PDB-1xs4: dCTP deaminase from Escherichia coli- E138A mutant enzyme in comp...

ID or keywords:

Entry

Database: PDB / ID: 1xs4

Title

dCTP deaminase from Escherichia coli- E138A mutant enzyme in complex with dCTP

Components

Deoxycytidine triphosphate deaminase

Keywords

HYDROLASE / dCTP deaminase / nucleotide metabolism / trimer

Function / homology

Function and homology information

dCTP deaminase / dUTP biosynthetic process / dCTP deaminase activity / dUMP biosynthetic process / nucleobase-containing small molecule interconversion / dTTP biosynthetic process / protein homotrimerization / response to radiation / nucleotide binding / protein-containing complex ...
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON / combination of SAD,

MOLECULAR REPLACEMENT / Resolution: 2.53 Å

Authors

Johansson, E. / Fano, M. / Bynck, J.H. / Neuhard, J. / Larsen, S. / Sigurskjold, B.W. / Christensen, U. / Willemoes, M.

Citation

Journal: J.Biol.Chem. / Year: 2005
Title: Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes
Authors: Johansson, E. / Fano, M. / Bynck, J.H. / Neuhard, J. / Larsen, S. / Sigurskjold, B.W. / Christensen, U. / Willemoes, M.

History

Deposition	Oct 18, 2004	Deposition site: RCSB / Processing site: PDBJ
Revision 1.0	Dec 21, 2004	Provider: repository / Type: Initial release
Revision 1.1	Apr 30, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Version format compliance
Revision 1.3	Aug 8, 2018	Group: Data collection / Category: diffrn_source / struct_biol / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.4	Nov 10, 2021	Group: Database references / Derived calculations Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_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_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_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_comp_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5	Oct 25, 2023	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_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.6	Nov 15, 2023	Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.7	Nov 13, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/xs/1xs4 ftp://data.pdbj.org/pub/pdb/validation_reports/xs/1xs4	HTTPS FTP

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Related structure data

Related structure data	1xs1C 1xs6C 1oghS C: citing same article (ref.) S: Starting model for refinement
Similar structure data	1xs1-2 1xs6-1 1xs6-2 1xs1-1 2j4q-1 2j4q-2 2r6t-1 2j4h-2 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	#259 - Jul 2021 Designed Proteins and Citizen Science similarity (3)

Deposited unit

A: Deoxycytidine triphosphate deaminase

B: Deoxycytidine triphosphate deaminase

C: Deoxycytidine triphosphate deaminase

D: Deoxycytidine triphosphate deaminase

E: Deoxycytidine triphosphate deaminase

F: Deoxycytidine triphosphate deaminase

hetero molecules

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

1

A: Deoxycytidine triphosphate deaminase

B: Deoxycytidine triphosphate deaminase

C: Deoxycytidine triphosphate deaminase

hetero molecules

defined by author&software
65.7 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: Deoxycytidine triphosphate deaminase

E: Deoxycytidine triphosphate deaminase

F: Deoxycytidine triphosphate deaminase

hetero molecules

defined by author&software
65.7 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

Idetical with deposited unit
defined by software

Unit cell

Length a, b, c (Å)	63.272, 97.882, 95.116
Angle α, β, γ (deg.)	90.00, 109.23, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Ens-ID: 1 / Refine code: 1

Dom-ID	Component-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	ARG	ARG	ASP	ASP	A	A	2 - 5	2 - 5
2	1	ARG	ARG	ASP	ASP	B	B	2 - 5	2 - 5
3	1	ARG	ARG	ASP	ASP	C	C	2 - 5	2 - 5
4	1	ARG	ARG	ASP	ASP	D	D	2 - 5	2 - 5
5	1	ARG	ARG	ASP	ASP	E	E	2 - 5	2 - 5
6	1	ARG	ARG	ASP	ASP	F	F	2 - 5	2 - 5
7	2	ALA	ALA	ASP	ASP	A	A	10 - 13	10 - 13
8	2	ALA	ALA	ASP	ASP	B	B	10 - 13	10 - 13
9	2	ALA	ALA	ASP	ASP	C	C	10 - 13	10 - 13
10	2	ALA	ALA	ASP	ASP	D	D	10 - 13	10 - 13
11	2	ALA	ALA	ASP	ASP	E	E	10 - 13	10 - 13
12	2	ALA	ALA	ASP	ASP	F	F	10 - 13	10 - 13
13	3	PRO	PRO	VAL	VAL	A	A	21 - 25	21 - 25
14	3	PRO	PRO	VAL	VAL	B	B	21 - 25	21 - 25
15	3	PRO	PRO	VAL	VAL	C	C	21 - 25	21 - 25
16	3	PRO	PRO	VAL	VAL	D	D	21 - 25	21 - 25
17	3	PRO	PRO	VAL	VAL	E	E	21 - 25	21 - 25
18	3	PRO	PRO	VAL	VAL	F	F	21 - 25	21 - 25
19	4	ARG	ARG	VAL	VAL	A	A	27 - 35	27 - 35
20	4	ARG	ARG	VAL	VAL	B	B	27 - 35	27 - 35
21	4	ARG	ARG	VAL	VAL	C	C	27 - 35	27 - 35
22	4	ARG	ARG	VAL	VAL	D	D	27 - 35	27 - 35
23	4	ARG	ARG	VAL	VAL	E	E	27 - 35	27 - 35
24	4	ARG	ARG	VAL	VAL	F	F	27 - 35	27 - 35
25	5	LYS	LYS	GLY	GLY	A	A	40 - 46	40 - 46
26	5	LYS	LYS	GLY	GLY	B	B	40 - 46	40 - 46
27	5	LYS	LYS	GLY	GLY	C	C	40 - 46	40 - 46
28	5	LYS	LYS	GLY	GLY	D	D	40 - 46	40 - 46
29	5	LYS	LYS	GLY	GLY	E	E	40 - 46	40 - 46
30	5	LYS	LYS	GLY	GLY	F	F	40 - 46	40 - 46
31	6	THR	THR	LEU	LEU	A	A	48 - 54	48 - 54
32	6	THR	THR	LEU	LEU	B	B	48 - 54	48 - 54
33	6	THR	THR	LEU	LEU	C	C	48 - 54	48 - 54
34	6	THR	THR	LEU	LEU	D	D	48 - 54	48 - 54
35	6	THR	THR	LEU	LEU	E	E	48 - 54	48 - 54
36	6	THR	THR	LEU	LEU	F	F	48 - 54	48 - 54
37	7	GLY	GLY	LYS	LYS	A	A	56 - 58	56 - 58
38	7	GLY	GLY	LYS	LYS	B	B	56 - 58	56 - 58
39	7	GLY	GLY	LYS	LYS	C	C	56 - 58	56 - 58
40	7	GLY	GLY	LYS	LYS	D	D	56 - 58	56 - 58
41	7	GLY	GLY	LYS	LYS	E	E	56 - 58	56 - 58
42	7	GLY	GLY	LYS	LYS	F	F	56 - 58	56 - 58
43	8	ALA	ALA	ASP	ASP	A	A	63 - 66	63 - 66
44	8	ALA	ALA	ASP	ASP	B	B	63 - 66	63 - 66
45	8	ALA	ALA	ASP	ASP	C	C	63 - 66	63 - 66
46	8	ALA	ALA	ASP	ASP	D	D	63 - 66	63 - 66
47	8	ALA	ALA	ASP	ASP	E	E	63 - 66	63 - 66
48	8	ALA	ALA	ASP	ASP	F	F	63 - 66	63 - 66
49	9	VAL	VAL	SER	SER	A	A	68 - 70	68 - 70
50	9	VAL	VAL	SER	SER	B	B	68 - 70	68 - 70
51	9	VAL	VAL	SER	SER	C	C	68 - 70	68 - 70
52	9	VAL	VAL	SER	SER	D	D	68 - 70	68 - 70
53	9	VAL	VAL	SER	SER	E	E	68 - 70	68 - 70
54	9	VAL	VAL	SER	SER	F	F	68 - 70	68 - 70
55	10	GLU	GLU	VAL	VAL	A	A	72 - 74	72 - 74
56	10	GLU	GLU	VAL	VAL	B	B	72 - 74	72 - 74
57	10	GLU	GLU	VAL	VAL	C	C	72 - 74	72 - 74
58	10	GLU	GLU	VAL	VAL	D	D	72 - 74	72 - 74
59	10	GLU	GLU	VAL	VAL	E	E	72 - 74	72 - 74
60	10	GLU	GLU	VAL	VAL	F	F	72 - 74	72 - 74
61	11	ALA	ALA	LEU	LEU	A	A	80 - 83	80 - 83
62	11	ALA	ALA	LEU	LEU	B	B	80 - 83	80 - 83
63	11	ALA	ALA	LEU	LEU	C	C	80 - 83	80 - 83
64	11	ALA	ALA	LEU	LEU	D	D	80 - 83	80 - 83
65	11	ALA	ALA	LEU	LEU	E	E	80 - 83	80 - 83
66	11	ALA	ALA	LEU	LEU	F	F	80 - 83	80 - 83
67	12	PRO	PRO	VAL	VAL	A	A	85 - 120	85 - 120
68	12	PRO	PRO	VAL	VAL	B	B	85 - 120	85 - 120
69	12	PRO	PRO	VAL	VAL	C	C	85 - 120	85 - 120
70	12	PRO	PRO	VAL	VAL	D	D	85 - 120	85 - 120
71	12	PRO	PRO	VAL	VAL	E	E	85 - 120	85 - 120
72	12	PRO	PRO	VAL	VAL	F	F	85 - 120	85 - 120
73	13	VAL	VAL	ALA	ALA	A	A	122 - 124	122 - 124
74	13	VAL	VAL	ALA	ALA	B	B	122 - 124	122 - 124
75	13	VAL	VAL	ALA	ALA	C	C	122 - 124	122 - 124
76	13	VAL	VAL	ALA	ALA	D	D	122 - 124	122 - 124
77	13	VAL	VAL	ALA	ALA	E	E	122 - 124	122 - 124
78	13	VAL	VAL	ALA	ALA	F	F	122 - 124	122 - 124
79	14	ARG	ARG	GLY	GLY	A	A	126 - 143	126 - 143
80	14	ARG	ARG	GLY	GLY	B	B	126 - 143	126 - 143
81	14	ARG	ARG	GLY	GLY	C	C	126 - 143	126 - 143
82	14	ARG	ARG	GLY	GLY	D	D	126 - 143	126 - 143
83	14	ARG	ARG	GLY	GLY	E	E	126 - 143	126 - 143
84	14	ARG	ARG	GLY	GLY	F	F	126 - 143	126 - 143
85	15	LEU	LEU	LEU	LEU	A	A	145 - 149	145 - 149
86	15	LEU	LEU	LEU	LEU	B	B	145 - 149	145 - 149
87	15	LEU	LEU	LEU	LEU	C	C	145 - 149	145 - 149
88	15	LEU	LEU	LEU	LEU	D	D	145 - 149	145 - 149
89	15	LEU	LEU	LEU	LEU	E	E	145 - 149	145 - 149
90	15	LEU	LEU	LEU	LEU	F	F	145 - 149	145 - 149
91	16	PRO	PRO	ASN	ASN	A	A	151 - 172	151 - 172
92	16	PRO	PRO	ASN	ASN	B	B	151 - 172	151 - 172
93	16	PRO	PRO	ASN	ASN	C	C	151 - 172	151 - 172
94	16	PRO	PRO	ASN	ASN	D	D	151 - 172	151 - 172
95	16	PRO	PRO	ASN	ASN	E	E	151 - 172	151 - 172
96	16	PRO	PRO	ASN	ASN	F	F	151 - 172	151 - 172
97	17	ASP	ASP	ARG	ARG	A	A	176 - 180	176 - 180
98	17	ASP	ASP	ARG	ARG	B	B	176 - 180	176 - 180
99	17	ASP	ASP	ARG	ARG	C	C	176 - 180	176 - 180
100	17	ASP	ASP	ARG	ARG	D	D	176 - 180	176 - 180
101	17	ASP	ASP	ARG	ARG	E	E	176 - 180	176 - 180
102	17	ASP	ASP	ARG	ARG	F	F	176 - 180	176 - 180
103	18	GLY	GLY	SER	SER	A	A	184 - 188	184 - 188
104	18	GLY	GLY	SER	SER	B	B	184 - 188	184 - 188
105	18	GLY	GLY	SER	SER	C	C	184 - 188	184 - 188
106	18	GLY	GLY	SER	SER	D	D	184 - 188	184 - 188
107	18	GLY	GLY	SER	SER	E	E	184 - 188	184 - 188
108	18	GLY	GLY	SER	SER	F	F	184 - 188	184 - 188
109	19	DCP	DCP	MG	MG	A - C	H - K	1194 - 1195
110	19	DCP	DCP	MG	MG	B - A	J - G	2194 - 2195
111	19	DCP	DCP	MG	MG	C - B	L - I	3194 - 3195
112	19	DCP	DCP	MG	MG	D - F	N - Q	4194 - 4195
113	19	DCP	DCP	MG	MG	E - D	P - M	5194 - 5195
114	19	DCP	DCP	MG	MG	F - E	R - O	6194 - 6195

Details

The biological assembly is a trimer and the asymmetric unit contains two trimers. The first trimer is built from chain A, B and C and the second trimer is built from chain D, E and F.

#1: Protein	Deoxycytidine triphosphate deaminase / dCTP deaminase Mass: 21405.801 Da / Num. of mol.: 6 / Mutation: E138A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: dcd / Plasmid: pET11a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P28248, dCTP deaminase
#2: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#3: Chemical	ChemComp-DCP / 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE Mass: 467.157 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₉H₁₆N₃O₁₃P₃
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 229 / Source method: isolated from a natural source / Formula: H₂O
Has protein modification	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.18 Å³/Da / Density % sol: 44 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 400, magnesium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: MAX II / Beamline: I711 / Wavelength: 0.969 Å
Detector	Type: MARRESEARCH / Detector: CCD / Date: Sep 12, 2003 / Details: Vertically focusing cylindrical mirror.
Radiation	Monochromator: Single asymmetrically cut Si(111) crystal with horizontal diffraction plane. The crystal is bendable for horizontal focusing. Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.969 Å / Relative weight: 1
Reflection	Resolution: 2.53→30 Å / Num. all: 37005 / Num. obs: 37005 / % possible obs: 98.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.7 % / R_sym value: 0.052 / Net I/σ(I): 25.6
Reflection shell	Resolution: 2.53→2.59 Å / Mean I/σ(I) obs: 12.5 / R_sym value: 0.092 / % possible all: 78.2

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Processing

Software

Name	Version	Classification
REFMAC	5.1.24	refinement
DENZO		data reduction
SCALEPACK		data scaling
AMoRE		phasing

Refinement

Method to determine structure: combination of SAD,

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1OGH

1ogh

Resolution: 2.53→30 Å / Cor.coef. F_o:F_c: 0.931 / Cor.coef. F_o:F_c free: 0.902 / SU B: 9.299 / SU ML: 0.21 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.302 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.22541	1818	5 %	RANDOM
R_work	0.18479	-	-	-
obs	0.18689	34581	99.44 %	-
all	-	36399	-	-

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: 19.611 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.85 Å²	0 Å²	-0.08 Å²
2-	-	0.3 Å²	0 Å²
3-	-	-	-1.2 Å²

Refinement step

Cycle: LAST / Resolution: 2.53→30 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8952	0	174	229	9355

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.02	0.021	9312
X-RAY DIFFRACTION	r_bond_other_d	0.003	0.02	8640
X-RAY DIFFRACTION	r_angle_refined_deg	1.66	1.994	12666
X-RAY DIFFRACTION	r_angle_other_deg	0.962	3	19926
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.608	5	1152
X-RAY DIFFRACTION	r_chiral_restr	0.095	0.2	1392
X-RAY DIFFRACTION	r_gen_planes_refined	0.008	0.02	10380
X-RAY DIFFRACTION	r_gen_planes_other	0.005	0.02	1962
X-RAY DIFFRACTION	r_nbd_refined	0.199	0.2	1616
X-RAY DIFFRACTION	r_nbd_other	0.251	0.2	9628
X-RAY DIFFRACTION	r_nbtor_other	0.086	0.2	5633
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.191	0.2	325
X-RAY DIFFRACTION	r_metal_ion_refined	0.075	0.2	5
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.16	0.2	12
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.261	0.2	56
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.178	0.2	3
X-RAY DIFFRACTION	r_mcbond_it	0.679	1.5	5760
X-RAY DIFFRACTION	r_mcangle_it	1.289	2	9222
X-RAY DIFFRACTION	r_scbond_it	2.077	3	3552
X-RAY DIFFRACTION	r_scangle_it	3.387	4.5	3444

Refine LS restraints NCS

Ens-ID: 1 / Number: 2226 / Refine-ID: X-RAY DIFFRACTION

Dom-ID	Auth asym-ID	Type	Rms dev position (Å)	Weight position
1	A	tight positional	0.04	0.05
2	B	tight positional	0.05	0.05
3	C	tight positional	0.05	0.05
4	D	tight positional	0.04	0.05
5	E	tight positional	0.04	0.05
6	F	tight positional	0.04	0.05
1	A	tight thermal	0.12	0.5
2	B	tight thermal	0.12	0.5
3	C	tight thermal	0.13	0.5
4	D	tight thermal	0.12	0.5
5	E	tight thermal	0.12	0.5
6	F	tight thermal	0.11	0.5

LS refinement shell

Resolution: 2.53→2.595 Å / Total num. of bins used: 20 /

	R_factor	Num. reflection
R_free	0.309	111
R_work	0.236	2332

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