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

ID or keywords:

Entry

Database: PDB / ID: 5pzy

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-(2-chlorophenyl)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: 2.21 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-(2-chlorophenyl)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	5pzy.cif.gz	973.6 KB	Display	PDBx/mmCIF format
PDB format	pdb5pzy.ent.gz	813.7 KB	Display	PDB format
PDBx/mmJSON format	5pzy.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/5pzy ftp://data.pdbj.org/pub/pdb/validation_reports/pz/5pzy	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	2fix-d 5q06-d 5zwk-d 5pzx-1 2fhy-d 5q07-2 5q05-1 2wbd-2 2wbb-2 2vt5-1 2y5k-d 5pzz-2 5q08-1 5q0a-d 5q08-2 2jjk-d 5q02-d 5q09-1 5q03-2 5q00-2 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)	66.214, 283.778, 83.368
Angle α, β, γ (deg.)	90.000, 97.310, 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-94V / N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-2-chlorobenzene-1-sulfonamide Mass: 396.668 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₁₀H₇BrClN₃O₃S₂
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 927 / 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: 54.8 %
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 20, 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: 2.21→24.255 Å / Num. obs: 140872 / % possible obs: 93.01 %

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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: 2.21→24.255 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 23.81 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.228	7106	5.04 %
R_work	0.1726	133766	-
obs	0.1754	140872	93.01 %

Solvent computation

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

Displacement parameters

B_iso max: 137.25 Å² / B_iso mean: 42.422 Å² / B_iso min: 9.2 Å²

Refinement step

Cycle: final / Resolution: 2.21→24.255 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19440	0	160	927	20527
B_iso mean	-	-	47.55	42.62	-
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	0.964	27001
X-RAY DIFFRACTION	f_chiral_restr	0.058	3054
X-RAY DIFFRACTION	f_plane_restr	0.006	3450
X-RAY DIFFRACTION	f_dihedral_angle_d	10.296	12137

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	12223	X-RAY DIFFRACTION	9.324	TORSIONAL
1	2	B	12223	X-RAY DIFFRACTION	9.324	TORSIONAL
1	3	C	12223	X-RAY DIFFRACTION	9.324	TORSIONAL
1	4	D	12223	X-RAY DIFFRACTION	9.324	TORSIONAL
1	5	E	12223	X-RAY DIFFRACTION	9.324	TORSIONAL
1	6	F	12223	X-RAY DIFFRACTION	9.324	TORSIONAL
1	7	G	12223	X-RAY DIFFRACTION	9.324	TORSIONAL
1	8	H	12223	X-RAY DIFFRACTION	9.324	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 (%)
2.21-2.2351	0.3082	207	0.2706	3786	3993	80
2.2351-2.2614	0.3325	222	0.2626	3885	4107	81
2.2614-2.2889	0.2988	216	0.2439	3928	4144	83
2.2889-2.3179	0.323	249	0.2355	4082	4331	86
2.3179-2.3484	0.2797	212	0.2222	4077	4289	85
2.3484-2.3805	0.2696	214	0.2231	4195	4409	87
2.3805-2.4145	0.3072	217	0.2267	4190	4407	89
2.4145-2.4505	0.309	237	0.2356	4387	4624	90
2.4505-2.4887	0.3086	235	0.2338	4354	4589	93
2.4887-2.5295	0.2924	241	0.2149	4497	4738	93
2.5295-2.5731	0.2763	266	0.2247	4557	4823	96
2.5731-2.6198	0.3006	233	0.22	4671	4904	97
2.6198-2.6701	0.2667	240	0.206	4679	4919	97
2.6701-2.7246	0.2539	235	0.1897	4679	4914	98
2.7246-2.7837	0.2718	230	0.1839	4750	4980	98
2.7837-2.8484	0.2247	255	0.1789	4657	4912	98
2.8484-2.9195	0.2473	270	0.179	4643	4913	98
2.9195-2.9983	0.2657	257	0.1822	4751	5008	98
2.9983-3.0864	0.235	233	0.1781	4665	4898	98
3.0864-3.1858	0.2346	239	0.1753	4728	4967	98
3.1858-3.2994	0.2345	212	0.1756	4719	4931	97
3.2994-3.4311	0.2375	251	0.1673	4628	4879	97
3.4311-3.5868	0.2287	227	0.1623	4648	4875	97
3.5868-3.7752	0.2071	273	0.1569	4607	4880	96
3.7752-4.0108	0.2102	257	0.1482	4592	4849	96
4.0108-4.3189	0.1749	233	0.1413	4595	4828	95
4.3189-4.7505	0.1658	255	0.1271	4604	4859	95
4.7505-5.4312	0.1755	216	0.1341	4557	4773	95
5.4312-6.8175	0.2025	245	0.1628	4584	4829	95
6.8175-24.2561	0.1845	229	0.1461	4071	4300	84

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	0.3245	0.2845	-0.1037	0.585	-0.2782	0.1762	-0.118	-0.0252	0.0814	-0.1265	-0.0167	-0.031	-0.1142	0.1083	-0.0167	0.1855	-0.0073	0.0322	0.1469	0.0141	0.1633	37.4011	16.0105	-5.5187
2	0.5197	-0.4312	-0.1479	0.2189	-0.0337	0.2667	-0.0272	-0.0357	0.0541	-0.206	0.0057	0.1475	-0.0118	0.0753	0.0004	0.2453	0.0012	-0.0652	0.1438	0.0178	0.2397	19.8192	22.8417	-7.8225
3	0.2529	-0.1527	0.027	0.1102	-0.1178	0.1365	-0.0129	-0.0257	0.1328	-0.0791	0.0367	0.0923	-0.2055	-0.0176	0.0326	0.3962	0.0171	-0.1037	0.1421	0.0096	0.3128	18.1126	31.3045	-10.2229
4	0.6802	-0.4599	-0.2892	0.8709	-0.1868	0.3873	-0.0612	-0.1417	-0.1948	-0.1724	0.0219	0.1774	0.1745	0.0661	-0.0261	0.0932	-0.002	0.0245	0.2236	0.0341	0.29	12.6091	-2.9126	15.9504
5	0.5066	-0.1304	-0.0469	0.3805	0.0152	0.3661	-0.0951	-0.118	0.0074	-0.0242	0.0149	0.1606	-0.1126	0.0187	-0.0579	0.0735	0.0416	0.0086	0.1757	-0.0262	0.2467	9.0224	15.5577	16.2264
6	0.3678	-0.091	0.0095	0.3331	-0.2371	1.0504	0.0227	-0.0847	-0.1059	0.0385	-0.0104	0.1842	-0.9538	0.0483	-0.0077	-0.1957	0.173	0.0135	0.2075	-0.05	0.4441	0.9318	18.9692	17.7307
7	0.28	-0.3096	-0.3795	0.4031	0.352	0.4346	-0.0427	0.0329	-0.0077	-0.1974	0.0102	0.1022	0.0347	0.0167	-0.0066	0.1882	0.0399	0.0083	0.1877	0.0212	0.129	35.9855	-8.9807	-11.3961
8	0.2036	-0.1356	0.0071	0.2899	-0.0796	0.4898	0.005	0.0443	-0.0098	-0.1949	-0.0501	-0.0083	0.1104	0.092	-0.0331	0.1744	0.0468	0.0735	0.2136	0.0228	0.1665	53.686	-18.7239	-7.132
9	0.0347	-0.1577	0.169	0.1195	-0.201	0.4662	0.0173	-0.0969	0.0478	0.0533	0.0152	0.0058	-0.0326	-0.0247	0.0061	0.0762	-0.0023	0.0439	0.2278	0.018	0.1849	32.8206	-4.6534	21.1679
10	0.0576	-0.0664	0.0592	0.0464	0.0076	0.0615	0.1494	0.2085	-0.172	0.1837	-0.0968	0.0348	-0.1673	0.1541	-0.0001	0.2946	0.0411	0.0008	0.2876	-0.0094	0.2261	43.8048	-4.2318	33.8832
11	0.2034	-0.0685	0.0467	0.3476	-0.2867	0.1612	0.0002	0.007	0.0677	0.1619	-0.0027	-0.1604	-0.0583	0.0534	0.0009	0.2028	0.0231	0.0111	0.2273	0.0305	0.1435	41.6724	-10.0442	30.9552
12	0.159	-0.0759	0.0067	0.334	-0.3693	0.4161	0.0107	-0.0411	-0.0215	-0.0052	-0.0071	0.0339	0.1481	0.0237	-0.0375	0.1345	0.0295	-0.0016	0.1329	0.0206	0.1336	41.5965	-25.6072	15.8425
13	0.1035	-0.1755	-0.23	0.0187	0.0826	0.1846	-0.0085	-0.043	0.0369	0.0687	0.0271	-0.0216	0.073	0.0577	0.0034	0.2274	0.065	-0.0174	0.1695	0.0368	0.1377	47.5975	-26.8982	24.7232
14	0.3662	-0.0552	0.0778	0.4612	-0.2701	0.3633	0.0702	-0.0617	-0.1586	0.108	-0.0659	-0.0324	0.0271	0.2044	0.0001	0.2975	-0.0134	-0.0213	0.2266	0.0065	0.2931	-0.609	51.0459	42.6566
15	0.4703	-0.1395	-0.1677	0.2966	0.1916	0.265	0.0489	-0.0479	-0.3315	0.0752	0.0387	0.2058	0.1016	-0.0709	-0.0119	0.2701	-0.0401	-0.0349	0.141	0.0719	0.2903	-5.9004	43.1845	46.1698
16	0.0122	-0.0019	0.1949	0.0448	-0.1007	0.326	0.0403	-0.1629	-0.3411	0.1328	0.0462	-0.0517	-0.1793	-0.2803	0.0073	0.1784	-0.0776	0.032	0.3122	-0.0161	0.4624	-26.4579	43.8905	37.7407
17	0.0888	0.0087	0.1772	0.152	-0.2361	0.1306	0.1288	-0.041	-0.2306	0.1796	-0.1224	0.0728	0.2954	-0.1397	-0.0017	0.3522	-0.0893	0.0166	0.2231	0.0216	0.4496	-20.686	35.2259	43.1089
18	0.6649	0.1437	0.1372	0.2552	-0.1262	0.24	-0.0872	0.1811	0.0566	-0.0338	-0.0017	0.1445	-0.2545	-0.0383	-0.0017	0.2805	0.0169	-0.0656	0.2606	-0.0149	0.2292	-18.512	69.4467	16.3862
19	0.8771	0.0301	0.0263	0.3318	0.0908	0.0947	0.0514	0.2556	-0.3	-0.0744	-0.16	0.1382	-0.1186	-0.0588	-0.059	0.1685	-0.0186	-0.0669	0.3288	-0.1526	0.3121	-22.4066	50.9809	15.2711
20	0.1697	0.1208	-0.0441	0.178	-0.1305	0.1156	0.0276	0.2834	-0.2369	0.0289	0.0507	0.1106	-0.0725	-0.014	0.0123	0.2176	0.0092	-0.072	0.3437	-0.1639	0.3784	-30.0799	47.8806	11.8889
21	0.2141	-0.1074	0.2444	0.5599	0.4404	0.3372	0.0251	-0.0441	0.0495	0.0776	-0.0336	-0.0093	-0.033	-0.0515	0.0001	0.2886	-0.0702	0.0105	0.1921	0.0173	0.1592	-2.7967	74.8698	48.9889
22	0.319	0.244	-0.153	0.494	-0.2412	0.4727	0.0662	-0.0703	0.0183	0.1637	-0.0625	-0.0689	-0.0157	0.0587	0.0001	0.2372	-0.0674	-0.0277	0.1917	0.0015	0.1391	15.5564	84.2829	49.5355
23	0.0312	-0.0311	0.0146	0.0304	-0.0371	0.0321	-0.0985	0.1982	0.0522	-0.0357	-0.0448	0.1355	-0.0654	-0.0892	-0.0003	0.3196	-0.0059	-0.0734	0.4929	0.0564	0.2209	-8.9089	79.6389	8.1582
24	0.1074	0.2496	0.0094	0.1353	-0.0519	0.0348	-0.0822	0.0374	-0.0515	-0.1722	0.1179	-0.0144	0.2101	0.0317	0	0.3192	-0.0058	-0.0009	0.207	-0.0194	0.1619	7.1546	66.8238	20.27
25	0.1407	0.0728	-0.0736	0.2049	-0.0439	0.0516	-0.0133	0.0763	-0.1117	-0.0186	-0.0021	-0.2486	0.4011	0.0015	-0.0019	0.5489	-0.0506	-0.0045	0.3441	-0.0312	0.1853	13.891	71.168	7.6983
26	0.0907	0.098	-0.0129	0.0211	-0.0365	0.0754	-0.1633	-0.0866	-0.0798	0.0116	-0.0833	-0.1178	0.1169	0.2034	-0	0.5027	-0.0236	0.0502	0.2893	0.0116	0.193	14.7379	77.5966	10.6932
27	0.1719	-0.0828	0.001	0.2332	-0.1727	0.0898	0.1123	0.1118	0.0527	-0.1584	0.0081	0.0619	0.0017	-0.0665	-0	0.3047	-0.0309	0.0074	0.2204	0.0253	0.1539	2.5073	85.7736	20.0483
28	0.1079	0.0579	-0.0397	0.0561	0.0014	0.0107	0.0232	-0.1652	-0.1027	-0.4978	-0.0594	-0.1318	-0.7324	0.172	-0.0002	0.4988	-0.1231	0.0706	0.3956	0.0134	0.3081	25.4952	99.6909	28.7836
29	0.2426	0.1076	0.1622	0.0598	0.0546	0.1125	0.2621	0.0939	0.0015	0.1699	0.0322	-0.0454	-0.102	0.0816	0.0411	0.443	-0.1131	0.085	0.1818	0.0172	0.2253	14.9106	100.8377	33.087
30	0.1189	0.0104	-0.0417	0.0888	-0.0429	0.0848	0.0779	0.1413	0.0716	0.0965	0.1525	-0.1468	0.0681	0.104	0.0112	0.3165	-0.0389	-0.0024	0.275	-0.0524	0.202	17.6862	90.7325	23.3455
31	0.0878	0.0018	0.1976	0.0983	-0.1549	0.1512	-0.0548	0.0597	-0.0649	-0.0799	0.1403	-0.096	-0.049	0.0893	-0.0001	0.4076	-0.0748	0.0522	0.248	-0.0009	0.2105	17.8317	93.4903	14.5648

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 122 )	B	9 - 122
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 123 through 247 )	B	123 - 247
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 248 through 335 )	B	248 - 335
7	X-RAY DIFFRACTION	7	chain 'C' and (resid 9 through 131 )	C	9 - 131
8	X-RAY DIFFRACTION	8	chain 'C' and (resid 132 through 335 )	C	132 - 335
9	X-RAY DIFFRACTION	9	chain 'D' and (resid 9 through 88 )	D	9 - 88
10	X-RAY DIFFRACTION	10	chain 'D' and (resid 89 through 106 )	D	89 - 106
11	X-RAY DIFFRACTION	11	chain 'D' and (resid 107 through 155 )	D	107 - 155
12	X-RAY DIFFRACTION	12	chain 'D' and (resid 156 through 247 )	D	156 - 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 106 )	E	9 - 106
15	X-RAY DIFFRACTION	15	chain 'E' and (resid 107 through 179 )	E	107 - 179
16	X-RAY DIFFRACTION	16	chain 'E' and (resid 180 through 247 )	E	180 - 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 122 )	F	9 - 122
19	X-RAY DIFFRACTION	19	chain 'F' and (resid 123 through 247 )	F	123 - 247
20	X-RAY DIFFRACTION	20	chain 'F' and (resid 248 through 335 )	F	248 - 335
21	X-RAY DIFFRACTION	21	chain 'G' and (resid 9 through 131 )	G	9 - 131
22	X-RAY DIFFRACTION	22	chain 'G' and (resid 132 through 335 )	G	132 - 335
23	X-RAY DIFFRACTION	23	chain 'H' and (resid 9 through 28 )	H	9 - 28
24	X-RAY DIFFRACTION	24	chain 'H' and (resid 29 through 88 )	H	29 - 88
25	X-RAY DIFFRACTION	25	chain 'H' and (resid 89 through 122 )	H	89 - 122
26	X-RAY DIFFRACTION	26	chain 'H' and (resid 123 through 155 )	H	123 - 155
27	X-RAY DIFFRACTION	27	chain 'H' and (resid 156 through 212 )	H	156 - 212
28	X-RAY DIFFRACTION	28	chain 'H' and (resid 213 through 231 )	H	213 - 231
29	X-RAY DIFFRACTION	29	chain 'H' and (resid 232 through 247 )	H	232 - 247
30	X-RAY DIFFRACTION	30	chain 'H' and (resid 248 through 274 )	H	248 - 274
31	X-RAY DIFFRACTION	31	chain 'H' and (resid 275 through 335 )	H	275 - 335

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