PDB-6j2z: AtFKBP53 N-terminal Nucleoplasmin Domain

ID or keywords:

Entry

Database: PDB / ID: 6j2z

Title

AtFKBP53 N-terminal Nucleoplasmin Domain

Components

Peptidyl-prolyl cis-trans isomerase FKBP53

Keywords

CHAPERONE / FKBP / FKBP-nucleoplasmin / histone chaperone

Function / homology

Function and homology information

peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / nucleosome assembly / histone binding / nucleolus / nucleus
Similarity search - Function

Biological species

Arabidopsis thaliana (thale cress)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.4 Å

Authors

Singh, A.K. / Vasudevan, D.

Citation

Journal: Nucleic Acids Res. / Year: 2020
Title: AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains.
Authors: Singh, A.K. / Datta, A. / Jobichen, C. / Luan, S. / Vasudevan, D.

History

Deposition	Jan 3, 2019	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Dec 4, 2019	Provider: repository / Type: Initial release
Revision 1.1	Dec 18, 2019	Group: Database references / Category: citation / citation_author Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed ..._citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2	Mar 4, 2020	Group: Database references / Category: citation Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.3	Nov 22, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / 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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Validation report

Summary document	6j2z_validation.pdf.gz	507.9 KB	Display	wwPDB validaton report
Full document	6j2z_full_validation.pdf.gz	532.1 KB	Display
Data in XML	6j2z_validation.xml.gz	33 KB	Display
Data in CIF	6j2z_validation.cif.gz	47 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/j2/6j2z ftp://data.pdbj.org/pub/pdb/validation_reports/j2/6j2z	HTTPS FTP

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Related structure data

Related structure data	6j2mC 1k5jS C: citing same article (ref.) S: Starting model for refinement
Similar structure data	1z50-d 3t30-2 1z4y-d 6ziv-6 3t30-1 7d6b-1 1uyq-d 1oim-1 1z4z-d 2e40-1 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

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#32 - Aug 2002 Chaperones similarity (1) #163 - Jul 2013 HIV Capsid similarity (1) #245 - May 2020 Spliceosomes similarity (1)

Deposited unit

F: Peptidyl-prolyl cis-trans isomerase FKBP53

G: Peptidyl-prolyl cis-trans isomerase FKBP53

H: Peptidyl-prolyl cis-trans isomerase FKBP53

I: Peptidyl-prolyl cis-trans isomerase FKBP53

J: Peptidyl-prolyl cis-trans isomerase FKBP53

A: Peptidyl-prolyl cis-trans isomerase FKBP53

B: Peptidyl-prolyl cis-trans isomerase FKBP53

C: Peptidyl-prolyl cis-trans isomerase FKBP53

D: Peptidyl-prolyl cis-trans isomerase FKBP53

E: Peptidyl-prolyl cis-trans isomerase FKBP53

121 kDa, 10 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

F: Peptidyl-prolyl cis-trans isomerase FKBP53

G: Peptidyl-prolyl cis-trans isomerase FKBP53

H: Peptidyl-prolyl cis-trans isomerase FKBP53

I: Peptidyl-prolyl cis-trans isomerase FKBP53

J: Peptidyl-prolyl cis-trans isomerase FKBP53

defined by author&software
Evidence: gel filtration
60.6 kDa, 5 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

A: Peptidyl-prolyl cis-trans isomerase FKBP53

B: Peptidyl-prolyl cis-trans isomerase FKBP53

C: Peptidyl-prolyl cis-trans isomerase FKBP53

D: Peptidyl-prolyl cis-trans isomerase FKBP53

E: Peptidyl-prolyl cis-trans isomerase FKBP53

defined by author&software
60.6 kDa, 5 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	56.590, 97.390, 96.430
Angle α, β, γ (deg.)	90.00, 94.12, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: _ / Refine code: _

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	PHE	PHE	GLU	GLU	G	B	3 - 96	3 - 96
2	1	PHE	PHE	GLU	GLU	H	C	3 - 96	3 - 96
1	2	PHE	PHE	GLU	GLU	G	B	3 - 96	3 - 96
2	2	PHE	PHE	GLU	GLU	I	D	3 - 96	3 - 96
1	3	PHE	PHE	GLU	GLU	G	B	3 - 96	3 - 96
2	3	PHE	PHE	GLU	GLU	J	E	3 - 96	3 - 96
1	4	PHE	PHE	GLU	GLU	G	B	3 - 96	3 - 96
2	4	PHE	PHE	GLU	GLU	A	F	3 - 96	3 - 96
1	5	PHE	PHE	GLU	GLU	G	B	3 - 96	3 - 96
2	5	PHE	PHE	GLU	GLU	B	G	3 - 96	3 - 96
1	6	PHE	PHE	GLU	GLU	G	B	3 - 96	3 - 96
2	6	PHE	PHE	GLU	GLU	C	H	3 - 96	3 - 96
1	7	PHE	PHE	GLU	GLU	G	B	3 - 96	3 - 96
2	7	PHE	PHE	GLU	GLU	D	I	3 - 96	3 - 96
1	8	PHE	PHE	GLU	GLU	G	B	3 - 96	3 - 96
2	8	PHE	PHE	GLU	GLU	E	J	3 - 96	3 - 96
1	9	GLY	GLY	TYR	TYR	H	C	2 - 97	2 - 97
2	9	GLY	GLY	TYR	TYR	I	D	2 - 97	2 - 97
1	10	PHE	PHE	LEU	LEU	H	C	3 - 95	3 - 95
2	10	PHE	PHE	LEU	LEU	J	E	3 - 95	3 - 95
1	11	GLY	GLY	TYR	TYR	H	C	2 - 97	2 - 97
2	11	GLY	GLY	TYR	TYR	A	F	2 - 97	2 - 97
1	12	GLY	GLY	GLU	GLU	H	C	2 - 96	2 - 96
2	12	GLY	GLY	GLU	GLU	B	G	2 - 96	2 - 96
1	13	GLY	GLY	TYR	TYR	H	C	2 - 97	2 - 97
2	13	GLY	GLY	TYR	TYR	C	H	2 - 97	2 - 97
1	14	GLY	GLY	TYR	TYR	H	C	2 - 97	2 - 97
2	14	GLY	GLY	TYR	TYR	D	I	2 - 97	2 - 97
1	15	GLY	GLY	TYR	TYR	H	C	2 - 97	2 - 97
2	15	GLY	GLY	TYR	TYR	E	J	2 - 97	2 - 97
1	16	PHE	PHE	LEU	LEU	I	D	3 - 95	3 - 95
2	16	PHE	PHE	LEU	LEU	J	E	3 - 95	3 - 95
1	17	GLY	GLY	TYR	TYR	I	D	2 - 97	2 - 97
2	17	GLY	GLY	TYR	TYR	A	F	2 - 97	2 - 97
1	18	GLY	GLY	GLU	GLU	I	D	2 - 96	2 - 96
2	18	GLY	GLY	GLU	GLU	B	G	2 - 96	2 - 96
1	19	GLY	GLY	TYR	TYR	I	D	2 - 97	2 - 97
2	19	GLY	GLY	TYR	TYR	C	H	2 - 97	2 - 97
1	20	GLY	GLY	TYR	TYR	I	D	2 - 97	2 - 97
2	20	GLY	GLY	TYR	TYR	D	I	2 - 97	2 - 97
1	21	GLY	GLY	TYR	TYR	I	D	2 - 97	2 - 97
2	21	GLY	GLY	TYR	TYR	E	J	2 - 97	2 - 97
1	22	PHE	PHE	LEU	LEU	J	E	3 - 95	3 - 95
2	22	PHE	PHE	LEU	LEU	A	F	3 - 95	3 - 95
1	23	PHE	PHE	LEU	LEU	J	E	3 - 95	3 - 95
2	23	PHE	PHE	LEU	LEU	B	G	3 - 95	3 - 95
1	24	PHE	PHE	LEU	LEU	J	E	3 - 95	3 - 95
2	24	PHE	PHE	LEU	LEU	C	H	3 - 95	3 - 95
1	25	PHE	PHE	LEU	LEU	J	E	3 - 95	3 - 95
2	25	PHE	PHE	LEU	LEU	D	I	3 - 95	3 - 95
1	26	PHE	PHE	LEU	LEU	J	E	3 - 95	3 - 95
2	26	PHE	PHE	LEU	LEU	E	J	3 - 95	3 - 95
1	27	GLY	GLY	GLU	GLU	A	F	2 - 96	2 - 96
2	27	GLY	GLY	GLU	GLU	B	G	2 - 96	2 - 96
1	28	GLY	GLY	TYR	TYR	A	F	2 - 97	2 - 97
2	28	GLY	GLY	TYR	TYR	C	H	2 - 97	2 - 97
1	29	GLY	GLY	TYR	TYR	A	F	2 - 97	2 - 97
2	29	GLY	GLY	TYR	TYR	D	I	2 - 97	2 - 97
1	30	GLY	GLY	TYR	TYR	A	F	2 - 97	2 - 97
2	30	GLY	GLY	TYR	TYR	E	J	2 - 97	2 - 97
1	31	GLY	GLY	GLU	GLU	B	G	2 - 96	2 - 96
2	31	GLY	GLY	GLU	GLU	C	H	2 - 96	2 - 96
1	32	GLY	GLY	GLU	GLU	B	G	2 - 96	2 - 96
2	32	GLY	GLY	GLU	GLU	D	I	2 - 96	2 - 96
1	33	GLY	GLY	GLU	GLU	B	G	2 - 96	2 - 96
2	33	GLY	GLY	GLU	GLU	E	J	2 - 96	2 - 96
1	34	GLY	GLY	TYR	TYR	C	H	2 - 97	2 - 97
2	34	GLY	GLY	TYR	TYR	D	I	2 - 97	2 - 97
1	35	GLY	GLY	TYR	TYR	C	H	2 - 97	2 - 97
2	35	GLY	GLY	TYR	TYR	E	J	2 - 97	2 - 97
1	36	GLY	GLY	TYR	TYR	D	I	2 - 97	2 - 97
2	36	GLY	GLY	TYR	TYR	E	J	2 - 97	2 - 97

NCS ensembles :

#1: Protein	Peptidyl-prolyl cis-trans isomerase FKBP53 / PPIase FKBP53 / FK506-binding protein 53 / AtFKBP53 / Immunophilin FKBP53 / Rotamase Mass: 12111.609 Da / Num. of mol.: 10 / Fragment: nucleoplasmin domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: FKBP53, At4g25340, T30C3_20 / Plasmid: pET22b(+) / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q93ZG9, peptidylprolyl isomerase
#2: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 38 / Source method: isolated from a natural source / Formula: H₂O

#1: Protein

Peptidyl-prolyl cis-trans isomerase FKBP53 / PPIase FKBP53 / FK506-binding protein 53 / AtFKBP53 / Immunophilin FKBP53 / Rotamase

Mass: 12111.609 Da / Num. of mol.: 10 / Fragment: nucleoplasmin domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Arabidopsis thaliana (thale cress) / Gene: FKBP53, At4g25340, T30C3_20 / Plasmid: pET22b(+) / Production host:

Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q93ZG9, peptidylprolyl isomerase

#2: Water

ChemComp-HOH / water

Mass: 18.015 Da / Num. of mol.: 38 / 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: 2.38 Å³/Da / Density % sol: 43.79 % / Description: rod-shaped
Crystal grow	Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 0.2 M DL-Malic acid (pH 7.0), 25% (w/v) PEG 3350

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.9537 Å
Detector	Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 28, 2016
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9537 Å / Relative weight: 1
Reflection	Resolution: 2.4→68.53 Å / Num. obs: 40837 / % possible obs: 100 % / Redundancy: 6.6 % / B_iso Wilson estimate: 56.493 Å² / CC_1/2: 0.999 / R_merge(I) obs: 0.063 / R_pim(I) all: 0.029 / R_rim(I) all: 0.073 / Net I/σ(I): 16.5
Reflection shell	Resolution: 2.4→2.49 Å / Redundancy: 6.5 % / R_merge(I) obs: 0.509 / Mean I/σ(I) obs: 3.2 / Num. unique obs: 27924 / CC_1/2: 0.905 / R_pim(I) all: 0.24 / R_rim(I) all: 0.609 / % possible all: 100

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0241	refinement
PHENIX		refinement
iMOSFLM	7.1.1	data reduction
Aimless		data scaling
PHENIX		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1K5J

1k5j

Resolution: 2.4→68.53 Å / Cor.coef. F_o:F_c: 0.949 / Cor.coef. F_o:F_c free: 0.938 / SU B: 19.597 / SU ML: 0.206 / Cross valid method: THROUGHOUT / ESU R: 0.424 / ESU R Free: 0.245 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.23325	2033	5 %	RANDOM
R_work	0.204	-	-	-
obs	0.20538	38867	99.99 %	-

Solvent computation

Ion probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1.1 Å

Displacement parameters

B_iso mean: 69 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-1.33 Å²	0 Å²	-2.25 Å²
2-	-	0.47 Å²	0 Å²
3-	-	-	1.18 Å²

Refinement step

Cycle: 1 / Resolution: 2.4→68.53 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7179	0	0	38	7217

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.013	7336
X-RAY DIFFRACTION	r_bond_other_d	0.003	0.017	6806
X-RAY DIFFRACTION	r_angle_refined_deg	1.527	1.644	9934
X-RAY DIFFRACTION	r_angle_other_deg	1.182	1.581	16013
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	8.051	5	923
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	33.38	25.968	315
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.903	15	1277
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	12.11	15	10
X-RAY DIFFRACTION	r_chiral_restr	0.131	0.2	962
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.02	8058
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	1272
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	2.72	2.716	3734
X-RAY DIFFRACTION	r_mcbond_other	2.719	2.716	3733
X-RAY DIFFRACTION	r_mcangle_it	4.074	4.072	4643
X-RAY DIFFRACTION	r_mcangle_other	4.073	4.072	4644
X-RAY DIFFRACTION	r_scbond_it	3.265	3.055	3602
X-RAY DIFFRACTION	r_scbond_other	3.265	3.056	3603
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	4.877	4.458	5292
X-RAY DIFFRACTION	r_long_range_B_refined	7.038	31.791	7047
X-RAY DIFFRACTION	r_long_range_B_other	7.037	31.793	7048
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 / Type: interatomic distance / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	G	2310	0.13
1	2	H	2310	0.13
2	1	G	2329	0.13
2	2	I	2329	0.13
3	1	G	2275	0.14
3	2	J	2275	0.14
4	1	G	2282	0.13
4	2	A	2282	0.13
5	1	G	2327	0.12
5	2	B	2327	0.12
6	1	G	2329	0.12
6	2	C	2329	0.12
7	1	G	2328	0.11
7	2	D	2328	0.11
8	1	G	2336	0.11
8	2	E	2336	0.11
9	1	H	2654	0.09
9	2	I	2654	0.09
10	1	H	2507	0.12
10	2	J	2507	0.12
11	1	H	2616	0.1
11	2	A	2616	0.1
12	1	H	2632	0.09
12	2	B	2632	0.09
13	1	H	2640	0.1
13	2	C	2640	0.1
14	1	H	2603	0.11
14	2	D	2603	0.11
15	1	H	2665	0.09
15	2	E	2665	0.09
16	1	I	2511	0.12
16	2	J	2511	0.12
17	1	I	2667	0.09
17	2	A	2667	0.09
18	1	I	2613	0.11
18	2	B	2613	0.11
19	1	I	2659	0.1
19	2	C	2659	0.1
20	1	I	2631	0.1
20	2	D	2631	0.1
21	1	I	2664	0.08
21	2	E	2664	0.08
22	1	J	2526	0.11
22	2	A	2526	0.11
23	1	J	2564	0.12
23	2	B	2564	0.12
24	1	J	2541	0.12
24	2	C	2541	0.12
25	1	J	2477	0.13
25	2	D	2477	0.13
26	1	J	2523	0.12
26	2	E	2523	0.12
27	1	A	2634	0.09
27	2	B	2634	0.09
28	1	A	2668	0.09
28	2	C	2668	0.09
29	1	A	2614	0.1
29	2	D	2614	0.1
30	1	A	2637	0.11
30	2	E	2637	0.11
31	1	B	2658	0.09
31	2	C	2658	0.09
32	1	B	2622	0.1
32	2	D	2622	0.1
33	1	B	2649	0.1
33	2	E	2649	0.1
34	1	C	2647	0.09
34	2	D	2647	0.09
35	1	C	2659	0.1
35	2	E	2659	0.1
36	1	D	2647	0.1
36	2	E	2647	0.1

LS refinement shell

Resolution: 2.4→2.462 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.315	172	-
R_work	0.278	2869	-
obs	-	-	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	4.4913	-0.2779	0.3996	7.6296	1.5484	5.4217	0.2368	1.0609	-0.0219	-2.1854	0.046	-0.958	-0.3172	0.4722	-0.2828	0.7406	0.0853	0.1832	0.3798	-0.0731	0.3874	-2.85	-4.135	127.513
2	4.7378	-0.3978	0.46	4.3172	0.6408	4.9396	0.3021	0.2932	-0.0713	0.0571	0.1856	-1.8355	0.2617	1.0007	-0.4877	0.2913	0.1065	-0.0649	0.3166	-0.1804	0.9867	10.709	-8.852	141.571
3	5.5796	-1.1081	-0.2145	7.1448	1.5929	5.3187	0.1104	0.5746	0.3803	-1.1808	-0.2134	0.954	-0.5959	-0.7305	0.103	0.3187	0.1422	-0.1825	0.3029	-0.059	0.4494	-17.006	5.478	135.667
4	5.3747	-1.4208	0.615	5.3307	0.4187	5.0263	-0.3009	-0.982	0.3899	1.248	0.1295	0.6022	-0.2358	-0.6269	0.1714	0.4938	0.1227	-0.0097	0.3931	-0.1854	0.4263	-13.366	6.114	154.98
5	4.9919	-0.9035	0.8069	3.9591	1.7606	5.9065	-0.1045	-1.0224	0.3255	1.3841	0.2474	-0.7008	0.3094	0.3598	-0.1429	0.633	0.0881	-0.2954	0.3593	-0.0999	0.5326	3.648	-2.577	158.389
6	4.2776	-0.5886	0.278	4.0947	-0.5689	3.3225	-0.0295	-0.1617	0.1626	0.1	0.1233	0.7277	-0.2076	-0.328	-0.0938	0.0242	0.0136	-0.0239	0.0437	0.046	0.3122	-42.135	-13.439	102.871
7	5.0029	0.0375	0.5076	4.8239	-0.135	3.7804	-0.1544	0.8705	0.1218	-1.2506	0.2099	0.2315	-0.1993	-0.023	-0.0554	0.389	-0.0655	-0.1417	0.1711	0.0509	0.3015	-35.857	-15.311	84.454
8	4.6923	-0.1471	1.0148	5.8363	0.5402	3.9527	-0.0299	-0.9066	-0.1246	1.1369	0.058	0.0143	-0.0611	-0.2456	-0.0281	0.2525	-0.0065	-0.0775	0.1937	0.0937	0.2778	-28.936	-21.373	114.712
9	4.2808	0.3967	0.8749	5.5936	-0.3005	3.8752	0.0964	-0.1084	-0.3059	0.3177	-0.0305	-0.9071	0.1953	0.4047	-0.0659	0.0367	0.0179	-0.0742	0.0557	0.0396	0.5261	-14.197	-28.384	103.992
10	3.8806	-0.2668	1.1159	5.4131	0.6331	4.2628	0.0018	0.926	-0.2898	-1.1185	0.1847	-1.0534	-0.0285	0.7706	-0.1865	0.3635	-0.0176	0.1303	0.305	-0.0777	0.5126	-18.575	-24.728	84.987

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	F	2 - 96
2	X-RAY DIFFRACTION	2	G	3 - 96
3	X-RAY DIFFRACTION	3	H	2 - 97
4	X-RAY DIFFRACTION	4	I	2 - 97
5	X-RAY DIFFRACTION	5	J	3 - 96
6	X-RAY DIFFRACTION	6	A	2 - 97
7	X-RAY DIFFRACTION	7	B	2 - 98
8	X-RAY DIFFRACTION	8	C	2 - 97
9	X-RAY DIFFRACTION	9	D	2 - 97
10	X-RAY DIFFRACTION	10	E	2 - 97

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