PDB-5q04: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosph...

ID or keywords:

Entry

Database: PDB / ID: 5q04

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-5-chlorothiophen-2-yl)sulfonyl-3-(5-bromo-1,3-thiazol-2-yl)urea

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: 2.502 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-5-chlorothiophen-2-yl)sulfonyl-3-(5-bromo-1,3-thiazol-2-yl)urea
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	5q04.cif.gz	965.5 KB	Display	PDBx/mmCIF format
PDB format	pdb5q04.ent.gz	808.4 KB	Display	PDB format
PDBx/mmJSON format	5q04.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/q0/5q04 ftp://data.pdbj.org/pub/pdb/validation_reports/q0/5q04	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 5pzr-d 5pzs-d 3kc0-d 2wbd-2 5pzv-d 5q0b-d 5q09-2 4fbp-d 2y5l-2 5pzx-2 5pzz-1 5pzx-1 2fix-d 5q01-1 5pzy-2 4mjo-1 5pzu-d 5q07-1 5q02-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)	66.281, 286.676, 83.272
Angle α, β, γ (deg.)	90.000, 97.680, 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-95P / 4-bromo-N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-5-chlorothiophene-2-sulfonamide Mass: 481.592 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₈H₄Br₂ClN₃O₃S₃
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 367 / 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: 2.75 Å³/Da / Density % sol: 55.22 %
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: 2.502→29.235 Å / Num. obs: 100143 / % possible obs: 94.92 %

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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: 2.502→29.235 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 27.36 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2511	5006	5 %
R_work	0.1857	95137	-
obs	0.189	100143	94.92 %

Solvent computation

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

Displacement parameters

B_iso max: 153.54 Å² / B_iso mean: 51.162 Å² / B_iso min: 13.39 Å²

Refinement step

Cycle: final / Resolution: 2.502→29.235 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19440	0	160	367	19967
B_iso mean	-	-	71.86	44.84	-
Num. residues	-	-	-	-	2540

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	19985
X-RAY DIFFRACTION	f_angle_d	1.069	27009
X-RAY DIFFRACTION	f_chiral_restr	0.062	3054
X-RAY DIFFRACTION	f_plane_restr	0.007	3450
X-RAY DIFFRACTION	f_dihedral_angle_d	11.032	12137

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	12203	X-RAY DIFFRACTION	10.536	TORSIONAL
1	2	B	12203	X-RAY DIFFRACTION	10.536	TORSIONAL
1	3	C	12203	X-RAY DIFFRACTION	10.536	TORSIONAL
1	4	D	12203	X-RAY DIFFRACTION	10.536	TORSIONAL
1	5	E	12203	X-RAY DIFFRACTION	10.536	TORSIONAL
1	6	F	12203	X-RAY DIFFRACTION	10.536	TORSIONAL
1	7	G	12203	X-RAY DIFFRACTION	10.536	TORSIONAL
1	8	H	12203	X-RAY DIFFRACTION	10.536	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 (%)
2.5017-2.5301	0.382	94	0.3491	1585	1679	48
2.5301-2.5599	0.4104	136	0.2811	2830	2966	85
2.5599-2.5911	0.3299	161	0.2778	2899	3060	86
2.5911-2.6239	0.3148	172	0.2551	2847	3019	86
2.6239-2.6584	0.2987	138	0.2559	2964	3102	89
2.6584-2.6948	0.3354	152	0.2522	3014	3166	90
2.6948-2.7332	0.3047	183	0.2439	2991	3174	92
2.7332-2.774	0.3709	150	0.2463	3168	3318	92
2.774-2.8173	0.3052	155	0.2293	3099	3254	95
2.8173-2.8635	0.332	172	0.2289	3222	3394	96
2.8635-2.9128	0.3059	165	0.2149	3238	3403	97
2.9128-2.9657	0.2784	186	0.2099	3245	3431	98
2.9657-3.0227	0.284	184	0.2041	3304	3488	99
3.0227-3.0843	0.2967	178	0.2009	3315	3493	99
3.0843-3.1513	0.2964	187	0.2048	3321	3508	100
3.1513-3.2245	0.2621	198	0.1943	3286	3484	100
3.2245-3.3051	0.2865	176	0.1907	3362	3538	100
3.3051-3.3943	0.2671	188	0.1845	3258	3446	100
3.3943-3.494	0.2645	181	0.1777	3389	3570	100
3.494-3.6066	0.2382	172	0.1732	3299	3471	100
3.6066-3.7353	0.27	162	0.1729	3336	3498	100
3.7353-3.8845	0.1965	169	0.173	3382	3551	100
3.8845-4.0609	0.2322	178	0.1598	3308	3486	100
4.0609-4.2743	0.1966	170	0.1596	3341	3511	100
4.2743-4.5412	0.2123	175	0.1552	3349	3524	100
4.5412-4.8903	0.1895	160	0.1446	3382	3542	100
4.8903-5.3797	0.2399	158	0.1675	3339	3497	100
5.3797-6.1519	0.2462	175	0.1895	3342	3517	100
6.1519-7.7269	0.2463	159	0.1918	3381	3540	100
7.7269-29.2372	0.1964	172	0.161	3341	3513	98

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	0.0285	-0.1018	-0.0889	0.1892	-0.1025	0.1735	-0.1322	-0.0078	0.002	-0.081	-0.0448	0.0087	-0.0923	0.1487	0	0.2709	-0.0459	0.0058	0.2708	0.0154	0.2626	37.2956	14.7634	-4.8712
2	0.1457	-0.1372	0.0281	0.2146	0.0018	0.3737	-0.096	-0.0594	0.0744	-0.2509	0.0566	0.1025	-0.1561	0.1151	0.0395	0.3271	0.0195	-0.0818	0.1828	0.0289	0.2531	22.4345	22.8828	-8.0105
3	0.8597	-0.2729	-0.0235	0.1319	0.0197	0.0076	0.0372	-0.1676	0.2759	-0.1105	0.0408	0.0411	-0.0684	-0.0122	0.1826	0.5748	0.0189	-0.1641	0.1468	0.0536	0.2775	18.3997	31.3863	-10.3664
4	0.0105	-0.0077	0.0044	0.0119	0.0052	0.0039	-0.0344	-0.0255	-0.0641	0.2118	0.1471	-0.0536	0.1065	0.0676	-0	0.321	0.0055	0.0468	0.398	-0.0038	0.3427	22.0876	0.9078	31.3315
5	0.0289	-0.0967	0.0274	0.5845	0.0009	0.0244	-0.1402	-0.0584	-0.1573	-0.1838	-0.103	0.1315	0.1058	-0.012	-0.1895	0.1145	0.0137	0.0453	0.2446	-0.0003	0.3521	15.7747	-3.2824	8.7471
6	0.01	0.027	0.0205	0.0756	0.0689	0.0725	-0.3475	0.1154	-0.317	-0.2402	-0.1647	0.1838	0.1839	-0.1254	-0.0148	0.2569	0.0135	0.04	0.3819	0.0264	0.503	1.3649	-5.4632	15.5689
7	0.0444	0.0897	0.096	0.4397	0.2285	0.6742	-0.0161	0.1033	-0.2753	-0.2275	-0.2023	0.1516	-0.1897	-0.0735	-0.157	0.1954	0.0579	0.0892	0.3484	0.0501	0.4765	7.7369	1.3047	12.0618
8	0.0302	-0.1143	-0.0299	0.1991	0.0717	0.0387	-0.1318	0.032	0.0522	0.0807	0.1035	0.0267	-0.0936	-0.071	-0.0019	0.1692	0.0502	0.0134	0.3018	0.0041	0.2974	11.5231	8.7058	20.8957
9	-0.0059	-0.0086	-0.0026	0.0092	-0.011	0.12	-0.0485	-0.0634	-0.0669	-0.0719	0.1376	0.2856	-0.4114	0.0997	-0.0003	0.4574	0.108	-0.1015	0.2477	-0.0756	0.463	3.478	32.1965	9.6755
10	0.0054	-0.0244	-0.0094	0.0697	0.0398	0.0342	-0.0106	-0.0602	0.0049	-0.0876	0.1286	0.393	-0.1469	-0.0744	0.0021	0.2061	0.0409	-0.0758	0.2811	0.009	0.4325	4.3545	16.9887	14.894
11	0.0414	0.0323	0.0811	0.0608	0.1219	0.7376	-0.2074	0.0617	-0.1442	0.1645	0.1307	0.2593	-0.3256	-0.0696	-0.0931	-0.0488	0.4799	0.113	0.2628	-0.1193	0.3965	-1.9821	21.3512	20.4002
12	0.1156	-0.171	-0.0515	0.2516	0.2049	0.1596	-0.0371	0.0399	0.0068	-0.334	0.0637	0.1408	-0.0941	-0.1356	0.0297	0.2153	-0.0046	0.0298	0.1896	0.0088	0.193	36.3574	-9.1349	-11.2612
13	0.3892	-0.2746	0.0601	0.3505	-0.1	0.2034	-0.0121	0.0306	-0.0272	-0.1436	0.0065	-0.0121	0.0944	0.0814	-0.0001	0.1946	-0.0046	0.041	0.2469	0.0102	0.21	54.0806	-18.932	-6.8492
14	0.0139	-0.0544	-0.0224	0.2028	0.0661	0.0248	0.0702	-0.0996	0.0819	-0.1305	-0.0667	0.3399	-0.176	-0.1685	-0.0086	0.2597	-0.0636	0.0571	0.4142	0.1207	0.3116	19.7884	-13.4643	26.608
15	0.1612	0.0673	0.0165	0.0639	0.0476	0.0521	-0.1543	-0.0465	-0.1371	0.2871	0.2262	-0.1793	0.0561	-0.03	0.0119	0.2785	0.02	0.0407	0.2448	0.0268	0.1973	32.7573	-5.5577	22.9792
16	0.193	0.1541	0.1607	0.1449	0.0766	0.3075	-0.0109	-0.0978	-0.0522	-0.0453	-0.1848	-0.0631	-0.114	-0.0264	-0.1746	0.2419	0.0116	0.0617	0.1674	0.0477	0.2352	42.4615	1.9264	16.6009
17	0.0268	-0.0192	0.0245	0.0064	-0.0116	0.021	0.1758	0.112	0.1703	0.1089	0.0666	0.0514	-0.2776	0.1556	-0.0002	0.3312	0.0483	-0.0009	0.2972	-0.0549	0.3269	44.0086	-4.4075	34.0176
18	0.0872	0.0417	0.0418	0.1766	-0.0449	0.0584	-0.0092	-0.008	-0.0301	0.011	-0.0303	-0.0311	-0.0216	-0.1402	0	0.1978	-0.0042	0.0544	0.1851	0.0168	0.1694	39.736	-12.4265	28.6508
19	0.0043	-0.0171	0.0371	0.0486	-0.0208	0.1138	0.0453	0.0217	0.1161	-0.0013	-0.0136	-0.0975	0.154	-0.0053	0.0003	0.2027	0.013	0.0189	0.2624	0.0173	0.337	33.0393	-21.6065	14.9371
20	0.7927	-0.3915	-1.0289	0.194	0.4987	1.3464	-0.4233	0.0423	-0.032	-0.0656	-0.1574	0.0598	0.1791	-0.0864	-0.3031	0.2512	0.0833	-0.0674	0.3541	0.0764	0.2973	57.7975	-34.3381	15.905
21	0.7081	-0.0423	0.1807	0.0055	-0.0119	0.0512	-0.1317	0.0523	0.1606	-0.0124	-0.117	-0.0018	0.3326	-0.0733	-0.0502	0.4039	0.0347	0.037	0.2558	0.0028	0.213	48.9595	-35.388	8.8773
22	-0.0104	0.0005	0.018	0.0617	-0.0535	0.0066	0.0036	-0.0143	0.2043	0.3431	0.0188	0.0093	0.158	0.03	0.0015	0.1999	0.0085	-0.0138	0.2497	-0.0051	0.3097	46.7625	-23.5442	22.1962
23	0.0282	0.0291	-0.0515	0.0125	-0.0303	0.0465	-0.0671	-0.0939	-0.0204	0.0363	0.0437	-0.0055	0.0827	0.2733	0.0001	0.212	0.0541	-0.0111	0.2818	0.0283	0.1853	48.5883	-30.8187	27.749
24	0.2879	0.1975	0.1811	0.3423	-0.0583	0.1783	-0.0409	-0.0918	-0.1579	0.0749	-0.0807	-0.0738	-0.1543	0.2278	-0.0001	0.2458	0.0343	-0.0586	0.2755	0.0335	0.2874	-1.8422	54.7894	41.7628
25	0.0951	0.0337	-0.0275	0.0787	-0.0389	0.0381	-0.0685	-0.0285	-0.2499	0.0716	0.1019	-0.143	0.1209	0.1253	-0	0.5508	0.0649	-0.0662	0.391	0.0403	0.4455	2.2288	41.2634	45.8307
26	0.5093	0.0425	-0.2918	0.0736	-0.017	0.1765	-0.1249	0.0343	-0.2432	0.1975	0.0748	0.0309	0.1494	-0.0068	-0.2377	0.4337	0.0119	-0.001	0.2274	0.1092	0.3911	-4.6965	40.0673	45.3328
27	0.221	-0.1327	-0.1068	0.1355	0.0709	0.1246	0.0058	0.0085	-0.124	0.0589	-0.0212	0.0812	-0.1171	-0.132	0.0002	0.264	-0.023	0.0081	0.2896	0.0178	0.3353	-23.2696	45.5568	39.4728
28	0.0518	0.0294	-0.0117	0.0045	-0.0078	-0.0118	0.0484	0.155	-0.2052	0.1625	-0.0226	-0.0714	0.3042	-0.2579	0.0003	0.4416	-0.1129	-0.0059	0.3161	0.0069	0.4961	-20.8346	35.6876	42.8742
29	0.3654	0.2912	0.1885	0.1766	0.131	0.1153	0.0089	0.0964	0.0354	-0.0608	0.0299	0.0793	-0.2176	0.0108	0.0028	0.2532	0.055	-0.0324	0.2945	-0.0124	0.2426	-17.3155	69.7058	16.8179
30	0.3172	0.2953	0.0487	0.3286	0.1543	0.0653	0.0839	0.1382	-0.1479	0.0342	-0.0621	0.0051	-0.0115	-0.0615	0.0023	0.1749	0.0515	-0.0452	0.2688	-0.0584	0.2547	-22.6871	53.6795	14.5077
31	0.1318	0.1539	0.0323	0.1125	0.0194	-0.0116	0.0506	0.326	0.0422	-0.1087	0.006	0.1005	0.1254	-0.135	0.0045	0.2589	-0.0038	-0.0466	0.421	-0.1112	0.3726	-29.9736	48.2205	11.5765
32	0.0058	-0.0133	-0.0018	0.0228	0.0015	-0.0003	0.1502	-0.2482	0.0798	0.0458	-0.0248	-0.12	0.0343	-0.0422	0.0044	0.3477	0.075	-0.0482	0.3977	-0.014	0.3146	6.6183	59.8854	54.5889
33	0.0064	-0.0222	0.023	0.0194	-0.0066	0.0125	0.1784	-0.0635	0.1576	-0.0084	-0.0654	-0.0922	0.0482	-0.2554	-0	0.2998	-0.0045	-0.0034	0.272	-0.0143	0.2079	-6.4852	76.058	42.8756
34	0.1708	0.084	0.0335	0.0535	0.0435	0.0326	0.0417	-0.0541	0.007	0.1223	0.0083	0.0051	-0.0603	0.1769	0	0.3066	-0.0108	0.0224	0.2618	0.0128	0.1587	-3.5771	82.6301	52.2853
35	0.321	-0.0417	0.1294	-0.0009	-0.0191	0.0543	-0.0068	-0.1818	0.0704	0.0197	-0.0366	-0.0489	-0.0764	-0.1186	0.0015	0.3046	-0.0464	0.0027	0.1483	0.0576	0.1979	0.9799	80.0153	61.5319
36	0.0173	-0.0186	0.0019	0.0121	-0.0011	-0.0011	-0.0274	-0.0648	-0.1496	0.0298	-0.0304	0.0497	0.0332	0.115	-0.0001	0.2664	-0.02	0.0267	0.2894	0.0011	0.1608	6.2947	80.7564	54.9545
37	0.1224	0.0012	0.0591	0.0103	0.0161	0.0334	0.017	0.0116	0.0978	-0.1981	-0.0543	-0.0092	0.1553	0.0979	0.0001	0.3876	0.0333	-0.0467	0.3384	0.0081	0.3018	14.1219	72.6411	44.2915
38	0.0374	-0.0148	0.0553	0.0409	-0.006	0.053	-0.1077	0.0745	0.0012	-0.0415	-0.0622	0.0389	-0.1726	0.1747	-0.0001	0.3207	-0.0139	0.0536	0.3863	-0.016	0.3805	25.7625	95.2801	40.4778
39	0.0159	0.0227	-0.0247	0.0019	-0.0322	0.0592	0.2246	-0.0636	-0.0391	-0.1702	-0.1189	0.1804	-0.1512	0.1639	0.0001	0.3146	-0.0279	-0.0437	0.2309	0.0469	0.2599	13.5289	87.4989	48.0285
40	0.6385	0.0286	-0.0652	0.1651	-0.1323	0.6302	0.2904	-0.1599	0.1995	0.0501	-0.2688	0.0932	-0.3008	0.241	0.0435	0.2438	-0.0998	-0.03	0.2403	0.0095	0.2226	19.8348	90.996	54.9473
41	0.2316	0.1664	-0.1429	0.104	-0.0818	0.1276	0.0165	0.1079	-0.047	-0.1002	-0.0503	0.0018	0.3084	-0.0542	-0.0001	0.3047	0.042	-0.0092	0.2356	-0.0213	0.1691	2.3457	71.3568	16.3673
42	0.0059	0.0102	-0.0039	0.0095	0.007	0.0036	-0.131	0.0686	-0.0998	0.0207	-0.1371	-0.1243	0.1703	0.0443	0.0001	0.4746	0.0522	0.0091	0.4423	0.0062	0.4219	16.1252	70.9665	7.1158
43	0.1205	0.0244	-0.0633	0.1252	-0.0484	0.0516	-0.0318	-0.0528	-0.1309	-0.1065	0.0101	0.0129	0.0954	-0.1326	-0.0924	0.2675	0.0737	-0.0123	0.194	0.0196	-0.0083	10.8176	78.9929	11.3314
44	0.04	-0.0033	0.0204	0.1397	-0.1399	0.1747	-0.0739	0.0514	-0.0165	-0.102	0.038	-0.0022	0.0011	0.08	-0	0.2999	-0.0259	0.0622	0.2813	0.0042	0.2792	10.0172	92.9873	24.8255
45	0.0509	0.0243	0.043	0.0952	-0.0206	0.0138	0.1537	0.0557	0.0309	-0.1363	0.0705	-0.1583	-0.2599	-0.0627	0.0005	0.3738	0.0091	0.0401	0.3123	-0.0224	0.3027	15.558	93.0215	22.8906
46	0.0843	0.1403	0.1314	0.2027	0.1771	0.1965	-0.1358	0.1547	0.1358	-0.4424	0.3991	-0.0423	-0.1909	0.2537	0.0002	0.3057	-0.0236	0.0862	0.3119	0.0288	0.2933	19.2403	97.2991	14.5139

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 106 )	A	9 - 106
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 107 through 247 )	A	107 - 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 28 )	B	9 - 28
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 29 through 88 )	B	29 - 88
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 89 through 106 )	B	89 - 106
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 107 through 131 )	B	107 - 131
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 132 through 212 )	B	132 - 212
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 213 through 247 )	B	213 - 247
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 248 through 290 )	B	248 - 290
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 291 through 335 )	B	291 - 335
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 9 through 131 )	C	9 - 131
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 132 through 335 )	C	132 - 335
14	X-RAY DIFFRACTION	14	chain 'D' and (resid 9 through 28 )	D	9 - 28
15	X-RAY DIFFRACTION	15	chain 'D' and (resid 29 through 48 )	D	29 - 48
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 49 through 88 )	D	49 - 88
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 89 through 106 )	D	89 - 106
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 107 through 179 )	D	107 - 179
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 180 through 212 )	D	180 - 212
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 213 through 231 )	D	213 - 231
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 232 through 247 )	D	232 - 247
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 248 through 290 )	D	248 - 290
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 291 through 335 )	D	291 - 335
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 9 through 88 )	E	9 - 88
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 89 through 122 )	E	89 - 122
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 123 through 155 )	E	123 - 155
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 156 through 247 )	E	156 - 247
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 248 through 335 )	E	248 - 335
29	X-RAY DIFFRACTION	29	chain 'F' and (resid 9 through 106 )	F	9 - 106
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 107 through 247 )	F	107 - 247
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 248 through 335 )	F	248 - 335
32	X-RAY DIFFRACTION	32	chain 'G' and (resid 9 through 28 )	G	9 - 28
33	X-RAY DIFFRACTION	33	chain 'G' and (resid 29 through 88 )	G	29 - 88
34	X-RAY DIFFRACTION	34	chain 'G' and (resid 89 through 131 )	G	89 - 131
35	X-RAY DIFFRACTION	35	chain 'G' and (resid 132 through 148 )	G	132 - 148
36	X-RAY DIFFRACTION	36	chain 'G' and (resid 149 through 170 )	G	149 - 170
37	X-RAY DIFFRACTION	37	chain 'G' and (resid 171 through 212 )	G	171 - 212
38	X-RAY DIFFRACTION	38	chain 'G' and (resid 213 through 247 )	G	213 - 247
39	X-RAY DIFFRACTION	39	chain 'G' and (resid 248 through 290 )	G	248 - 290
40	X-RAY DIFFRACTION	40	chain 'G' and (resid 291 through 335 )	G	291 - 335
41	X-RAY DIFFRACTION	41	chain 'H' and (resid 9 through 88 )	H	9 - 88
42	X-RAY DIFFRACTION	42	chain 'H' and (resid 89 through 106 )	H	89 - 106
43	X-RAY DIFFRACTION	43	chain 'H' and (resid 107 through 179 )	H	107 - 179
44	X-RAY DIFFRACTION	44	chain 'H' and (resid 180 through 231 )	H	180 - 231
45	X-RAY DIFFRACTION	45	chain 'H' and (resid 232 through 290 )	H	232 - 290
46	X-RAY DIFFRACTION	46	chain 'H' and (resid 291 through 335 )	H	291 - 335

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