PDB-2jjd: Protein Tyrosine Phosphatase, Receptor Type, E isoform

ID or keywords:

Entry

Database: PDB / ID: 2jjd

Title

Protein Tyrosine Phosphatase, Receptor Type, E isoform

Components

RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

Keywords

HYDROLASE / TRANSMEMBRANE / PHOSPHOPROTEIN / PROTEIN PHOSPHATASE / CONSORTIUM / STRUCTURAL / PHOSPHATASE / GLYCOPROTEIN / SGC / PTPRE / MEMBRANE / GENOMICS

Function / homology

Function and homology information

transmembrane receptor protein tyrosine phosphatase activity / negative regulation of insulin receptor signaling pathway / protein dephosphorylation / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / nucleus / plasma membrane / cytoplasm
Similarity search - Function

Biological species

HOMO SAPIENS (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.2 Å

Authors

Elkins, J.M. / Ugochukwu, E. / Alfano, I. / Barr, A.J. / Bunkoczi, G. / King, O.N.F. / Filippakopoulos, P. / Savitsky, P. / Salah, E. / Pike, A. ...

Citation

Journal: Cell(Cambridge,Mass.) / Year: 2009
Title: Large-Scale Structural Analysis of the Classical Human Protein Tyrosine Phosphatome.
Authors: Barr, A.J. / Ugochukwu, E. / Lee, W.H. / King, O.N.F. / Filippakopoulos, P. / Alfano, I. / Savitsky, P. / Burgess-Brown, N.A. / Muller, S. / Knapp, S.

History

Deposition	Mar 31, 2008	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Apr 8, 2008	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Refinement description / Version format compliance
Revision 1.2	Jun 6, 2012	Group: Other

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	2jjd.cif.gz	583.5 KB	Display	PDBx/mmCIF format
PDB format	pdb2jjd.ent.gz	475.4 KB	Display	PDB format
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Validation report

Summary document	2jjd_validation.pdf.gz	488.5 KB	Display	wwPDB validaton report
Full document	2jjd_full_validation.pdf.gz	541.4 KB	Display
Data in XML	2jjd_validation.xml.gz	103.7 KB	Display
Data in CIF	2jjd_validation.cif.gz	143.1 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/jj/2jjd ftp://data.pdbj.org/pub/pdb/validation_reports/jj/2jjd	HTTPS FTP

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Related structure data

Related structure data	2ahsC 2b49C 2cfvC 2cjzC 2gjtC 2h4vC 2i75C 2nlkC 2nz6C 2oc3C 2ooqC 2p6xC 2pa5C 2qepC 3b7oC C: citing same article (ref.)
Similar structure data	6ebg-d 4lkm-d 3buu-d 1lar-2 3rmv-1 3dw0-d 1jny-1 4bl5-4 5eg3-d 4eiv-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) Search similar-shape structures by Omokage search (details) 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

Related structure data

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#126 - Jun 2010 Epidermal Growth Factor similarity (12) #145 - Jan 2012 Messenger RNA Capping similarity (5) #225 - Sep 2018 Phytase similarity (5)

Deposited unit

A: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

B: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

C: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

D: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

E: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

F: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

hetero molecules

418 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

hetero molecules

defined by author&software
69.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

hetero molecules

defined by author&software
69.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

hetero molecules

defined by author&software
69.6 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

hetero molecules

defined by author&software
69.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

5

E: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

hetero molecules

defined by author&software
69.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

6

F: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON

hetero molecules

defined by author&software
69.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	126.020, 123.616, 219.116
Angle α, β, γ (deg.)	90.00, 91.13, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Refine code	Auth asym-ID	Auth seq-ID
1	1	1	1	A	111 - 142
2	1	1	1	B	111 - 142
3	1	1	1	C	111 - 142
4	1	1	1	D	111 - 142
5	1	1	1	E	111 - 142
6	1	1	1	F	111 - 142
1	1	2	1	A	152 - 235
2	1	2	1	B	152 - 235
3	1	2	1	C	152 - 235
4	1	2	1	D	152 - 235
5	1	2	1	E	152 - 235
6	1	2	1	F	152 - 235
1	2	2	1	A	242 - 303
2	2	2	1	B	242 - 303
3	2	2	1	C	242 - 303
4	2	2	1	D	242 - 303
5	2	2	1	E	242 - 303
6	2	2	1	F	242 - 303
1	3	2	1	A	313 - 359
2	3	2	1	B	313 - 359
3	3	2	1	C	313 - 359
4	3	2	1	D	313 - 359
5	3	2	1	E	313 - 359
6	3	2	1	F	313 - 359
1	4	2	1	A	366 - 373
2	4	2	1	B	366 - 373
3	4	2	1	C	366 - 373
4	4	2	1	D	366 - 373
5	4	2	1	E	366 - 373
6	4	2	1	F	366 - 373
1	5	2	1	A	387 - 423
2	5	2	1	B	387 - 423
3	5	2	1	C	387 - 423
4	5	2	1	D	387 - 423
5	5	2	1	E	387 - 423
6	5	2	1	F	387 - 423
1	1	3	4	A	143 - 151
2	1	3	4	B	143 - 151
3	1	3	4	C	143 - 151
4	1	3	4	D	143 - 151
5	1	3	4	E	143 - 151
6	1	3	4	F	143 - 151
1	2	3	4	A	236 - 241
2	2	3	4	B	236 - 241
3	2	3	4	C	236 - 241
4	2	3	4	D	236 - 241
5	2	3	4	E	236 - 241
6	2	3	4	F	236 - 241
1	3	3	4	A	304 - 312
2	3	3	4	B	304 - 312
3	3	3	4	C	304 - 312
4	3	3	4	D	304 - 312
5	3	3	4	E	304 - 312
6	3	3	4	F	304 - 312
1	4	3	4	A	360 - 365
2	4	3	4	B	360 - 365
3	4	3	4	C	360 - 365
4	4	3	4	D	360 - 365
5	4	3	4	E	360 - 365
6	4	3	4	F	360 - 365
1	5	3	4	A	374 - 386
2	5	3	4	B	374 - 386
3	5	3	4	C	374 - 386
4	5	3	4	D	374 - 386
5	5	3	4	E	374 - 386
6	5	3	4	F	374 - 386
1	1	4	1	A	424 - 432
2	1	4	1	B	424 - 432
3	1	4	1	C	424 - 432
4	1	4	1	D	424 - 432
5	1	4	1	E	424 - 432
6	1	4	1	F	424 - 432
1	2	4	1	A	444 - 574
2	2	4	1	B	444 - 574
3	2	4	1	C	444 - 574
4	2	4	1	D	444 - 574
5	2	4	1	E	444 - 574
6	2	4	1	F	444 - 574
1	3	4	1	A	585 - 619
2	3	4	1	B	585 - 619
3	3	4	1	C	585 - 619
4	3	4	1	D	585 - 619
5	3	4	1	E	585 - 619
6	3	4	1	F	585 - 619
1	4	4	4	A	626 - 691
2	4	4	4	B	626 - 691
3	4	4	4	C	626 - 691
4	4	4	4	D	626 - 691
5	4	4	4	E	626 - 691
6	4	4	4	F	626 - 691
1	1	5	4	A	433 - 443
2	1	5	4	B	433 - 443
3	1	5	4	C	433 - 443
4	1	5	4	D	433 - 443
5	1	5	4	E	433 - 443
6	1	5	4	F	433 - 443
1	2	5	4	A	575 - 584
2	2	5	4	B	575 - 584
3	2	5	4	C	575 - 584
4	2	5	4	D	575 - 584
5	2	5	4	E	575 - 584
6	2	5	4	F	575 - 584
1	3	5	4	A	620 - 625
2	3	5	4	B	620 - 625
3	3	5	4	C	620 - 625
4	3	5	4	D	620 - 625
5	3	5	4	E	620 - 625
6	3	5	4	F	620 - 625

NCS ensembles :

ID
1
2
3
4
5

NCS oper:

ID	Code	Matrix	Vector
1	given	(-0.9858, -0.04493, -0.16179), (-0.04436, 0.99899, -0.00714), (0.16195, 0.00013, -0.9868)	-61.88751, 55.96052, -99.51503
2	given	(0.33799, 0.01381, 0.94105), (-0.09495, 0.99529, 0.01949), (-0.93635, -0.09594, 0.33771)	57.70181, 12.23866, -118.23937
3	given	(-0.4735, 0.00167, -0.88079), (-0.05678, 0.99786, 0.03242), (0.87896, 0.06536, -0.47239)	-118.28419, 80.18089, 0.21715
4	given	(-0.46401, -0.00026, 0.88583), (-0.02436, 0.99963, -0.01247), (-0.88549, -0.02736, -0.46385)	-56.26374, 40.01058, -105.86585
5	given	(0.59319, 0.01957, -0.80482), (-0.04287, 0.99905, -0.0073), (0.80392, 0.03883, 0.59347)	11.48757, 97.01311, -3.3822

#1: Protein	RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON / PROTEIN-TYROSINE PHOSPHATASE EPSILON / R-PTP -EPSILON / PROTEIN TYROSINE PHOSPHATASE / RECEPTOR ...PROTEIN-TYROSINE PHOSPHATASE EPSILON / R-PTP -EPSILON / PROTEIN TYROSINE PHOSPHATASE / RECEPTOR TYPE / E ISOFORM Mass: 69600.383 Da / Num. of mol.: 6 / Fragment: RESIDUES 107-697 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PNIC-CH / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): R3-PRARE2 / References: UniProt: P23469, protein-tyrosine-phosphatase
#2: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Cl
Sequence details	THERE IS A MUTATION OF GLU->GLY AT RESIDUE 581 (CLONING ERROR)

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 5.13 Å³/Da / Density % sol: 75.84 % / Description: NONE
Crystal grow	pH: 6.5 / Details: 1.60 M MGSO4, 0.1 M MES PH 6.5

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9537
Detector	Type: MARRESEARCH / Detector: CCD / Date: Mar 3, 2007
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9537 Å / Relative weight: 1
Reflection	Resolution: 3.2→34.65 Å / Num. obs: 373908 / % possible obs: 98.7 % / Observed criterion σ(I): 0 / Redundancy: 3.4 % / R_merge(I) obs: 0.14 / Net I/σ(I): 9
Reflection shell	Resolution: 3.2→3.37 Å / Redundancy: 2.5 % / R_merge(I) obs: 0.56 / Mean I/σ(I) obs: 1.5 / % possible all: 92.4

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Processing

Software

Name	Version	Classification
REFMAC	5.4.0066	refinement
MOSFLM		data reduction
SCALA		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 3.2→218.22 Å / Cor.coef. F_o:F_c: 0.911 / Cor.coef. F_o:F_c free: 0.884 / SU B: 41.207 / SU ML: 0.315 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 1.158 / ESU R Free: 0.4 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.256	5502	5 %	RANDOM
R_work	0.221	-	-	-
obs	0.223	104282	98.7 %	-

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: 49.37 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-3.9 Å²	0 Å²	2.51 Å²
2-	-	5.05 Å²	0 Å²
3-	-	-	-1.05 Å²

Refinement step

Cycle: LAST / Resolution: 3.2→218.22 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	23738	0	12	0	23750

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.01	0.021	24353
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	15151
X-RAY DIFFRACTION	r_angle_refined_deg	1.169	1.925	33330
X-RAY DIFFRACTION	r_angle_other_deg	0.871	3	36749
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.448	5	3199
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	29.21	22.587	924
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.566	15	3134
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.412	15	122
X-RAY DIFFRACTION	r_chiral_restr	0.063	0.2	3850
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.021	27893
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	5329
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
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
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
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	0.202	1.5	16133
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	0.396	2	25372
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	0.635	3	8220
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	1.044	4.5	7958
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

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	263	tight positional	0.02	0.05
1	2	B	263	tight positional	0.02	0.05
1	3	C	263	tight positional	0.02	0.05
1	4	D	263	tight positional	0.02	0.05
1	5	E	263	tight positional	0.02	0.05
1	6	F	263	tight positional	0.03	0.05
2	1	A	2530	tight positional	0.02	0.05
2	2	B	2530	tight positional	0.02	0.05
2	3	C	2530	tight positional	0.02	0.05
2	4	D	2530	tight positional	0.02	0.05
2	5	E	2530	tight positional	0.02	0.05
2	6	F	2530	tight positional	0.02	0.05
4	1	A	1959	tight positional	0.22	0.05
4	2	B	1959	tight positional	0.21	0.05
4	3	C	1959	tight positional	0.21	0.05
4	4	D	1959	tight positional	0.2	0.05
4	5	E	1959	tight positional	0.23	0.05
4	6	F	1959	tight positional	0.22	0.05
3	1	A	480	medium positional	0.33	0.5
3	2	B	480	medium positional	0.46	0.5
3	3	C	480	medium positional	0.39	0.5
3	4	D	480	medium positional	0.29	0.5
3	5	E	480	medium positional	0.29	0.5
3	6	F	480	medium positional	0.28	0.5
4	1	A	813	medium positional	0.2	0.5
4	2	B	813	medium positional	0.2	0.5
4	3	C	813	medium positional	0.21	0.5
4	4	D	813	medium positional	0.19	0.5
4	5	E	813	medium positional	0.18	0.5
4	6	F	813	medium positional	0.2	0.5
5	1	A	201	medium positional	0.45	0.5
5	2	B	201	medium positional	0.31	0.5
5	3	C	201	medium positional	0.47	0.5
5	4	D	201	medium positional	0.29	0.5
5	5	E	201	medium positional	0.28	0.5
5	6	F	201	medium positional	0.43	0.5
1	1	A	263	tight thermal	0.03	0.5
1	2	B	263	tight thermal	0.03	0.5
1	3	C	263	tight thermal	0.03	0.5
1	4	D	263	tight thermal	0.03	0.5
1	5	E	263	tight thermal	0.02	0.5
1	6	F	263	tight thermal	0.03	0.5
2	1	A	2530	tight thermal	0.03	0.5
2	2	B	2530	tight thermal	0.03	0.5
2	3	C	2530	tight thermal	0.03	0.5
2	4	D	2530	tight thermal	0.03	0.5
2	5	E	2530	tight thermal	0.03	0.5
2	6	F	2530	tight thermal	0.03	0.5
4	1	A	1959	tight thermal	0.21	0.5
4	2	B	1959	tight thermal	0.18	0.5
4	3	C	1959	tight thermal	0.19	0.5
4	4	D	1959	tight thermal	0.19	0.5
4	5	E	1959	tight thermal	0.19	0.5
4	6	F	1959	tight thermal	0.17	0.5
3	1	A	480	medium thermal	0.2	2
3	2	B	480	medium thermal	0.19	2
3	3	C	480	medium thermal	0.2	2
3	4	D	480	medium thermal	0.17	2
3	5	E	480	medium thermal	0.19	2
3	6	F	480	medium thermal	0.16	2
4	1	A	813	medium thermal	0.19	2
4	2	B	813	medium thermal	0.18	2
4	3	C	813	medium thermal	0.21	2
4	4	D	813	medium thermal	0.18	2
4	5	E	813	medium thermal	0.19	2
4	6	F	813	medium thermal	0.18	2
5	1	A	201	medium thermal	0.19	2
5	2	B	201	medium thermal	0.19	2
5	3	C	201	medium thermal	0.18	2
5	4	D	201	medium thermal	0.15	2
5	5	E	201	medium thermal	0.14	2
5	6	F	201	medium thermal	0.17	2

LS refinement shell

Resolution: 3.2→3.28 Å / Total num. of bins used: 20 /

	R_factor	Num. reflection
R_free	0.361	345
R_work	0.341	6911

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	3.4274	1.0342	0.6041	3.0759	1.2706	5.9558	0.0979	0.0805	-0.14	-0.129	0.0969	0.0642	-0.1058	-0.1098	-0.1947	-0.2943	0.0275	-0.161	-0.1424	-0.0531	-0.2083	-70.346	-37.431	-47.336
2	3.5588	-0.0495	-0.447	4.4475	-0.065	2.2247	0.1226	0.2468	0.0343	-0.2388	-0.07	-0.0932	-0.1175	-0.1285	-0.0526	-0.2045	0.0111	-0.0692	-0.1025	0.0224	-0.3329	-45.061	-9.379	-52.817
3	2.9247	-0.5911	0.1649	1.923	-0.0245	5.0314	0.1158	-0.0383	-0.1331	-0.0299	-0.0301	-0.1124	0.1081	0.2497	-0.0858	-0.2804	-0.0344	-0.1529	-0.1193	0.0295	-0.1959	16.841	21.973	-63.574
4	2.7916	-0.4554	-0.316	5.3675	-0.0071	2.594	0.0809	-0.5188	-0.0594	0.3483	-0.0106	0.1883	-0.364	-0.0386	-0.0703	-0.1935	0.001	-0.0583	0.104	-0.0975	-0.3125	-8.406	48.749	-54.652
5	6.2276	1.027	0.4133	1.8048	-0.1329	3.9585	-0.2099	-0.3416	-0.394	0.0394	-0.0409	-0.0285	-0.0314	-0.1976	0.2508	-0.1333	0.0418	-0.0112	-0.1927	-0.015	-0.2217	-11.643	-19.226	-64.864
6	2.7921	-0.0281	0.0828	4.9908	0.4486	3.4117	-0.0844	0.2196	0.1669	-0.2256	-0.1285	0.3012	-0.0748	-0.4227	0.2129	-0.174	0.0282	-0.1645	-0.0197	0.0414	-0.3554	-7.354	5.886	-92.97
7	6.2634	-1.2985	-0.3299	2.7945	0.3874	4.1099	-0.3056	0.3536	-0.5247	0.0835	0.0371	-0.0102	0.0932	0.1535	0.2685	-0.2281	-0.0041	0.0044	-0.0105	0.0198	-0.1222	-43.774	45.631	-42.281
8	2.4947	-0.3852	-0.1287	4.9117	0.0828	4.0755	0.0223	-0.3424	0.1321	0.3348	-0.2145	-0.2479	0.0091	0.4396	0.1923	-0.1636	-0.0626	-0.1445	0.0987	-0.065	-0.3134	-50.627	71.495	-14.995
9	3.593	0.0308	-0.7208	2.3378	-0.7983	3.8645	-0.0727	-0.2737	0.0841	0.1355	0.1232	0.0774	0.1779	0.1478	-0.0505	-0.1129	0.0401	-0.1244	-0.0598	-0.0517	-0.33	-65.023	5.193	-20.658
10	3.6158	0.0707	0.6374	4.2741	0.0434	2.541	0.0854	-0.4253	0.5346	0.0337	-0.0012	0.2315	-0.0149	-0.0924	-0.0841	-0.2611	0.0457	-0.0779	-0.0842	-0.0907	-0.1947	-81.967	32.307	-41.433
11	3.4932	0.1591	-0.6285	2.8273	0.947	4.1885	-0.0401	0.2009	0.1129	-0.2214	0.0978	-0.0882	0.0989	-0.0554	-0.0576	-0.0662	0.0184	-0.1635	-0.1632	-0.004	-0.3571	6.792	63.321	-89.564
12	3.5196	-0.134	0.1641	5.3808	-0.1881	3.2071	0.2306	0.4438	0.3789	-0.3006	-0.0332	-0.4179	-0.0637	0.3186	-0.1974	-0.255	-0.0563	-0.0848	0.1033	0.0132	-0.1948	26.924	89.699	-71.046

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	112 - 406
2	X-RAY DIFFRACTION	2	A	425 - 691
3	X-RAY DIFFRACTION	3	B	111 - 406
4	X-RAY DIFFRACTION	4	B	425 - 691
5	X-RAY DIFFRACTION	5	C	111 - 406
6	X-RAY DIFFRACTION	6	C	425 - 691
7	X-RAY DIFFRACTION	7	D	112 - 406
8	X-RAY DIFFRACTION	8	D	425 - 691
9	X-RAY DIFFRACTION	9	E	111 - 406
10	X-RAY DIFFRACTION	10	E	425 - 691
11	X-RAY DIFFRACTION	11	F	111 - 406
12	X-RAY DIFFRACTION	12	F	425 - 691

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