PDB-4qqg: Crystal structure of an N-terminal HTATIP fragment

ID or keywords:

Entry

Database: PDB / ID: 4qqg

Title

Crystal structure of an N-terminal HTATIP fragment

Components

Histone acetyltransferase KAT5

Keywords

TRANSFERASE / Structural Genomics Consortium / SGC

Function / homology

Function and homology information

peptide crotonyltransferase activity / histone H2AK5 acetyltransferase activity / histone H2A acetyltransferase activity / peptidyl-lysine acetylation / positive regulation of protein acetylation / positive regulation of mitotic sister chromatid segregation / piccolo histone acetyltransferase complex / histone H4K16 acetyltransferase activity / peptide butyryltransferase activity / Sensing of DNA Double Strand Breaks ...peptide crotonyltransferase activity / histone H2AK5 acetyltransferase activity / histone H2A acetyltransferase activity / peptidyl-lysine acetylation / positive regulation of protein acetylation / positive regulation of mitotic sister chromatid segregation / piccolo histone acetyltransferase complex / histone H4K16 acetyltransferase activity / peptide butyryltransferase activity / Sensing of DNA Double Strand Breaks / lipid droplet disassembly / peptide 2-hydroxyisobutyryltransferase activity / positive regulation of triglyceride biosynthetic process / positive regulation of attachment of mitotic spindle microtubules to kinetochore / sperm DNA condensation / peptide lactyltransferase (CoA-dependent) activity / histone H4 acetyltransferase activity / Swr1 complex / positive regulation of circadian rhythm / Impaired BRCA2 binding to PALB2 / regulation of double-strand break repair / positive regulation of innate immune response / positive regulation of aggrephagy / Cardiogenesis / regulation of hematopoietic stem cell differentiation / neural tube development / positive regulation of regulatory T cell differentiation / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / negative regulation of interleukin-2 production / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Resolution of D-loop Structures through Holliday Junction Intermediates / HDR through Single Strand Annealing (SSA) / mitotic spindle pole / DNA repair-dependent chromatin remodeling / acetyltransferase activity / response to ionizing radiation / Impaired BRCA2 binding to RAD51 / NuA4 histone acetyltransferase complex / histone acetyltransferase activity / establishment of mitotic spindle orientation / Presynaptic phase of homologous DNA pairing and strand exchange / protein-lysine-acetyltransferase activity / spermatid development / positive regulation of myoblast differentiation / negative regulation of double-strand break repair via homologous recombination / histone acetyltransferase / cellular response to glucose starvation / positive regulation of double-strand break repair via homologous recombination / neurogenesis / positive regulation of autophagy / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / nucleotide-excision repair / DNA damage response, signal transduction by p53 class mediator / cellular response to estradiol stimulus / Nonhomologous End-Joining (NHEJ) / cellular response to glucose stimulus / Formation of the beta-catenin:TCF transactivating complex / double-strand break repair via homologous recombination / G2/M DNA damage checkpoint / kinetochore / HDR through Homologous Recombination (HRR) / DNA Damage/Telomere Stress Induced Senescence / cellular senescence / nucleosome / double-strand break repair / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / site of double-strand break / HATs acetylate histones / Processing of DNA double-strand break ends / regulation of apoptotic process / transcription regulator complex / Estrogen-dependent gene expression / Regulation of TP53 Activity through Phosphorylation / DNA-binding transcription factor binding / proteasome-mediated ubiquitin-dependent protein catabolic process / transcription coactivator activity / regulation of cell cycle / innate immune response / negative regulation of DNA-templated transcription / apoptotic process / DNA damage response / chromatin binding / positive regulation of DNA-templated transcription / chromatin / nucleolus / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus / cytoplasm / cytosol
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.8 Å

Authors

Liu, Y. / Tempel, W. / Wernimont, A.K. / Dobrovetsky, E. / Bountra, C. / Arrowsmith, C.H. / Edwards, A.M. / Min, J. / Structural Genomics Consortium (SGC)

Citation

Journal: FEBS Lett. / Year: 2018
Title: Structural and histone binding studies of the chromo barrel domain of TIP60.
Authors: Zhang, Y. / Lei, M. / Yang, X. / Feng, Y. / Yang, Y. / Loppnau, P. / Li, Y. / Yang, Y. / Min, J. / Liu, Y.

History

Deposition	Jun 27, 2014	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jul 9, 2014	Provider: repository / Type: Initial release
Revision 1.1	Apr 18, 2018	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2	May 2, 2018	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.3	Sep 20, 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 / struct_ref_seq_dif 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_alt_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 / _struct_ref_seq_dif.details

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	4qqg.cif.gz	210.8 KB	Display	PDBx/mmCIF format
PDB format	pdb4qqg.ent.gz	170 KB	Display	PDB format
PDBx/mmJSON format	4qqg.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qq/4qqg ftp://data.pdbj.org/pub/pdb/validation_reports/qq/4qqg	HTTPS FTP

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Related structure data

Related structure data	2ekoS S: Starting model for refinement
Similar structure data	7jh1-d 4esr-1 1o5u-1 4c26-d 6wav-2 7klr-d 6v2s-2 6log-d 4efo-2 2kug-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) 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

2ekoS

S: Starting model for refinement

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#172 - Apr 2014 RecA and Rad51 similarity (5) #85 - Jan 2007 Importins similarity (1) #122 - Feb 2010 Enhanceosome similarity (1) #150 - Jun 2012 Sliding Clamps similarity (2) #43 - Jul 2003 Src Tyrosine Kinase similarity (1) #146 - Feb 2012 Aminoglycoside Antibiotics similarity (1) #55 - Jul 2004 DNA Ligase similarity (1) #67 - Jul 2005 TATA-Binding Protein similarity (1) #97 - Jan 2008 Circadian Clock Proteins similarity (1) #241 - Jan 2020 Twenty Years of Molecules similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#172 - Apr 2014
RecA and Rad51
similarity (5)
#85 - Jan 2007
Importins
similarity (1)
#122 - Feb 2010
Enhanceosome
similarity (1)
#150 - Jun 2012
Sliding Clamps
similarity (2)
#43 - Jul 2003
Src Tyrosine Kinase
similarity (1)
#146 - Feb 2012
Aminoglycoside Antibiotics
similarity (1)
#55 - Jul 2004
DNA Ligase
similarity (1)
#67 - Jul 2005
TATA-Binding Protein
similarity (1)
#97 - Jan 2008
Circadian Clock Proteins
similarity (1)
#241 - Jan 2020
Twenty Years of Molecules
similarity (1)

Deposited unit

A: Histone acetyltransferase KAT5

B: Histone acetyltransferase KAT5

C: Histone acetyltransferase KAT5

D: Histone acetyltransferase KAT5

E: Histone acetyltransferase KAT5

F: Histone acetyltransferase KAT5

G: Histone acetyltransferase KAT5

67.3 kDa, 7 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Histone acetyltransferase KAT5

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

2

B: Histone acetyltransferase KAT5

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

3

C: Histone acetyltransferase KAT5

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

4

D: Histone acetyltransferase KAT5

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

5

E: Histone acetyltransferase KAT5

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

6

F: Histone acetyltransferase KAT5

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

7

G: Histone acetyltransferase KAT5

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

Unit cell

Length a, b, c (Å)	43.544, 59.986, 101.638
Angle α, β, γ (deg.)	90.000, 100.650, 90.000
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	Beg label alt-ID
1	1	GLU	GLU	PRO	PRO	A	A	3 - 71	4 - 72
2	1	GLU	GLU	PRO	PRO	B	B	3 - 71	4 - 72
1	2	ALA	ALA	PHE	PHE	A	A	2 - 70	3 - 71
2	2	ALA	ALA	PHE	PHE	C	C	2 - 70	3 - 71	A
1	3	GLU	GLU	PHE	PHE	A	A	3 - 70	4 - 71
2	3	GLU	GLU	PHE	PHE	D	D	3 - 70	4 - 71
1	4	MET	MET	PHE	PHE	A	A	1 - 70	2 - 71
2	4	MET	MET	PHE	PHE	E	E	1 - 70	2 - 71
1	5	GLU	GLU	PHE	PHE	A	A	3 - 70	4 - 71
2	5	GLU	GLU	PHE	PHE	F	F	3 - 70	4 - 71
1	6	MET	MET	PHE	PHE	A	A	1 - 70	2 - 71
2	6	MET	MET	PHE	PHE	G	G	1 - 70	2 - 71
1	7	GLU	GLU	LYS	LYS	B	B	3 - 72	4 - 73
2	7	GLU	GLU	LYS	LYS	C	C	3 - 72	4 - 73
1	8	GLU	GLU	PRO	PRO	B	B	3 - 71	4 - 72
2	8	GLU	GLU	PRO	PRO	D	D	3 - 71	4 - 72
1	9	GLU	GLU	LYS	LYS	B	B	3 - 72	4 - 73
2	9	GLU	GLU	LYS	LYS	E	E	3 - 72	4 - 73
1	10	GLU	GLU	LYS	LYS	B	B	3 - 72	4 - 73
2	10	GLU	GLU	LYS	LYS	F	F	3 - 72	4 - 73
1	11	GLU	GLU	LYS	LYS	B	B	3 - 72	4 - 73
2	11	GLU	GLU	LYS	LYS	G	G	3 - 72	4 - 73
1	12	GLU	GLU	PHE	PHE	C	C	3 - 70	4 - 71
2	12	GLU	GLU	PHE	PHE	D	D	3 - 70	4 - 71
1	13	ALA	ALA	LYS	LYS	C	C	2 - 72	3 - 73	A
2	13	ALA	ALA	LYS	LYS	E	E	2 - 72	3 - 73
1	14	GLU	GLU	LYS	LYS	C	C	3 - 72	4 - 73
2	14	GLU	GLU	LYS	LYS	F	F	3 - 72	4 - 73
1	15	ALA	ALA	PRO	PRO	C	C	2 - 71	3 - 72	A
2	15	ALA	ALA	PRO	PRO	G	G	2 - 71	3 - 72
1	16	GLU	GLU	PHE	PHE	D	D	3 - 70	4 - 71
2	16	GLU	GLU	PHE	PHE	E	E	3 - 70	4 - 71
1	17	GLU	GLU	PHE	PHE	D	D	3 - 70	4 - 71
2	17	GLU	GLU	PHE	PHE	F	F	3 - 70	4 - 71
1	18	GLU	GLU	PHE	PHE	D	D	3 - 70	4 - 71
2	18	GLU	GLU	PHE	PHE	G	G	3 - 70	4 - 71
1	19	GLU	GLU	PRO	PRO	E	E	3 - 71	4 - 72
2	19	GLU	GLU	PRO	PRO	F	F	3 - 71	4 - 72
1	20	MET	MET	PRO	PRO	E	E	1 - 71	2 - 72
2	20	MET	MET	PRO	PRO	G	G	1 - 71	2 - 72
1	21	GLU	GLU	PRO	PRO	F	F	3 - 71	4 - 72
2	21	GLU	GLU	PRO	PRO	G	G	3 - 71	4 - 72

NCS ensembles :

Details

AUTHORS HAVE INDICATED THAT THE BIOLOGICAL UNIT IS UNKNOWN.

#1: Protein	Histone acetyltransferase KAT5 / 60 kDa Tat-interactive protein / Tip60 / Histone acetyltransferase HTATIP / HIV-1 Tat interactive ...60 kDa Tat-interactive protein / Tip60 / Histone acetyltransferase HTATIP / HIV-1 Tat interactive protein / Lysine acetyltransferase 5 / cPLA(2)-interacting protein Mass: 9613.062 Da / Num. of mol.: 7 / Fragment: unp residues 1-80 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KAT5, HTATIP, TIP60 / Plasmid: pET28-MHL / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-V2R-pRARE2 / References: UniProt: Q92993, histone acetyltransferase
#2: Chemical	ChemComp-UNX / UNKNOWN ATOM OR ION Num. of mol.: 13 / Source method: obtained synthetically

#1: Protein

Histone acetyltransferase KAT5 / 60 kDa Tat-interactive protein / Tip60 / Histone acetyltransferase HTATIP / HIV-1 Tat interactive ...

Mass: 9613.062 Da / Num. of mol.: 7 / Fragment: unp residues 1-80
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Homo sapiens (human) / Gene: KAT5, HTATIP, TIP60 / Plasmid: pET28-MHL / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-V2R-pRARE2 / References: UniProt: Q92993, histone acetyltransferase

#2: Chemical

ChemComp-UNX / UNKNOWN ATOM OR ION

Num. of mol.: 13 / Source method: obtained synthetically

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 1.94 Å³/Da / Density % sol: 36.55 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion Details: 20% PEG3350, 0.2 M calcium acetate. The protein sample may have been treated with trypsin, VAPOR DIFFUSION, temperature 291K

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 19-ID / Wavelength: 1.283 Å

Detector

Type: adsc q315 / Detector: CCD / Date: Feb 11, 2012

Radiation

Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1.283 Å / Relative weight: 1

Reflection

Resolution: 2.8→42.26 Å / Num. obs: 12878 / % possible obs: 99.9 % / Redundancy: 3.7 % / R_merge(I) obs: 0.134 / Net I/σ(I): 10.1

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Mean I/σ(I) obs	Num. measured all	Num. unique all	% possible all
2.8-2.95	3.7	0.565	2.8	6923	1879	99.9
8.85-42.26	3.4	0.034	24	1466	429	98.6

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
Aimless	0.3.6	data scaling
MOLREP		phasing
REFMAC		refinement
PDB_EXTRACT	3.14	data extraction
XDS		data reduction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: pdb entry 2EKO

2eko

Resolution: 2.8→99.89 Å / Cor.coef. F_o:F_c: 0.91 / Cor.coef. F_o:F_c free: 0.884 / WR_factor R_free: 0.2245 / WR_factor R_work: 0.1991 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.7826 / SU B: 43.352 / SU ML: 0.378 / SU R Cruickshank DPI: 0.3992 / SU R_free: 0.4265 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.426 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: molecular replacement coordinates, based on an nmr model, were initially processed by the program phaser, before input to MOLREP. PARROT was used for NCS- and solvent-based density ...

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2595	771	6 %	THIN SHELLS (SFTOOLS)
R_work	0.2257	-	-	-
obs	0.2277	12868	99.74 %	-

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 max: 112.49 Å² / B_iso mean: 36.3753 Å² / B_iso min: 2.31 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-3.69 Å²	0 Å²	-1.77 Å²
2-	-	3.72 Å²	-0 Å²
3-	-	-	0.59 Å²

Refinement step

Cycle: LAST / Resolution: 2.8→99.89 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	3956	0	13	0	3969

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.014	0.019	4070
X-RAY DIFFRACTION	r_bond_other_d	0.009	0.02	3853
X-RAY DIFFRACTION	r_angle_refined_deg	1.384	1.958	5520
X-RAY DIFFRACTION	r_angle_other_deg	1.389	3	8806
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.196	5	484
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	22.814	23.713	202
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.27	15	694
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	21.877	15	32
X-RAY DIFFRACTION	r_chiral_restr	0.074	0.2	609
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.021	4533
X-RAY DIFFRACTION	r_gen_planes_other	0.006	0.02	939
X-RAY DIFFRACTION	r_mcbond_it	1.282	1.687	1960
X-RAY DIFFRACTION	r_mcbond_other	1.282	1.687	1961
X-RAY DIFFRACTION	r_mcangle_it	2.177	2.528	2437

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	A	3693	0.11
1	2	B	3693	0.11
2	1	A	3837	0.1
2	2	C	3837	0.1
3	1	A	3800	0.1
3	2	D	3800	0.1
4	1	A	3878	0.11
4	2	E	3878	0.11
5	1	A	3594	0.11
5	2	F	3594	0.11
6	1	A	3723	0.13
6	2	G	3723	0.13
7	1	B	3796	0.09
7	2	C	3796	0.09
8	1	B	3732	0.08
8	2	D	3732	0.08
9	1	B	3734	0.09
9	2	E	3734	0.09
10	1	B	3544	0.1
10	2	F	3544	0.1
11	1	B	3580	0.11
11	2	G	3580	0.11
12	1	C	3681	0.11
12	2	D	3681	0.11
13	1	C	3903	0.08
13	2	E	3903	0.08
14	1	C	3652	0.1
14	2	F	3652	0.1
15	1	C	3669	0.11
15	2	G	3669	0.11
16	1	D	3731	0.09
16	2	E	3731	0.09
17	1	D	3576	0.1
17	2	F	3576	0.1
18	1	D	3641	0.11
18	2	G	3641	0.11
19	1	E	3610	0.11
19	2	F	3610	0.11
20	1	E	3723	0.12
20	2	G	3723	0.12
21	1	F	3593	0.12
21	2	G	3593	0.12

LS refinement shell

Resolution: 2.8→2.873 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.383	113	-
R_work	0.343	858	-
all	-	971	-
obs	-	-	99.9 %

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	6.7502	-1.0258	1.0512	1.5801	0.8601	6.7437	-0.2087	-0.0652	0.2557	-0.0233	0.0804	0.045	-0.3386	-0.0299	0.1283	0.1263	-0.013	-0.0087	0.016	0.0215	0.0637	36.268	30.3838	-3.9589
2	2.1332	-0.0113	3.6616	6.0278	-0.5189	8.3575	-0.0387	0.0194	0.2122	0.2553	0.0282	0.0579	-0.2643	-0.2108	0.0106	0.0924	0.0458	0.0126	0.0833	0.0037	0.1108	41.6444	1.5694	29.6134
3	6.5404	-0.1522	1.8432	3.2673	2.2871	7.3166	-0.0946	-0.2384	-0.2227	0.2698	-0.0083	-0.0264	0.3324	-0.0871	0.1029	0.1275	0.0206	0.0227	0.0842	0.0124	0.0669	12.5345	28.2248	54.1374
4	3.5811	-0.4246	2.0155	3.1497	-0.7547	5.0117	-0.0751	0.1804	0.1018	-0.4057	-0.0214	-0.128	-0.1185	0.4206	0.0965	0.1492	0.0142	-0.0194	0.2132	-0.1012	0.1453	26.1368	28.4324	23.3913
5	6.204	0.6602	1.1611	5.2684	0.7783	6.0549	-0.0788	-0.253	0.1504	0.3623	0.1945	0.0242	0.2181	0.2647	-0.1156	0.1755	0.0119	-0.0292	0.0388	-0.0158	0.0207	49.9184	27.2063	13.1172
6	6.9835	-1.047	1.6988	4.5588	-2.3681	6.0467	-0.0277	-0.0788	-0.2089	-0.14	-0.027	-0.1325	0.2281	0.2101	0.0546	0.0919	0.0156	0.0076	0.115	-0.0441	0.1396	25.7739	56.7966	15.0826
7	6.0683	1.4628	2.1082	5.5189	-1.954	2.8856	0.0151	-0.0783	-0.0617	0.1353	-0.015	0.0724	-0.1455	0.0235	-0	0.1527	0.001	0.0063	0.0994	-0.0404	0.0281	37.8325	31.0412	41.3517

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 71
2	X-RAY DIFFRACTION	2	B	3 - 72
3	X-RAY DIFFRACTION	3	C	2 - 72
4	X-RAY DIFFRACTION	4	D	3 - 71
5	X-RAY DIFFRACTION	5	E	1 - 72
6	X-RAY DIFFRACTION	6	F	3 - 72
7	X-RAY DIFFRACTION	7	G	0 - 72

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