PDB-5q03: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosph...

ID or keywords:

Entry

Database: PDB / ID: 5q03

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-[5-(2-methylpropyl)thiophen-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: 2.31 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-[5-(2-methylpropyl) ...
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	5q03.cif.gz	961.7 KB	Display	PDBx/mmCIF format
PDB format	pdb5q03.ent.gz	802.1 KB	Display	PDB format
PDBx/mmJSON format	5q03.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/q0/5q03 ftp://data.pdbj.org/pub/pdb/validation_reports/q0/5q03	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	5q0a-d 4mjo-1 5q06-d 6lw2-d 5pzy-1 2fix-d 5pzu-d 5pzx-1 2y5l-1 4fbp-d 1frp-1 5pzy-2 5q07-2 5pzs-d 3a29-d 5q07-1 2wbd-2 5q08-2 5pzv-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

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)	66.435, 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 37 or resid 39...
2	1	(chain B and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))
3	1	(chain C and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))
4	1	(chain D and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))
5	1	(chain E and (resid 9 through 37 or resid 39...
6	1	(chain F and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))
7	1	(chain G and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))
8	1	(chain H and (resid 9 through 37 or resid 39 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	LEU	LEU	(chain A and (resid 9 through 37 or resid 39...	A	A	9 - 37	10 - 38
1	2	THR	THR	GLY	GLY	(chain A and (resid 9 through 37 or resid 39...	A	A	39 - 61	40 - 62
1	3	LYS	LYS	TYR	TYR	(chain A and (resid 9 through 37 or resid 39...	A	A	72 - 139	73 - 140
1	4	LYS	LYS	SER	SER	(chain A and (resid 9 through 37 or resid 39...	A	A	141 - 335	142 - 336
2	1	ASP	ASP	LEU	LEU	(chain B and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	B	B	9 - 37	10 - 38
2	2	THR	THR	TYR	TYR	(chain B and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	B	B	39 - 139	40 - 140
2	3	LYS	LYS	SER	SER	(chain B and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	B	B	141 - 335	142 - 336
3	1	ASP	ASP	LEU	LEU	(chain C and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	C	C	9 - 37	10 - 38
3	2	THR	THR	TYR	TYR	(chain C and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	C	C	39 - 139	40 - 140
3	3	LYS	LYS	SER	SER	(chain C and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	C	C	141 - 335	142 - 336
4	1	ASP	ASP	LEU	LEU	(chain D and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	D	D	9 - 37	10 - 38
4	2	THR	THR	TYR	TYR	(chain D and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	D	D	39 - 139	40 - 140
4	3	LYS	LYS	SER	SER	(chain D and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	D	D	141 - 335	142 - 336
5	1	ASP	ASP	LEU	LEU	(chain E and (resid 9 through 37 or resid 39...	E	E	9 - 37	10 - 38
5	2	THR	THR	GLY	GLY	(chain E and (resid 9 through 37 or resid 39...	E	E	39 - 61	40 - 62
5	3	LYS	LYS	TYR	TYR	(chain E and (resid 9 through 37 or resid 39...	E	E	72 - 139	73 - 140
5	4	LYS	LYS	SER	SER	(chain E and (resid 9 through 37 or resid 39...	E	E	141 - 335	142 - 336
6	1	ASP	ASP	LEU	LEU	(chain F and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	F	F	9 - 37	10 - 38
6	2	THR	THR	TYR	TYR	(chain F and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	F	F	39 - 139	40 - 140
6	3	LYS	LYS	SER	SER	(chain F and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	F	F	141 - 335	142 - 336
7	1	ASP	ASP	LEU	LEU	(chain G and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	G	G	9 - 37	10 - 38
7	2	THR	THR	TYR	TYR	(chain G and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	G	G	39 - 139	40 - 140
7	3	LYS	LYS	SER	SER	(chain G and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	G	G	141 - 335	142 - 336
8	1	ASP	ASP	LEU	LEU	(chain H and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	H	H	9 - 37	10 - 38
8	2	THR	THR	TYR	TYR	(chain H and (resid 9 through 37 or resid 39 through 139 or resid 141 through 335))	H	H	39 - 139	40 - 140
8	3	LYS	LYS	SER	SER	(chain H and (resid 9 through 37 or resid 39 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-95M / N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-5-(2-methylpropyl)thiophene-2-sulfonamide Mass: 424.357 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₁₂H₁₄BrN₃O₃S₃
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 1070 / 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: 2.31→20.369 Å / Num. obs: 133552 / % possible obs: 96.71 %

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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: 2.31→20.369 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 25.72 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2379	6681	5 %
R_work	0.1784	126871	-
obs	0.1815	133552	96.71 %

Solvent computation

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

Displacement parameters

B_iso max: 142.59 Å² / B_iso mean: 39.1678 Å² / B_iso min: 6.06 Å²

Refinement step

Cycle: final / Resolution: 2.31→20.369 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19440	0	176	1070	20686
B_iso mean	-	-	47.76	40.1	-
Num. residues	-	-	-	-	2540

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.01	20015
X-RAY DIFFRACTION	f_angle_d	1.063	27047
X-RAY DIFFRACTION	f_chiral_restr	0.063	3056
X-RAY DIFFRACTION	f_plane_restr	0.007	3454
X-RAY DIFFRACTION	f_dihedral_angle_d	10.427	12163

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	12159	X-RAY DIFFRACTION	10.55	TORSIONAL
1	2	B	12159	X-RAY DIFFRACTION	10.55	TORSIONAL
1	3	C	12159	X-RAY DIFFRACTION	10.55	TORSIONAL
1	4	D	12159	X-RAY DIFFRACTION	10.55	TORSIONAL
1	5	E	12159	X-RAY DIFFRACTION	10.55	TORSIONAL
1	6	F	12159	X-RAY DIFFRACTION	10.55	TORSIONAL
1	7	G	12159	X-RAY DIFFRACTION	10.55	TORSIONAL
1	8	H	12159	X-RAY DIFFRACTION	10.55	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 (%)
2.3103-2.3366	0.3427	84	0.2687	1509	1593	35
2.3366-2.364	0.3087	166	0.263	3172	3338	72
2.364-2.3928	0.3036	206	0.2629	4128	4334	94
2.3928-2.423	0.3428	224	0.2636	4348	4572	100
2.423-2.4549	0.327	247	0.2476	4419	4666	100
2.4549-2.4884	0.3459	211	0.2483	4327	4538	100
2.4884-2.5239	0.3076	232	0.2491	4395	4627	100
2.5239-2.5615	0.3625	254	0.2448	4342	4596	100
2.5615-2.6015	0.3115	238	0.2323	4312	4550	100
2.6015-2.644	0.2844	222	0.2243	4399	4621	100
2.644-2.6895	0.2979	232	0.2157	4391	4623	100
2.6895-2.7383	0.2987	216	0.2118	4306	4522	100
2.7383-2.7909	0.2693	234	0.2079	4442	4676	100
2.7909-2.8477	0.2913	210	0.2032	4343	4553	100
2.8477-2.9094	0.2734	260	0.1937	4388	4648	100
2.9094-2.9769	0.2428	231	0.1903	4332	4563	100
2.9769-3.0511	0.2919	241	0.1933	4324	4565	100
3.0511-3.1333	0.2558	213	0.1835	4440	4653	100
3.1333-3.2252	0.2506	219	0.1823	4373	4592	100
3.2252-3.3289	0.2402	208	0.1734	4435	4643	100
3.3289-3.4473	0.2299	222	0.1743	4323	4545	100
3.4473-3.5846	0.2338	225	0.1684	4372	4597	100
3.5846-3.7468	0.2266	242	0.1562	4360	4602	100
3.7468-3.943	0.2102	246	0.1561	4392	4638	100
3.943-4.188	0.2095	240	0.1423	4399	4639	100
4.188-4.5081	0.1741	232	0.1323	4333	4565	100
4.5081-4.9559	0.1691	233	0.1206	4381	4614	100
4.9559-5.6595	0.188	214	0.1432	4396	4610	100
5.6595-7.0803	0.2017	241	0.1729	4393	4634	100
7.0803-20.3694	0.1816	238	0.163	4397	4635	100

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	0.0133	0.0002	0.0064	0.0482	0.0347	0.0343	-0.0433	-0.024	0.0148	-0.1211	-0.0317	-0.0273	-0.0564	0.0373	-0.0105	0.1385	-0.0266	0.0107	0.1191	0.0292	0.1647	37.2144	16.5968	-5.5514
2	0.0097	-0.0218	-0.0052	0.0655	0.0078	0.0069	-0.0645	0.0382	0.0824	-0.0988	-0.0032	0.071	-0.07	0.0285	-0.0662	0.1922	0.0327	-0.0688	0.0928	0.0341	0.2039	19.579	23.561	-7.9431
3	0.0047	0.0046	0.0048	0.0186	-0.0034	0.0146	-0.0123	-0.0015	0.037	-0.0432	-0.0142	0.0043	-0.0142	-0.0055	-0.007	0.3117	0.0311	-0.1569	0.028	0.0543	0.2381	17.8449	32.341	-10.3615
4	0.0128	-0.0025	0.0024	0.0112	0.002	0.0095	-0.006	-0.0466	-0.0824	-0.0216	0.0188	0.1098	0.0152	-0.0204	-0.0027	-0.0162	0.0228	0.0218	0.2006	0.0722	0.2713	12.3513	-1.9773	14.6938
5	0.0057	0.0036	0.0064	0.0034	0.0029	0.0161	0.0152	-0.0102	-0.0108	0.0115	-0.0081	0.0073	0.0265	-0.016	0.0092	0.0827	0.0514	0.0798	0.2207	-0.0089	0.2957	1.4723	-1.6169	23.7526
6	0.0673	-0.0342	0.0002	0.0456	0.0353	0.0483	-0.0494	-0.0985	0.0028	0.001	-0.0556	0.0915	-0.1058	-0.0493	-0.1038	-0.0007	0.1225	0.0192	0.1181	-0.0557	0.2608	9.8589	19.6516	16.2938
7	0.009	-0.0055	-0.0126	0.0037	0.0006	0.0199	-0.0041	-0.0274	-0.038	0.0032	0.0143	0.0654	-0.0297	-0.0291	0.0093	0.0109	0.0992	0.0165	0.2022	-0.0827	0.3955	0.6631	19.6401	17.68
8	0.0114	-0.0041	-0.0052	0.0289	0.0176	0.0185	-0.0228	0.026	-0.0428	-0.1166	-0.0252	0.0318	0.0133	-0.0078	-0.0119	0.1208	0.0517	0.0377	0.135	0.0314	0.1147	35.9037	-9.4277	-11.3696
9	0.0121	-0.0261	-0.0233	0.022	0.0194	0.0117	0.0343	0.0623	-0.054	-0.1432	-0.0022	-0.07	0.0916	0.1287	0.0673	-0.0238	0.1146	0.1783	0.137	-0.0187	0.0288	53.7014	-19.3924	-7.0035
10	0.0158	-0.0107	0.0039	0.0161	-0.0064	0.0069	-0.0297	-0.0457	0.0232	0.0702	0.0328	-0.0305	-0.0004	-0.007	-0.0029	0.005	0.0678	0.0594	0.1527	0.0172	0.0561	36.6862	-5.4885	24.0849
11	0.0325	0.002	0.0223	0.0222	-0.0132	0.0323	-0.0171	-0.0575	-0.021	0.0518	0.0313	0.0092	0.0821	0.0178	0.019	0.0766	0.0411	0.015	0.1257	0.024	0.1006	41.1361	-23.5737	20.615
12	0.0039	-0.0051	-0.0039	0.006	0.0044	0.0157	-0.0241	-0.0405	0.0034	0.0491	0.0196	-0.0424	0.0756	0.0254	-0.0021	0.1635	0.087	0.0026	0.1499	0.0246	0.1398	47.3465	-27.8794	24.8893
13	0.0646	0.0545	0.0174	0.0757	0.0251	0.0207	0.0558	-0.0342	-0.1654	0.0603	0.0433	-0.0502	0.0262	0.0131	0.0693	0.2798	-0.0151	-0.078	0.027	0.0754	0.1384	-3.3635	49.1856	44.1518
14	0.0011	0.0036	-0.0001	0.03	-0.0248	0.0234	0.0132	0.0011	-0.07	0.0227	0.0029	0.0447	-0.0234	-0.0311	0.0017	0.1389	-0.0871	-0.0015	0.1363	0.0011	0.2359	-26.8504	45.6875	37.537
15	0.0025	0.0014	0.0045	0.0075	-0.0035	0.0043	0.0315	-0.0051	-0.0476	0.025	-0.0273	0.0146	0.0298	-0.0285	0	0.304	-0.0871	-0.0064	0.1558	0.0347	0.4213	-21.242	36.6772	43.0122
16	0.0113	0.0121	0.006	0.0098	0.0016	0.0042	-0.0165	0.0789	0.0182	0.0301	-0.0086	0.0887	-0.0339	0.0215	-0	0.2862	0.0069	-0.0436	0.2032	-0.0213	0.1716	-14.0983	70.8501	17.9705
17	0.008	0.0052	0.0056	0.0038	0.004	0.0039	0.0142	0.016	-0.0175	-0.0107	-0.013	0.0025	-0.0239	-0.0214	-0	0.4582	0.0509	-0.0668	0.427	0.0731	0.3542	-26.7602	71.0409	16.5301
18	0.023	0.0127	0.0059	0.0068	-0.0014	0.0167	0.0225	0.083	-0.0414	0.0003	0.0077	0.0174	-0.0311	0.0022	0.0676	0.1486	0.0036	-0.0758	0.2208	-0.0916	0.1292	-18.9236	59.9092	11.0839
19	0.0042	0.0015	-0.0011	0.0027	0.0025	0.0021	0.0166	0.0078	0.0019	0.0026	0.0234	0.0016	-0.0058	-0.0027	0.0001	0.2659	-0.0895	-0.0298	0.3294	-0.1694	0.4825	-30.7671	36.2694	19.8899
20	0.0053	0.0041	0.0065	0.0032	0.0003	0.0038	0.0057	0.0768	-0.0274	0.0157	0.0317	0.0261	0.002	-0.0506	-0	0.2019	0.01	-0.0995	0.2952	-0.09	0.3386	-30.2853	49.7786	11.6607
21	0.0134	0.0117	-0.0003	0.0353	0.0018	0.0025	0.046	-0.0287	0.0224	0.0036	-0.0301	0.0422	-0.0243	-0.0203	-0.0099	0.2719	-0.0558	0.0138	0.0752	0.0134	0.0761	-3.389	75.8171	48.8846
22	0.0089	0.0018	0.0017	0.0144	0.007	0.0035	0.029	-0.0142	0.0502	-0.0356	-0.0154	0.0101	-0.001	-0.0026	-0	0.3357	-0.1357	0.0175	0.2125	-0.0043	0.1372	0.0532	84.111	55.8442
23	0.0366	-0.0224	0.0012	0.0135	-0.0008	0.0142	0.0446	-0.021	0.0335	0.0658	-0.0233	-0.0318	0.0299	0.1014	0.0006	0.2633	-0.0743	-0.0085	0.1565	0.0018	0.1018	16.6323	85.9633	45.2613
24	0.0023	0.0026	0.0017	0.0023	0.004	0.0027	-0.0302	-0.0174	0.0056	0.0311	-0.0566	-0.0084	-0.0295	0.0148	-0	0.2084	-0.1164	-0.0195	0.2108	0.0022	0.1556	20.1467	93.1434	55.1125
25	0.0068	0.0007	-0.0079	0.0056	-0.0008	0.006	-0.0207	0.0523	-0.0087	-0.0378	0.056	-0.023	0.022	-0.0152	0	0.3249	-0.0263	-0.029	0.1823	-0.0101	0.1051	2.3444	73.2058	16.5073
26	0.0079	0.0009	-0.0021	0.0084	-0.005	0.004	0.0183	0.0117	-0.0357	-0.0337	-0.0159	-0.022	0.0062	0.0161	-0	0.4814	-0.0433	0.0435	0.3947	0.0132	0.2188	14.2615	74.649	12.3264
27	0.0051	0.0041	0.0017	0.0066	-0.0018	0.002	0.0037	-0.0113	-0.0107	0.0052	-0.019	-0.023	0.0025	0.0089	-0	0.325	-0.0266	0.0398	0.2563	-0.0076	0.1263	12.3115	80.2059	3.6275
28	0.057	0.0208	0.0303	0.011	0.0088	0.0149	0.0508	0.0516	0.011	-0.0702	0.0253	0.0125	0.0114	0.0175	0.0156	0.2759	-0.0697	0.0144	0.1448	0.0064	0.0778	4.3089	88.1862	17.8084
29	0.0053	0.0019	-0.0028	0.0028	-0.0042	0.0052	-0.013	-0.0016	-0.0122	-0.0017	-0.0444	0.0189	-0.0282	0.0067	-0	0.2943	-0.0848	0.0645	0.2077	0.0176	0.2091	20.8995	103.7545	30.525
30	0.0064	0.0002	0.0078	0.0042	-0.007	0.0112	0.0293	0.0386	-0.0039	-0.0306	0.0322	-0.0679	0.0179	0.037	0	0.3833	-0.0779	0.0333	0.2182	0.0128	0.1732	17.7189	96.0203	17.1058

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 131 )	B	9 - 131
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 132 through 148 )	B	132 - 148
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 149 through 247 )	B	149 - 247
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 248 through 335 )	B	248 - 335
8	X-RAY DIFFRACTION	8	chain 'C' and (resid 9 through 131 )	C	9 - 131
9	X-RAY DIFFRACTION	9	chain 'C' and (resid 132 through 335 )	C	132 - 335
10	X-RAY DIFFRACTION	10	chain 'D' and (resid 9 through 131 )	D	9 - 131
11	X-RAY DIFFRACTION	11	chain 'D' and (resid 132 through 247 )	D	132 - 247
12	X-RAY DIFFRACTION	12	chain 'D' and (resid 248 through 335 )	D	248 - 335
13	X-RAY DIFFRACTION	13	chain 'E' and (resid 9 through 179 )	E	9 - 179
14	X-RAY DIFFRACTION	14	chain 'E' and (resid 180 through 247 )	E	180 - 247
15	X-RAY DIFFRACTION	15	chain 'E' and (resid 248 through 335 )	E	248 - 335
16	X-RAY DIFFRACTION	16	chain 'F' and (resid 9 through 88 )	F	9 - 88
17	X-RAY DIFFRACTION	17	chain 'F' and (resid 89 through 131 )	F	89 - 131
18	X-RAY DIFFRACTION	18	chain 'F' and (resid 132 through 212 )	F	132 - 212
19	X-RAY DIFFRACTION	19	chain 'F' and (resid 213 through 247 )	F	213 - 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 106 )	G	9 - 106
22	X-RAY DIFFRACTION	22	chain 'G' and (resid 107 through 155 )	G	107 - 155
23	X-RAY DIFFRACTION	23	chain 'G' and (resid 156 through 290 )	G	156 - 290
24	X-RAY DIFFRACTION	24	chain 'G' and (resid 291 through 335 )	G	291 - 335
25	X-RAY DIFFRACTION	25	chain 'H' and (resid 9 through 88 )	H	9 - 88
26	X-RAY DIFFRACTION	26	chain 'H' and (resid 89 through 131 )	H	89 - 131
27	X-RAY DIFFRACTION	27	chain 'H' and (resid 132 through 148 )	H	132 - 148
28	X-RAY DIFFRACTION	28	chain 'H' and (resid 149 through 212 )	H	149 - 212
29	X-RAY DIFFRACTION	29	chain 'H' and (resid 213 through 247 )	H	213 - 247
30	X-RAY DIFFRACTION	30	chain 'H' and (resid 248 through 335 )	H	248 - 335

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