRACTION	28	chain 'G' and (resid 123 through 335 )	G	123 - 335
29	X-RAY DIFFRACTION	29	chain 'H' and (resid 9 through 155 )	H	9 - 155
30	X-RAY DIFFRACTION	30	chain 'H' and (resid 156 through 335 )	H	156 - 335

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