PDB-1ocx: E. coli maltose-O-acetyltransferase

ID or keywords:

Entry

Database: PDB / ID: 1ocx

Title

E. coli maltose-O-acetyltransferase

Components

MALTOSE O-ACETYLTRANSFERASE

Keywords

TRANSFERASE / ACETYL TRANSFERASE / LEFT-HANDED PARALLEL BETA-HELIX

Function / homology

Function and homology information

maltose O-acetyltransferase / maltose O-acetyltransferase activity / O-acyltransferase activity / protein-containing complex / identical protein binding
Similarity search - Function

Biological species

ESCHERICHIA COLI (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON / OTHER / Resolution: 2.15 Å

Authors

Lo Leggio, L. / Dal Degan, F. / Poulsen, P. / Larsen, S.

Citation

Journal: Biochemistry / Year: 2003
Title: The Structure and Specificity of Escherichia Coli Maltose Acetyltransferase Give New Insight Into the Laca Family of Acyltransferases.
Authors: Lo Leggio, L. / Degan, F.D. / Poulsen, P. / Andersen, S.M. / Larsen, S.

History

Deposition	Feb 11, 2003	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jun 12, 2003	Provider: repository / Type: Initial release
Revision 1.1	Sep 3, 2014	Group: Database references / Derived calculations ...Database references / Derived calculations / Non-polymer description / Other / Version format compliance
Revision 1.2	May 8, 2019	Group: Data collection / Experimental preparation / Other Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.3	May 8, 2024	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	1ocx.cif.gz	231.1 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	1ocx_validation.pdf.gz	443.5 KB	Display	wwPDB validaton report
Full document	1ocx_full_validation.pdf.gz	456.2 KB	Display
Data in XML	1ocx_validation.xml.gz	25.6 KB	Display
Data in CIF	1ocx_validation.cif.gz	36.3 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/oc/1ocx ftp://data.pdbj.org/pub/pdb/validation_reports/oc/1ocx	HTTPS FTP

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Related structure data

Similar structure data	3ftt-1 1ue5-1 4k4t-1 2ic7-d 2p2o-2 3cnc-2 3oup-1 3srt-1 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	#165 - Sep 2013 Designed Protein Cages similarity (7) #39 - Mar 2003 lac Repressor similarity (8) #49 - Jan 2004 Carbonic Anhydrase similarity (4)

Deposited unit

A: MALTOSE O-ACETYLTRANSFERASE

B: MALTOSE O-ACETYLTRANSFERASE

C: MALTOSE O-ACETYLTRANSFERASE

hetero molecules

61.2 kDa, 3 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)	64.623, 106.238, 175.433
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	20
Space group name H-M	C222₁

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
3	1	C

NCS domain segments:

Ens-ID: 1

Dom-ID	Component-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	SER	SER	THR	THR	6	A	A	2 - 3	1 - 2
2	1	SER	SER	THR	THR	6	B	B	2 - 3	1 - 2
3	1	SER	SER	THR	THR	6	C	C	2 - 3	1 - 2
1	2	GLU	GLU	LYS	LYS	2	A	A	4 - 5	3 - 4
2	2	GLU	GLU	LYS	LYS	2	B	B	4 - 5	3 - 4
3	2	GLU	GLU	LYS	LYS	2	C	C	4 - 5	3 - 4
1	3	GLU	GLU	GLU	GLU	3	A	A	6	5
2	3	GLU	GLU	GLU	GLU	3	B	B	6	5
3	3	GLU	GLU	GLU	GLU	3	C	C	6	5
1	4	LYS	LYS	GLY	GLY	2	A	A	7 - 11	6 - 10
2	4	LYS	LYS	GLY	GLY	2	B	B	7 - 11	6 - 10
3	4	LYS	LYS	GLY	GLY	2	C	C	7 - 11	6 - 10
1	5	GLU	GLU	GLU	GLU	3	A	A	12	11
2	5	GLU	GLU	GLU	GLU	3	B	B	12	11
3	5	GLU	GLU	GLU	GLU	3	C	C	12	11
1	6	LEU	LEU	ARG	ARG	2	A	A	13 - 15	12 - 14
2	6	LEU	LEU	ARG	ARG	2	B	B	13 - 15	12 - 14
3	6	LEU	LEU	ARG	ARG	2	C	C	13 - 15	12 - 14
1	7	SER	SER	ARG	ARG	6	A	A	16 - 23	15 - 22
2	7	SER	SER	ARG	ARG	6	B	B	16 - 23	15 - 22
3	7	SER	SER	ARG	ARG	6	C	C	16 - 23	15 - 22
1	8	ASP	ASP	ARG	ARG	3	A	A	24 - 25	23 - 24
2	8	ASP	ASP	ARG	ARG	3	B	B	24 - 25	23 - 24
3	8	ASP	ASP	ARG	ARG	3	C	C	24 - 25	23 - 24
1	9	LEU	LEU	LEU	LEU	6	A	A	26	25
2	9	LEU	LEU	LEU	LEU	6	B	B	26	25
3	9	LEU	LEU	LEU	LEU	6	C	C	26	25
1	10	ARG	ARG	ARG	ARG	3	A	A	27	26
2	10	ARG	ARG	ARG	ARG	3	B	B	27	26
3	10	ARG	ARG	ARG	ARG	3	C	C	27	26
1	11	ALA	ALA	ARG	ARG	2	A	A	28 - 29	27 - 28
2	11	ALA	ALA	ARG	ARG	2	B	B	28 - 29	27 - 28
3	11	ALA	ALA	ARG	ARG	2	C	C	28 - 29	27 - 28
1	12	GLN	GLN	GLN	GLN	3	A	A	30	29
2	12	GLN	GLN	GLN	GLN	3	B	B	30	29
3	12	GLN	GLN	GLN	GLN	3	C	C	30	29
1	13	LEU	LEU	ILE	ILE	2	A	A	31 - 32	30 - 31
2	13	LEU	LEU	ILE	ILE	2	B	B	31 - 32	30 - 31
3	13	LEU	LEU	ILE	ILE	2	C	C	31 - 32	30 - 31
1	14	HIS	HIS	ARG	ARG	3	A	A	33 - 34	32 - 33
2	14	HIS	HIS	ARG	ARG	3	B	B	33 - 34	32 - 33
3	14	HIS	HIS	ARG	ARG	3	C	C	33 - 34	32 - 33
1	15	TYR	TYR	SER	SER	2	A	A	35 - 38	34 - 37
2	15	TYR	TYR	SER	SER	2	B	B	35 - 38	34 - 37
3	15	TYR	TYR	SER	SER	2	C	C	35 - 38	34 - 37
1	16	LEU	LEU	THR	THR	6	A	A	39 - 44	38 - 43
2	16	LEU	LEU	THR	THR	6	B	B	39 - 44	38 - 43
3	16	LEU	LEU	THR	THR	6	C	C	39 - 44	38 - 43
1	17	LEU	LEU	ARG	ARG	2	A	A	45 - 46	44 - 45
2	17	LEU	LEU	ARG	ARG	2	B	B	45 - 46	44 - 45
3	17	LEU	LEU	ARG	ARG	2	C	C	45 - 46	44 - 45
1	18	GLN	GLN	GLN	GLN	3	A	A	47 - 48	46 - 47
2	18	GLN	GLN	GLN	GLN	3	B	B	47 - 48	46 - 47
3	18	GLN	GLN	GLN	GLN	3	C	C	47 - 48	46 - 47
1	19	ILE	ILE	ILE	ILE	2	A	A	49	48
2	19	ILE	ILE	ILE	ILE	2	B	B	49	48
3	19	ILE	ILE	ILE	ILE	2	C	C	49	48
1	20	LEU	LEU	LEU	LEU	5	A	A	50	49
2	20	LEU	LEU	LEU	LEU	5	B	B	50	49
3	20	LEU	LEU	LEU	LEU	5	C	C	50	49
1	21	ALA	ALA	ALA	ALA	2	A	A	51	50
2	21	ALA	ALA	ALA	ALA	2	B	B	51	50
3	21	ALA	ALA	ALA	ALA	2	C	C	51	50
1	22	ASP	ASP	LEU	LEU	3	A	A	52 - 53	51 - 52
2	22	ASP	ASP	LEU	LEU	3	B	B	52 - 53	51 - 52
3	22	ASP	ASP	LEU	LEU	3	C	C	52 - 53	51 - 52
1	23	PHE	PHE	ALA	ALA	2	A	A	54 - 60	53 - 59
2	23	PHE	PHE	ALA	ALA	2	B	B	54 - 60	53 - 59
3	23	PHE	PHE	ALA	ALA	2	C	C	54 - 60	53 - 59
1	24	TYR	TYR	TYR	TYR	3	A	A	61	60
2	24	TYR	TYR	TYR	TYR	3	B	B	61	60
3	24	TYR	TYR	TYR	TYR	3	C	C	61	60
1	25	ILE	ILE	PRO	PRO	2	A	A	62 - 64	61 - 63
2	25	ILE	ILE	PRO	PRO	2	B	B	62 - 64	61 - 63
3	25	ILE	ILE	PRO	PRO	2	C	C	62 - 64	61 - 63
1	26	THR	THR	THR	THR	3	A	A	65	64
2	26	THR	THR	THR	THR	3	B	B	65	64
3	26	THR	THR	THR	THR	3	C	C	65	64
1	27	PHE	PHE	ALA	ALA	2	A	A	66 - 119	65 - 118
2	27	PHE	PHE	ALA	ALA	2	B	B	66 - 119	65 - 118
3	27	PHE	PHE	ALA	ALA	2	C	C	66 - 119	65 - 118
1	28	ARG	ARG	ARG	ARG	3	A	A	120	119
2	28	ARG	ARG	ARG	ARG	3	B	B	120	119
3	28	ARG	ARG	ARG	ARG	3	C	C	120	119
1	29	ASN	ASN	ALA	ALA	2	A	A	121 - 124	120 - 123
2	29	ASN	ASN	ALA	ALA	2	B	B	121 - 124	120 - 123
3	29	ASN	ASN	ALA	ALA	2	C	C	121 - 124	120 - 123
1	30	GLU	GLU	GLU	GLU	3	A	A	125	124
2	30	GLU	GLU	GLU	GLU	3	B	B	125	124
3	30	GLU	GLU	GLU	GLU	3	C	C	125	124
1	31	LEU	LEU	ILE	ILE	2	A	A	126 - 179	125 - 178
2	31	LEU	LEU	ILE	ILE	2	B	B	126 - 179	125 - 178
3	31	LEU	LEU	ILE	ILE	2	C	C	126 - 179	125 - 178
1	32	ILE	ILE	LEU	LEU	6	A	A	180 - 183	179 - 182
2	32	ILE	ILE	LEU	LEU	6	B	B	180 - 183	179 - 182
3	32	ILE	ILE	LEU	LEU	6	C	C	180 - 183	179 - 182

NCS oper: (Code: given
Matrix: (-0.36843, 0.82206, 0.43414), (-0.83462, -0.49818, 0.23503), (0.40948, -0.27575, 0.86965)
Vector: 42.247, 13.796, -12.817)

#1: Protein	MALTOSE O-ACETYLTRANSFERASE / MALTOSE ACETYLTRANSFERASE Mass: 19987.771 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH TRIMETHYL LEAD / Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Strain: NF1830 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P77791, maltose O-acetyltransferase
#2: Chemical	ChemComp-PBM / TRIMETHYL LEAD ION Mass: 252.304 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C₃H₉Pb
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 304 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION

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Sample preparation

Crystal

Density Matthews: 2.51 Å³/Da / Density % sol: 51.01 %
Description: INITIAL PHASES WERE OBTAINED FROM DATA COLLECTED AT ELETTRA, WHILE FINAL REFINEMENT WAS CARRIED OUT AGAINST THE DATA COLLECTED AT ESRF

Crystal grow

Method: vapor diffusion, hanging drop / pH: 5.6
Details: HANGING DROP CRYSTALLIZATION CRYSTALS FORM IN A 3 UL (RESERVOIR) + 1 UL (PROTEIN AT 15 MG/ML) DROP WITH RESERVOIR 0.1 M NA CITRATE PH 5.6, 3% ETHANOL, 15 % PEG 4000). ADDITION OF 6 UL OF ...

Crystal grow

*PLUS

pH: 5.6 / Method: vapor diffusion, hanging drop

Components of the solutions

*PLUS

ID	Conc.	Common name	Crystal-ID	Sol-ID	Details
1	0.1 M	sodium citrate	1	reservoir	pH5.6
2	3 %	ethanol	1	reservoir
3	15 %	PEG4000	1	reservoir
4	15 mg/ml	protein	1	drop

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.95
Detector	Detector: CCD
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.95 Å / Relative weight: 1
Reflection	Resolution: 2.15→15 Å / Num. obs: 33084 / % possible obs: 99.7 % / Redundancy: 3.7 % / R_merge(I) obs: 0.061
Reflection shell	Resolution: 2.15→2.23 Å / R_merge(I) obs: 0.396 / % possible all: 99.8
Reflection	PLUS Highest resolution: 2.15 Å / Lowest resolution: 15 Å / Num. measured all: 120930 / R_merge(I) obs*: 0.061
Reflection shell	PLUS % possible obs: 99.8 % / R_merge(I) obs*: 0.396

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Processing

Software

Name	Version	Classification
REFMAC	5	refinement
DENZO		data reduction
SCALEPACK		data scaling

Refinement

Method to determine structure: OTHER / Resolution: 2.15→15 Å / Cor.coef. F_o:F_c: 0.95 / Cor.coef. F_o:F_c free: 0.931 / SU B: 4.197 / SU ML: 0.11 / Cross valid method: THROUGHOUT / ESU R: 0.294 / ESU R Free: 0.214 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. INDIVIDUAL B-FACTOR REFINEMENT WAS PRECEEDED BY TLS REFINEMENT IN WHICH EACH MONOMER WAS DIVIDED INTO THREE TLS GROUPS. THE DEPOSITED ...

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.235	3117	9.9 %	RANDOM
R_work	0.194	-	-	-
obs	0.198	28344	94.9 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 15.39 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.92 Å²	0 Å²	0 Å²
2-	-	0.3 Å²	0 Å²
3-	-	-	-1.22 Å²

Refinement step

Cycle: LAST / Resolution: 2.15→15 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	4212	0	20	304	4536

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.016	0.021	4326
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	3972
X-RAY DIFFRACTION	r_angle_refined_deg	1.554	1.942	5877
X-RAY DIFFRACTION	r_angle_other_deg	0.764	2.992	9195
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	4.685	3	543
X-RAY DIFFRACTION	r_dihedral_angle_2_deg
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.77	15	750
X-RAY DIFFRACTION	r_dihedral_angle_4_deg
X-RAY DIFFRACTION	r_chiral_restr	0.086	0.2	677
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	4866
X-RAY DIFFRACTION	r_gen_planes_other	0.003	0.02	867
X-RAY DIFFRACTION	r_nbd_refined	0.239	0.3	1023
X-RAY DIFFRACTION	r_nbd_other	0.217	0.3	3969
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.187	0.5	388
X-RAY DIFFRACTION	r_xyhbond_nbd_other	0.109	0.5	11
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.355	0.3	24
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.418	0.3	46
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.168	0.5	7
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	0.492	1.5	2715
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	0.9	2	4401
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	1.75	3	1611
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	2.775	4.5	1476
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

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	935	tight positional	0.04	0.05
2	B	935	tight positional	0.05	0.05
3	C	935	tight positional	0.05	0.05
1	A	1269	medium positional	0.28	0.5
2	B	1269	medium positional	0.21	0.5
3	C	1269	medium positional	0.21	0.5
1	A	514	loose positional	0.56	5
2	B	514	loose positional	0.64	5
3	C	514	loose positional	0.83	5
1	A	935	tight thermal	0.12	0.5
2	B	935	tight thermal	0.14	0.5
3	C	935	tight thermal	0.13	0.5
1	A	1269	medium thermal	0.5	2
2	B	1269	medium thermal	0.47	2
3	C	1269	medium thermal	0.49	2
1	A	514	loose thermal	1.26	10
2	B	514	loose thermal	1.26	10
3	C	514	loose thermal	1.34	10

LS refinement shell

Resolution: 2.15→2.21 Å / Total num. of bins used: 20 /

	R_factor	Num. reflection
R_free	0.262	195
R_work	0.214	1939

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	4.1576	-1.6303	-2.5934	9.8044	4.1409	9.3703	-0.3401	-0.9032	-0.8043	0.6017	-0.0367	-0.3307	0.2366	0.6694	0.3768	0.0829	0.144	-0.0493	0.4839	0.2102	0.4035	59.6063	11.9197	71.1002
2	2.7019	1.5806	-1.9896	5.2136	-3.5793	6.7956	0.3443	-0.639	0.2867	0.5231	-0.3131	-0.176	-0.2339	0.5507	-0.0312	0.1555	-0.075	0.0369	0.2222	-0.1009	0.1689	39.3146	37.1151	77.6871
3	9.3572	-1.0574	3.4373	3.4516	-0.6876	6.1882	-0.1699	-0.6732	0.0492	0.4829	0.003	0.1759	0.0354	0.3408	0.167	0.3244	-0.0786	0.0476	0.203	0.0741	0.0983	28.4554	6.2067	80.704
4	4.0759	0.2673	0.4117	2.0266	-0.66	3.5973	-0.0502	-0.0398	-0.0866	-0.0392	0.0189	-0.1646	-0.0266	0.3028	0.0313	0.0238	0.0483	0.0226	0.1357	-0.0107	0.1255	51.5791	21.8125	57.1836
5	2.6461	0.4256	0.0803	2.6734	0.6367	3.0078	0.1104	-0.051	0.1149	0.0195	-0.0557	0.2278	0.0233	-0.1544	-0.0547	0.0397	0.0262	0.0304	0.0197	0.0067	0.1173	28.3577	29.39	64.4865
6	2.594	0.4661	-1.152	2.831	-0.3825	3.7335	-0.0504	-0.082	-0.2744	-0.1303	-0.0019	-0.1193	0.5899	0.131	0.0523	0.2224	-0.0036	-0.0258	0.028	0.0374	0.1394	33.6054	4.605	62.6393
7	11.3299	17.9869	-2.1414	25.1501	-3.9537	-1.1796	-0.4175	0.0275	-1.3124	-0.8669	0.1079	-0.7185	0.7609	0.1124	0.3096	0.602	0.1909	0.0815	0.3268	-0.0707	0.6173	47.8842	-1.4347	55.6953
8	20.5795	-2.2088	-12.5478	3.908	0.0998	2.3152	0.0054	0.3868	0.3022	-0.5305	0.0459	-0.8437	0.0586	0.2744	-0.0514	0.296	-0.0577	0.1014	0.3322	0.0072	0.3992	48.4492	38.3994	56.0502
9	1.8662	-5.4311	-0.1815	13.1054	-3.3115	-0.441	0.1887	0.0983	0.0428	-0.1053	-0.1969	1.1166	0.2182	-0.5781	0.0082	0.179	-0.0515	-0.0336	0.3262	-0.0067	0.4037	15.0964	18.8325	66.0617

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	2 - 55
2	X-RAY DIFFRACTION	2	B	2 - 55
3	X-RAY DIFFRACTION	3	C	2 - 55
4	X-RAY DIFFRACTION	4	A	56 - 110
5	X-RAY DIFFRACTION	4	A	129 - 183
6	X-RAY DIFFRACTION	5	B	56 - 110
7	X-RAY DIFFRACTION	5	B	129 - 183
8	X-RAY DIFFRACTION	6	C	56 - 110
9	X-RAY DIFFRACTION	6	C	129 - 183
10	X-RAY DIFFRACTION	7	A	111 - 128
11	X-RAY DIFFRACTION	8	B	111 - 128
12	X-RAY DIFFRACTION	9	C	111 - 128

Refine LS restraints

*PLUS

Refine-ID	Type	Dev ideal
X-RAY DIFFRACTION	r_bond_d	0.016
X-RAY DIFFRACTION	r_angle_d
X-RAY DIFFRACTION	r_angle_deg	1.55

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