PDB-7r3b: S-adenosylmethionine synthetase from Lactobacillus plantarum comp...

ID or keywords:

Entry

Database: PDB / ID: 7r3b

Title

S-adenosylmethionine synthetase from Lactobacillus plantarum complexed with AMPPNP, methionine and SAM

Components

S-adenosylmethionine synthase

Keywords

TRANSFERASE / Dihedral D2 symmetry / homotetramer A4 symmetry / isologous interfaces 2 / S-adenosylmethionine synthetase

Function / homology

Function and homology information

methionine adenosyltransferase / methionine adenosyltransferase activity / S-adenosylmethionine biosynthetic process / one-carbon metabolic process / magnesium ion binding / ATP binding / cytoplasm
Similarity search - Function

Biological species

Lactiplantibacillus plantarum (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.82 Å

Authors

Shahar, A. / Kleiner, D. / Bershtein, S. / Zarivach, R.

Funding support

United States, 1items

Citation

Journal: Protein Sci. / Year: 2022
Title: Evolution of homo-oligomerization of methionine S-adenosyltransferases is replete with structure-function constrains.
Authors: Kleiner, D. / Shapiro Tuchman, Z. / Shmulevich, F. / Shahar, A. / Zarivach, R. / Kosloff, M. / Bershtein, S.

History

Deposition	Feb 7, 2022	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jul 13, 2022	Provider: repository / Type: Initial release
Revision 1.1	Jan 31, 2024	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._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
Revision 1.2	Nov 13, 2024	Group: Structure summary / Category: pdbx_entry_details / Item: _pdbx_entry_details.has_protein_modification

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	7r3b_validation.pdf.gz	5.7 MB	Display	wwPDB validaton report
Full document	7r3b_full_validation.pdf.gz	5.8 MB	Display
Data in XML	7r3b_validation.xml.gz	105.1 KB	Display
Data in CIF	7r3b_validation.cif.gz	138.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/r3/7r3b ftp://data.pdbj.org/pub/pdb/validation_reports/r3/7r3b	HTTPS FTP

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Related structure data

Related structure data	7r2wC 1p7lS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	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	#253 - Jan 2021 Expressome similarity (1) #231 - Mar 2019 Measles Virus Proteins similarity (1) #81 - Sep 2006 Elongation Factors similarity (1) #108 - Dec 2008 Hsp90 similarity (1) #168 - Dec 2013 DNA Helicase similarity (1) #182 - Feb 2015 Insulin receptor similarity (1) #214 - Oct 2017 Chimeric Antigen Receptors similarity (1) #238 - Oct 2019 Ribonucleotide Reductase similarity (1) #43 - Jul 2003 Src Tyrosine Kinase similarity (1) #50 - Feb 2004 Glycolytic Enzymes similarity (1) #60 - Dec 2004 Ubiquitin similarity (1) #73 - Jan 2006 Topoisomerase similarity (1) #80 - Aug 2006 AAA+ Proteases similarity (1) #95 - Nov 2007 Multidrug Resistance Transporters similarity (1) #139 - Jul 2011 DNA Methyltransferase similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#253 - Jan 2021
Expressome
similarity (1)
#231 - Mar 2019
Measles Virus Proteins
similarity (1)
#81 - Sep 2006
Elongation Factors
similarity (1)
#108 - Dec 2008
Hsp90
similarity (1)
#168 - Dec 2013
DNA Helicase
similarity (1)
#182 - Feb 2015
Insulin receptor
similarity (1)
#214 - Oct 2017
Chimeric Antigen Receptors
similarity (1)
#238 - Oct 2019
Ribonucleotide Reductase
similarity (1)
#43 - Jul 2003
Src Tyrosine Kinase
similarity (1)
#50 - Feb 2004
Glycolytic Enzymes
similarity (1)
#60 - Dec 2004
Ubiquitin
similarity (1)
#73 - Jan 2006
Topoisomerase
similarity (1)
#80 - Aug 2006
AAA+ Proteases
similarity (1)
#95 - Nov 2007
Multidrug Resistance Transporters
similarity (1)
#139 - Jul 2011
DNA Methyltransferase
similarity (1)

Deposited unit

A: S-adenosylmethionine synthase

B: S-adenosylmethionine synthase

C: S-adenosylmethionine synthase

D: S-adenosylmethionine synthase

E: S-adenosylmethionine synthase

F: S-adenosylmethionine synthase

G: S-adenosylmethionine synthase

H: S-adenosylmethionine synthase

hetero molecules

353 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: S-adenosylmethionine synthase

B: S-adenosylmethionine synthase

C: S-adenosylmethionine synthase

D: S-adenosylmethionine synthase

hetero molecules

defined by author&software
Evidence: gel filtration
176 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: S-adenosylmethionine synthase

F: S-adenosylmethionine synthase

G: S-adenosylmethionine synthase

H: S-adenosylmethionine synthase

hetero molecules

defined by author&software
177 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	58.426, 110.927, 112.661
Angle α, β, γ (deg.)	93.82, 104.03, 99.59
Int Tables number	1
Space group name H-M	P1

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	GLU	GLU	ALA	ALA	A	A	3 - 393	3 - 393
2	1	GLU	GLU	ALA	ALA	B	B	3 - 393	3 - 393
1	2	ARG	ARG	ALA	ALA	A	A	4 - 393	4 - 393
2	2	ARG	ARG	ALA	ALA	C	C	4 - 393	4 - 393
1	3	ARG	ARG	ALA	ALA	A	A	4 - 393	4 - 393
2	3	ARG	ARG	ALA	ALA	D	D	4 - 393	4 - 393
1	4	GLU	GLU	ALA	ALA	A	A	3 - 393	3 - 393
2	4	GLU	GLU	ALA	ALA	E	E	3 - 393	3 - 393
1	5	HIS	HIS	ALA	ALA	A	A	5 - 393	5 - 393
2	5	HIS	HIS	ALA	ALA	F	F	5 - 393	5 - 393
1	6	ARG	ARG	ALA	ALA	A	A	4 - 393	4 - 393
2	6	ARG	ARG	ALA	ALA	G	G	4 - 393	4 - 393
1	7	GLU	GLU	ALA	ALA	A	A	3 - 393	3 - 393
2	7	GLU	GLU	ALA	ALA	H	H	3 - 393	3 - 393
1	8	ARG	ARG	ALA	ALA	B	B	4 - 393	4 - 393
2	8	ARG	ARG	ALA	ALA	C	C	4 - 393	4 - 393
1	9	ARG	ARG	ALA	ALA	B	B	4 - 393	4 - 393
2	9	ARG	ARG	ALA	ALA	D	D	4 - 393	4 - 393
1	10	GLU	GLU	ALA	ALA	B	B	3 - 393	3 - 393
2	10	GLU	GLU	ALA	ALA	E	E	3 - 393	3 - 393
1	11	HIS	HIS	ALA	ALA	B	B	5 - 393	5 - 393
2	11	HIS	HIS	ALA	ALA	F	F	5 - 393	5 - 393
1	12	ARG	ARG	ALA	ALA	B	B	4 - 393	4 - 393
2	12	ARG	ARG	ALA	ALA	G	G	4 - 393	4 - 393
1	13	GLU	GLU	ALA	ALA	B	B	3 - 393	3 - 393
2	13	GLU	GLU	ALA	ALA	H	H	3 - 393	3 - 393
1	14	ARG	ARG	LYS	LYS	C	C	4 - 395	4 - 395
2	14	ARG	ARG	LYS	LYS	D	D	4 - 395	4 - 395
1	15	ARG	ARG	LYS	LYS	C	C	4 - 395	4 - 395
2	15	ARG	ARG	LYS	LYS	E	E	4 - 395	4 - 395
1	16	HIS	HIS	ALA	ALA	C	C	5 - 393	5 - 393
2	16	HIS	HIS	ALA	ALA	F	F	5 - 393	5 - 393
1	17	ARG	ARG	PHE	PHE	C	C	4 - 394	4 - 394
2	17	ARG	ARG	PHE	PHE	G	G	4 - 394	4 - 394
1	18	ARG	ARG	ALA	ALA	C	C	4 - 393	4 - 393
2	18	ARG	ARG	ALA	ALA	H	H	4 - 393	4 - 393
1	19	ARG	ARG	PHE	PHE	D	D	4 - 394	4 - 394
2	19	ARG	ARG	PHE	PHE	E	E	4 - 394	4 - 394
1	20	HIS	HIS	PHE	PHE	D	D	5 - 394	5 - 394
2	20	HIS	HIS	PHE	PHE	F	F	5 - 394	5 - 394
1	21	ARG	ARG	PHE	PHE	D	D	4 - 394	4 - 394
2	21	ARG	ARG	PHE	PHE	G	G	4 - 394	4 - 394
1	22	ARG	ARG	ALA	ALA	D	D	4 - 393	4 - 393
2	22	ARG	ARG	ALA	ALA	H	H	4 - 393	4 - 393
1	23	HIS	HIS	ALA	ALA	E	E	5 - 393	5 - 393
2	23	HIS	HIS	ALA	ALA	F	F	5 - 393	5 - 393
1	24	ARG	ARG	ALA	ALA	E	E	4 - 393	4 - 393
2	24	ARG	ARG	ALA	ALA	G	G	4 - 393	4 - 393
1	25	GLU	GLU	ALA	ALA	E	E	3 - 393	3 - 393
2	25	GLU	GLU	ALA	ALA	H	H	3 - 393	3 - 393
1	26	HIS	HIS	PHE	PHE	F	F	5 - 394	5 - 394
2	26	HIS	HIS	PHE	PHE	G	G	5 - 394	5 - 394
1	27	HIS	HIS	ALA	ALA	F	F	5 - 393	5 - 393
2	27	HIS	HIS	ALA	ALA	H	H	5 - 393	5 - 393
1	28	ARG	ARG	ALA	ALA	G	G	4 - 393	4 - 393
2	28	ARG	ARG	ALA	ALA	H	H	4 - 393	4 - 393

NCS ensembles :

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Protein , 1 types, 8 molecules ABCDEFGH

#1: Protein	S-adenosylmethionine synthase / AdoMet synthase / MAT / Methionine adenosyltransferase Mass: 43526.738 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lactiplantibacillus plantarum (bacteria) Gene: metK, AVR83_15510, AYO51_09395, C7M36_00090, C7M40_01013, E3U93_09955, FEE41_07350, IV39_GL000589, Lp19_1604, Lp90_1155, LPJSA22_01228, Nizo2802_1764, SN35N_0475 Production host: Escherichia coli (E. coli) References: UniProt: A0A0G9F5E5, methionine adenosyltransferase

#1: Protein

S-adenosylmethionine synthase / AdoMet synthase / MAT / Methionine adenosyltransferase

Mass: 43526.738 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Lactiplantibacillus plantarum (bacteria)
Gene: metK, AVR83_15510, AYO51_09395, C7M36_00090, C7M40_01013, E3U93_09955, FEE41_07350, IV39_GL000589, Lp19_1604, Lp90_1155, LPJSA22_01228, Nizo2802_1764, SN35N_0475
Production host:

Escherichia coli (E. coli)
References: UniProt: A0A0G9F5E5, methionine adenosyltransferase

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Non-polymers , 7 types, 79 molecules

#2: Chemical	ChemComp-PHE / PHENYLALANINE Type: L-peptide linking / Mass: 165.189 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₉H₁₁NO₂ / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical	ChemComp-PPK / (DIPHOSPHONO)AMINOPHOSPHONIC ACID Mass: 256.970 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: H₆NO₉P₃ / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical	ChemComp-K / POTASSIUM ION Mass: 39.098 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: K / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical	ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER Mass: 506.196 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₀H₁₇N₆O₁₂P₃ / Feature type: SUBJECT OF INVESTIGATION / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#7: Chemical	ChemComp-SAM / S-ADENOSYLMETHIONINE Mass: 398.437 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₁₅H₂₂N₆O₅S / Feature type: SUBJECT OF INVESTIGATION
#8: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 46 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y
Has protein modification	N

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Experiment

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

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Sample preparation

Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: 50mM CaCl2 0.1M Bis-Tris pH 6.8 32.14% PEG MME 550

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å
Detector	Type: DECTRIS EIGER2 S 16M / Detector: PIXEL / Date: Apr 3, 2019
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9795 Å / Relative weight: 1
Reflection	Resolution: 2.82→29.39 Å / Num. obs: 61578 / % possible obs: 94.6 % / Redundancy: 3.5 % / B_iso Wilson estimate: 65.91 Å² / CC_1/2: 0.996 / R_rim(I) all: 0.114 / Net I/σ(I): 10.2
Reflection shell	Resolution: 2.82→2.921 Å / Mean I/σ(I) obs: 1.6 / Num. unique obs: 4103 / CC_1/2: 0.706 / R_rim(I) all: 0.7

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0267	refinement
xia2		data reduction
DIALS		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1P7L

1p7l

Resolution: 2.82→29.41 Å / Cor.coef. F_o:F_c: 0.964 / Cor.coef. F_o:F_c free: 0.897 / SU B: 59.888 / SU ML: 0.476 / Cross valid method: THROUGHOUT / ESU R Free: 0.5 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.27492	3108	5 %	RANDOM
R_work	0.15563	-	-	-
obs	0.16143	58472	94.93 %	-

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: 68.045 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-2.92 Å²	-4.73 Å²	0.58 Å²
2-	-	-6.27 Å²	-1.77 Å²
3-	-	-	9.82 Å²

Refinement step

Cycle: 1 / Resolution: 2.82→29.41 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	22380	0	273	46	22699

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.006	0.013	23016
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.015	21950
X-RAY DIFFRACTION	r_angle_refined_deg	1.546	1.645	31304
X-RAY DIFFRACTION	r_angle_other_deg	1.223	1.588	50485
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	7.725	5	2920
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	39.338	22.887	1164
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	18.475	15	3785
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	22.277	15	143
X-RAY DIFFRACTION	r_chiral_restr	0.067	0.2	3123
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	26164
X-RAY DIFFRACTION	r_gen_planes_other	0.002	0.02	4945
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	8.322	6.159	11740
X-RAY DIFFRACTION	r_mcbond_other	8.314	6.159	11739
X-RAY DIFFRACTION	r_mcangle_it	10.943	9.238	14640
X-RAY DIFFRACTION	r_mcangle_other	10.945	9.238	14641
X-RAY DIFFRACTION	r_scbond_it	9.129	6.657	11276
X-RAY DIFFRACTION	r_scbond_other	9.112	6.653	11270
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	11.997	9.85	16656
X-RAY DIFFRACTION	r_long_range_B_refined	13.34	73.037	23919
X-RAY DIFFRACTION	r_long_range_B_other	13.343	73.046	23920
X-RAY DIFFRACTION	r_rigid_bond_restr	3.237	3	44966
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	A	11310	0.09
1	2	B	11310	0.09
2	1	A	11393	0.09
2	2	C	11393	0.09
3	1	A	11331	0.09
3	2	D	11331	0.09
4	1	A	11263	0.1
4	2	E	11263	0.1
5	1	A	11281	0.09
5	2	F	11281	0.09
6	1	A	11208	0.11
6	2	G	11208	0.11
7	1	A	11307	0.1
7	2	H	11307	0.1
8	1	B	11327	0.09
8	2	C	11327	0.09
9	1	B	11286	0.09
9	2	D	11286	0.09
10	1	B	11293	0.1
10	2	E	11293	0.1
11	1	B	11260	0.1
11	2	F	11260	0.1
12	1	B	11159	0.1
12	2	G	11159	0.1
13	1	B	11248	0.1
13	2	H	11248	0.1
14	1	C	11503	0.1
14	2	D	11503	0.1
15	1	C	11460	0.1
15	2	E	11460	0.1
16	1	C	11487	0.09
16	2	F	11487	0.09
17	1	C	11298	0.1
17	2	G	11298	0.1
18	1	C	11354	0.1
18	2	H	11354	0.1
19	1	D	11431	0.1
19	2	E	11431	0.1
20	1	D	11385	0.1
20	2	F	11385	0.1
21	1	D	11301	0.11
21	2	G	11301	0.11
22	1	D	11297	0.11
22	2	H	11297	0.11
23	1	E	11317	0.1
23	2	F	11317	0.1
24	1	E	11223	0.11
24	2	G	11223	0.11
25	1	E	11299	0.11
25	2	H	11299	0.11
26	1	F	11309	0.1
26	2	G	11309	0.1
27	1	F	11207	0.1
27	2	H	11207	0.1
28	1	G	11212	0.11
28	2	H	11212	0.11

LS refinement shell

Resolution: 2.82→2.893 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.412	136	-
R_work	0.293	2280	-
obs	-	-	50.01 %

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	0.0061	0.0196	0.0012	0.0678	0.0036	0.0005	-0.0019	-0.0091	0.0019	-0.0053	0.0006	0.0111	0.004	-0.0029	0.0013	0.1238	0.0515	0.0221	0.1958	0.0329	0.0092	3.3614	25.0935	-0.9214
2	0.0097	0.0211	0.0058	0.0475	0.0134	0.0039	-0.0047	-0.0045	-0.0036	-0.0116	0.0057	-0.0054	0.0005	0.0069	-0.0009	0.1329	0.0519	0.0157	0.1964	0.0352	0.0074	1.1502	-0.0964	-5.3401
3	0.0021	0.0145	0.0063	0.1045	0.0448	0.0193	-0.0004	-0.0034	0.0011	0.0018	-0.0039	0.0112	0.0009	-0.0034	0.0042	0.1298	0.0456	0.0208	0.1798	0.0299	0.0077	-6.5855	5.9058	49.7357
4	0.0207	0.0227	0.0001	0.0251	0.0003	0.0004	-0.0118	0.0037	-0.0115	-0.0106	0.0105	-0.0117	0.0073	0.0037	0.0013	0.1379	0.0509	0.0148	0.179	0.0298	0.0121	18.3069	0.4991	46.6564
5	0.0494	0.0491	-0.0167	0.0491	-0.0168	0.0058	0.0021	0.0011	-0.0126	0.0039	-0.0061	-0.0134	-0.0013	0.0041	0.0041	0.1367	0.0481	0.0217	0.1744	0.0335	0.0111	-4.7791	-40.2702	-26.7722
6	0.0411	0.0265	0.0288	0.023	0.0167	0.0207	0.0055	0.0025	-0.0032	0.0182	0.0016	0.0083	0.0018	0.0003	-0.0071	0.137	0.042	0.0234	0.1776	0.0271	0.0222	-30.1561	-39.5541	-24.9521
7	0.0102	-0.0175	-0.0083	0.0474	0.0227	0.011	0.0019	0.003	0.011	0.0029	0.0004	-0.0065	0.0057	0.0041	-0.0024	0.1193	0.0442	0.0171	0.1968	0.0343	0.0241	-12.1933	-35.6847	27.3557
8	0.0012	-0.0088	0.0016	0.0789	-0.0132	0.0023	0.0017	0.0072	0.0007	-0.0003	-0.0016	0.0049	0.0033	0.0026	-0.0001	0.127	0.0417	0.0197	0.1977	0.034	0.0075	-16.84	-60.5165	23.9284

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	3 - 884
2	X-RAY DIFFRACTION	2	B	3 - 684
3	X-RAY DIFFRACTION	3	C	4 - 484
4	X-RAY DIFFRACTION	4	D	4 - 484
5	X-RAY DIFFRACTION	5	E	3 - 484
6	X-RAY DIFFRACTION	6	F	5 - 484
7	X-RAY DIFFRACTION	7	G	4 - 685
8	X-RAY DIFFRACTION	8	H	3 - 885

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