PDB-3zm3: Catalytic domain of human SHP2

ID or keywords:

Entry

Database: PDB / ID: 3zm3

Title

Catalytic domain of human SHP2

Components

TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11

Keywords

HYDROLASE / PTP1B

Function / homology

Function and homology information

negative regulation of cortisol secretion / intestinal epithelial cell migration / microvillus organization / negative regulation of growth hormone secretion / genitalia development / multicellular organismal reproductive process / atrioventricular canal development / negative regulation of cell adhesion mediated by integrin / STAT5 Activation / Netrin mediated repulsion signals ...negative regulation of cortisol secretion / intestinal epithelial cell migration / microvillus organization / negative regulation of growth hormone secretion / genitalia development / multicellular organismal reproductive process / atrioventricular canal development / negative regulation of cell adhesion mediated by integrin / STAT5 Activation / Netrin mediated repulsion signals / cerebellar cortex formation / positive regulation of hormone secretion / Interleukin-37 signaling / regulation of protein export from nucleus / positive regulation of ossification / hormone metabolic process / Signaling by Leptin / MET activates PTPN11 / negative regulation of chondrocyte differentiation / Regulation of RUNX1 Expression and Activity / face morphogenesis / Costimulation by the CD28 family / triglyceride metabolic process / ERBB signaling pathway / Signal regulatory protein family interactions / organ growth / platelet formation / megakaryocyte development / negative regulation of type I interferon production / peptide hormone receptor binding / Platelet sensitization by LDL / CTLA4 inhibitory signaling / PI-3K cascade:FGFR2 / Interleukin-20 family signaling / PI-3K cascade:FGFR3 / Interleukin-6 signaling / STAT5 activation downstream of FLT3 ITD mutants / PI-3K cascade:FGFR4 / Prolactin receptor signaling / MAPK3 (ERK1) activation / PI-3K cascade:FGFR1 / PECAM1 interactions / regulation of cell adhesion mediated by integrin / MAPK1 (ERK2) activation / regulation of type I interferon-mediated signaling pathway / Bergmann glial cell differentiation / neurotrophin TRK receptor signaling pathway / inner ear development / phosphoprotein phosphatase activity / platelet-derived growth factor receptor signaling pathway / non-membrane spanning protein tyrosine phosphatase activity / PI3K Cascade / RET signaling / peptidyl-tyrosine dephosphorylation / Interleukin-3, Interleukin-5 and GM-CSF signaling / Regulation of IFNA/IFNB signaling / fibroblast growth factor receptor signaling pathway / regulation of protein-containing complex assembly / ephrin receptor signaling pathway / PD-1 signaling / GAB1 signalosome / Activated NTRK2 signals through FRS2 and FRS3 / negative regulation of insulin secretion / Regulation of IFNG signaling / Signaling by CSF3 (G-CSF) / positive regulation of insulin receptor signaling pathway / cell adhesion molecule binding / FRS-mediated FGFR2 signaling / FRS-mediated FGFR3 signaling / Signaling by FLT3 ITD and TKD mutants / FRS-mediated FGFR4 signaling / homeostasis of number of cells within a tissue / GPVI-mediated activation cascade / Tie2 Signaling / FRS-mediated FGFR1 signaling / FLT3 Signaling / T cell costimulation / cellular response to epidermal growth factor stimulus / phosphotyrosine residue binding / protein dephosphorylation / positive regulation of interferon-beta production / hormone-mediated signaling pathway / protein tyrosine kinase binding / Downstream signal transduction / positive regulation of mitotic cell cycle / axonogenesis / protein-tyrosine-phosphatase / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / protein tyrosine phosphatase activity / DNA damage checkpoint signaling / integrin-mediated signaling pathway / positive regulation of D-glucose import / Negative regulation of FGFR2 signaling / Negative regulation of FGFR3 signaling / Negative regulation of FGFR4 signaling / insulin receptor binding / Negative regulation of FGFR1 signaling / Spry regulation of FGF signaling / brain development / epidermal growth factor receptor signaling pathway
Similarity search - Function

Biological species

HOMO SAPIENS (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.5 Å

Authors

Bohm, K. / Schuetz, A. / Roske, Y. / Heinemann, U.

Citation

Journal: Chemmedchem / Year: 2015
Title: Selective Inhibitors of the Protein Tyrosine Phosphatase Shp2 Block Cellular Motility and Growth of Cancer Cells in Vitro and in Vivo.
Authors: Grosskopf, S. / Eckert, C. / Arkona, C. / Radetzki, S. / Bohm, K. / Heinemann, U. / Wolber, G. / Von Kries, J. / Birchmeier, W. / Rademann, J.

History

Deposition	Feb 4, 2013	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Apr 23, 2014	Provider: repository / Type: Initial release
Revision 1.1	Apr 29, 2015	Group: Database references
Revision 1.2	May 13, 2015	Group: Database references
Revision 1.3	Dec 20, 2023	Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	3zm3.cif.gz	127.3 KB	Display	PDBx/mmCIF format
PDB format	pdb3zm3.ent.gz	100.2 KB	Display	PDB format
PDBx/mmJSON format	3zm3.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	3zm3_validation.pdf.gz	426.4 KB	Display	wwPDB validaton report
Full document	3zm3_full_validation.pdf.gz	432.4 KB	Display
Data in XML	3zm3_validation.xml.gz	14.6 KB	Display
Data in CIF	3zm3_validation.cif.gz	21.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/zm/3zm3 ftp://data.pdbj.org/pub/pdb/validation_reports/zm/3zm3	HTTPS FTP

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Related structure data

Related structure data	3zm0C 3zm1C 3zm2C 3b7oS C: citing same article (ref.) S: Starting model for refinement
Similar structure data	6zyv-2 4o8m-1 6bai-d 4nq8-1 4pdd-1 4n15-d 4n8y-1 2xhs-d 6b95-d 6s4u-2 Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#148 - Apr 2012 Ras Protein similarity (11) #60 - Dec 2004 Ubiquitin similarity (10) #126 - Jun 2010 Epidermal Growth Factor similarity (15) #43 - Jul 2003 Src Tyrosine Kinase similarity (9) #236 - Aug 2019 Cyclin and Cyclin-dependent Kinase similarity (2) #52 - Apr 2004 Growth Hormone similarity (1) #122 - Feb 2010 Enhanceosome similarity (7) #134 - Feb 2011 Integrin similarity (1) #195 - Mar 2016 RAF Protein Kinases similarity (10) #149 - May 2012 Leptin similarity (1) #128 - Aug 2010 Interferons similarity (2) #145 - Jan 2012 Messenger RNA Capping similarity (5) #225 - Sep 2018 Phytase similarity (5) #224 - Aug 2018 Legumain similarity (1) #56 - Aug 2004 Caspases similarity (1) #98 - Feb 2008 Small Interfering RNA similarity (1) #204 - Dec 2016 PD-1 similarity (1) #63 - Mar 2005 T-Cell Receptor similarity (1) #239 - Nov 2019 Phospholipase A2 similarity (1) #28 - Apr 2002 Anthrax Toxin similarity (1) #214 - Oct 2017 Chimeric Antigen Receptors similarity (1) #247 - Jul 2020 Myelin-associated Glycoprotein similarity (1) #245 - May 2020 Spliceosomes similarity (1) #222 - Jun 2018 Proteins and Nanoparticles similarity (1) #169 - Jan 2014 HIV Envelope Glycoprotein similarity (1) #209 - May 2017 Tissue Transglutaminase and Celiac Disease similarity (1) #62 - Feb 2005 Major Histocompatibility Complex similarity (1) #68 - Aug 2005 Neurotrophins similarity (1) #267 - Mar 2022 Vascular Endothelial Growth Factor (VegF similarity (1) #143 - Nov 2011 Toll-like Receptors similarity (1) #234 - Jun 2019 MDM2 and Cancer similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#148 - Apr 2012
Ras Protein
similarity (11)
#60 - Dec 2004
Ubiquitin
similarity (10)
#126 - Jun 2010
Epidermal Growth Factor
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#43 - Jul 2003
Src Tyrosine Kinase
similarity (9)
#236 - Aug 2019
Cyclin and Cyclin-dependent Kinase
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#52 - Apr 2004
Growth Hormone
similarity (1)
#122 - Feb 2010
Enhanceosome
similarity (7)
#134 - Feb 2011
Integrin
similarity (1)
#195 - Mar 2016
RAF Protein Kinases
similarity (10)
#149 - May 2012
Leptin
similarity (1)
#128 - Aug 2010
Interferons
similarity (2)
#145 - Jan 2012
Messenger RNA Capping
similarity (5)
#225 - Sep 2018
Phytase
similarity (5)
#224 - Aug 2018
Legumain
similarity (1)
#56 - Aug 2004
Caspases
similarity (1)
#98 - Feb 2008
Small Interfering RNA
similarity (1)
#204 - Dec 2016
PD-1
similarity (1)
#63 - Mar 2005
T-Cell Receptor
similarity (1)
#239 - Nov 2019
Phospholipase A2
similarity (1)
#28 - Apr 2002
Anthrax Toxin
similarity (1)
#214 - Oct 2017
Chimeric Antigen Receptors
similarity (1)
#247 - Jul 2020
Myelin-associated Glycoprotein
similarity (1)
#245 - May 2020
Spliceosomes
similarity (1)
#222 - Jun 2018
Proteins and Nanoparticles
similarity (1)
#169 - Jan 2014
HIV Envelope Glycoprotein
similarity (1)
#209 - May 2017
Tissue Transglutaminase and Celiac Disease
similarity (1)
#62 - Feb 2005
Major Histocompatibility Complex
similarity (1)
#68 - Aug 2005
Neurotrophins
similarity (1)
#267 - Mar 2022
Vascular Endothelial Growth Factor (VegF
similarity (1)
#143 - Nov 2011
Toll-like Receptors
similarity (1)
#234 - Jun 2019
MDM2 and Cancer
similarity (1)

Deposited unit

A: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11

33.2 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	40.190, 42.091, 49.386
Angle α, β, γ (deg.)	71.99, 81.09, 75.36
Int Tables number	1
Space group name H-M	P1

#1: Protein	TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11 / PROTEIN-TYROSINE PHOSPHATASE 1D / PTP-1D / PROTEIN-TYROSINE PHOSPHATASE 2C / PTP-2C / SH-PTP2 / SHP- ...PROTEIN-TYROSINE PHOSPHATASE 1D / PTP-1D / PROTEIN-TYROSINE PHOSPHATASE 2C / PTP-2C / SH-PTP2 / SHP-2 / SHP2 / SH-PTP3 Mass: 33163.660 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 248-527 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PT7HT (MODIFIED PET) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): SCS1 ROSETTA T1R / References: UniProt: Q06124, protein-tyrosine-phosphatase
#2: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 221 / Source method: isolated from a natural source / Formula: H₂O

#1: Protein

TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11 / PROTEIN-TYROSINE PHOSPHATASE 1D / PTP-1D / PROTEIN-TYROSINE PHOSPHATASE 2C / PTP-2C / SH-PTP2 / SHP- ...

Mass: 33163.660 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 248-527
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

HOMO SAPIENS (human) / Plasmid: PT7HT (MODIFIED PET) / Production host:

ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): SCS1 ROSETTA T1R / References: UniProt: Q06124, protein-tyrosine-phosphatase

#2: Water

ChemComp-HOH / water

Mass: 18.015 Da / Num. of mol.: 221 / 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: 2.31 Å³/Da / Density % sol: 46.84 % / Description: NONE
Crystal grow	Details: 16-22% (W/V) PEG3350, 0.1-0.2 M SODIUM CITRATE

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9184
Detector	Type: MARRESEARCH / Detector: CCD / Date: Feb 26, 2009
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9184 Å / Relative weight: 1
Reflection	Resolution: 1.5→20 Å / Num. obs: 39749 / % possible obs: 83 % / Observed criterion σ(I): 0 / Redundancy: 2.5 % / R_merge(I) obs: 0.04 / Net I/σ(I): 13.8
Reflection shell	Resolution: 1.5→1.59 Å / R_merge(I) obs: 0.04 / Mean I/σ(I) obs: 3.4 / % possible all: 50.7

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0019	refinement
XDS		data reduction
XSCALE		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3B7O

3b7o

Resolution: 1.5→19.53 Å / Cor.coef. F_o:F_c: 0.948 / Cor.coef. F_o:F_c free: 0.932 / SU B: 2.755 / SU ML: 0.055 / Cross valid method: THROUGHOUT / ESU R: 0.087 / ESU R Free: 0.09 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 255-262 AND 314-321 ARE DISORDERED.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.22747	2126	5.1 %	RANDOM
R_work	0.19056	-	-	-
obs	0.19249	39569	87.76 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 14.745 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	1.14 Å²	-0.14 Å²	-0.22 Å²
2-	-	-0.52 Å²	0.45 Å²
3-	-	-	-0.75 Å²

Refinement step

Cycle: LAST / Resolution: 1.5→19.53 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	2185	0	0	221	2406

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.024	0.022	2275
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	2.012	1.935	3081
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.133	5	276
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	33.987	23.782	119
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.248	15	413
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	17.027	15	19
X-RAY DIFFRACTION	r_chiral_restr	0.152	0.2	329
X-RAY DIFFRACTION	r_gen_planes_refined	0.012	0.02	1744
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.245	0.2	1099
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.316	0.2	1554
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.138	0.2	164
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.242	0.2	41
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.092	0.2	11
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	1.549	2	1383
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	2.126	3	2196
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	3.65	4.5	1026
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	5.058	6	879
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

LS refinement shell

Resolution: 1.5→1.539 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.282	94	-
R_work	0.233	1699	-
obs	-	-	51.24 %

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	4.0807	-2.7416	-4.3656	4.371	1.895	8.167	-0.0441	-0.0424	-0.0731	-0.1295	-0.0272	-0.1402	0.0322	0.168	0.0713	0.0632	-0.0125	0.002	0.013	0.0314	0.0289	22.0798	24.9049	48.9359
2	2.8788	0.5279	-0.5188	2.0654	0.1956	3.3565	0.1262	-0.0625	-0.1596	0.0042	-0.0737	-0.2064	0.5343	0.2935	-0.0525	0.1012	0.0569	-0.0271	-0.0003	-0.0113	0.0183	27.5353	18.5125	20.9283
3	0.3033	0.1178	-0.337	0.0514	-0.3319	7.4985	0.0006	0.0174	-0.005	0.0405	-0.0323	-0.0399	0.3478	0.2205	0.0317	0.0882	0.0104	-0.0157	0.0196	-0.0141	0.0103	20.3803	22.5587	7.9809
4	3.0329	-1.944	-1.2257	1.9455	0.4617	3.3715	-0.0381	-0.0639	-0.223	0.1807	0.0726	0.3804	0.1831	-0.4939	-0.0345	0.0434	-0.0288	0.0159	0.0445	0.0078	0.0561	13.6337	26.3646	25.8946
5	6.6016	0.4508	-3.1782	0.8328	0.407	4.8907	-0.0053	0.0191	-0.1097	-0.0179	0.0253	0.0362	0.0936	-0.0106	-0.02	0.0218	0.0075	0.0073	0.0066	0.0132	0.0311	19.5878	29.9379	24.5635
6	7.0883	-0.931	5.9422	7.372	4.5132	8.847	0.0714	0.3163	-0.0659	-0.4124	0.0748	-0.4457	-0.0891	0.6422	-0.1461	0.03	0.0203	0.0488	0.0556	0.0126	0.0463	30.3	32.0171	13.8399
7	1.5783	0.0801	-0.3679	1.7057	0.9636	1.8028	-0.0238	0.0713	-0.0625	-0.1025	-0.0257	0.0623	0.147	-0.0568	0.0495	0.039	-0.0034	-0.0039	0.0217	0.0052	0.0237	16.6412	33.6912	15.0871
8	9.3813	-1.159	-1.2321	0.3405	0.4293	1.3685	-0.0622	-0.3327	-0.0632	-0.0441	0.0276	-0.1806	-0.0045	0.2749	0.0347	-0.0075	-0.0016	0.0034	0.0535	0.0185	0.0541	33.0009	38.7144	26.4561
9	1.6981	-1.8926	0.5534	5.2163	-1.5899	1.7795	0.0285	0.0235	0.0958	-0.0604	-0.0808	-0.2021	-0.157	0.2153	0.0523	0.0159	-0.029	0.0116	0.066	0.0109	0.0398	27.6573	42.6197	17.2808
10	1.9005	-2.3498	-1.3243	24.6867	10.5429	12.2734	0.1367	0.0781	-0.0998	-0.138	-0.3148	-0.3682	-0.0848	0.0675	0.1781	0.0153	-0.0181	0.0369	0.0389	0.0331	0.0398	22.7433	47.6007	8.5652
11	0.5624	-0.1205	0.1295	3.2449	0.3212	2.838	-0.0081	0.0203	0.0261	-0.0347	-0.0212	-0.0345	-0.2875	-0.0021	0.0292	0.0413	-0.0166	0.0074	0.0326	0.0123	0.0619	20.4766	46.6415	18.0167
12	4.9532	-0.3446	-0.6532	7.9554	-0.4915	7.1956	0.1049	0.6077	-0.1081	-0.8423	-0.2717	0.4179	0.4363	-0.5114	0.1668	0.0692	0.0006	-0.0219	0.0687	-0.0076	-0.0061	14.4273	40.1634	7.4443
13	1.9164	-0.2473	1.0088	2.93	-0.3693	4.09	-0.0654	0.2258	0.0446	-0.0689	0.0101	0.0519	-0.18	0.0667	0.0554	0.008	0.0077	0.0211	0.0281	0.0088	0.0457	18.4978	42.942	21.6466
14	7.6458	-0.6841	-0.4618	6.8026	-0.1354	12.7946	-0.0763	-0.047	0.2475	0.0753	-0.043	-0.435	0.1225	0.5043	0.1192	0.0435	-0.0145	-0.0255	0.0629	-0.0015	0.0727	31.2147	39.9087	39.5885
15	4.9588	-0.359	4.1606	1.6232	-0.0224	5.825	-0.1233	-0.1826	0.1338	0.0311	0.0534	0.0801	-0.1632	-0.3359	0.0699	0.0314	0.0151	0.0066	0.0217	0.0125	0.0157	15.1494	43.1515	34.737
16	0.8713	-0.3778	0.2172	0.7139	-0.2175	1.459	-0.0039	0.0009	0.0032	0.0182	0.0386	0.0892	-0.0021	-0.1116	-0.0347	0.0175	-0.0118	0.0037	0.0218	0.0069	0.0359	15.7597	34.4529	29.8977
17	5.5605	4.0664	-3.4953	9.9287	-5.819	10.8024	-0.0509	-0.2936	-0.0557	0.1587	0.1053	0.1697	0.3427	-0.3773	-0.0544	-0.0268	0.0567	0.0608	0.1264	0.0439	0.0371	5.2136	33.7002	43.6713
18	1.6298	-0.1893	-0.6613	1.3328	0.4354	6.6778	-0.0353	-0.1883	-0.0118	0.0777	0.0673	0.1753	0.1901	-0.3742	-0.032	0.0467	-0.0075	-0.0059	0.0101	0.0167	0.0283	17.0852	22.8647	37.7215
19	9.5292	3.9157	2.7116	6.9992	3.5999	6.4581	-0.0784	0.2201	-0.1816	0.1088	0.2065	-0.1796	0.2127	0.3776	-0.1281	0.0474	0.0055	0.0005	0.0054	0.0109	0.0118	27.6574	27.8739	38.3167
20	4.8354	-1.4795	-0.2418	3.8547	-0.6197	2.4676	-0.0893	-0.2648	0.2466	0.2959	0.1215	0.1714	-0.1692	-0.2774	-0.0322	0.0512	0.0197	0.0121	0.046	-0.0058	0.0051	17.6012	37.0427	45.6963

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	244 - 254
2	X-RAY DIFFRACTION	2	A	255 - 288
3	X-RAY DIFFRACTION	3	A	289 - 303
4	X-RAY DIFFRACTION	4	A	304 - 325
5	X-RAY DIFFRACTION	5	A	326 - 332
6	X-RAY DIFFRACTION	6	A	333 - 338
7	X-RAY DIFFRACTION	7	A	339 - 353
8	X-RAY DIFFRACTION	8	A	354 - 365
9	X-RAY DIFFRACTION	9	A	366 - 374
10	X-RAY DIFFRACTION	10	A	375 - 379
11	X-RAY DIFFRACTION	11	A	380 - 400
12	X-RAY DIFFRACTION	12	A	401 - 408
13	X-RAY DIFFRACTION	13	A	409 - 423
14	X-RAY DIFFRACTION	14	A	424 - 431
15	X-RAY DIFFRACTION	15	A	432 - 444
16	X-RAY DIFFRACTION	16	A	445 - 478
17	X-RAY DIFFRACTION	17	A	479 - 486
18	X-RAY DIFFRACTION	18	A	487 - 502
19	X-RAY DIFFRACTION	19	A	503 - 510
20	X-RAY DIFFRACTION	20	A	511 - 525

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