PDB-1xs6: dCTP deaminase from Escherichia coli. E138A mutant enzyme in comp...

ID or keywords:

Entry

Database: PDB / ID: 1xs6

Title

dCTP deaminase from Escherichia coli. E138A mutant enzyme in complex with dUTP

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 /

MOLECULAR REPLACEMENT / Resolution: 2 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	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.pdbx_dist_value / _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.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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4	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

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	1xs6.cif.gz	245.2 KB	Display	PDBx/mmCIF format
PDB format	pdb1xs6.ent.gz	196.7 KB	Display	PDB format
PDBx/mmJSON format	1xs6.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	1xs6_validation.pdf.gz	2.4 MB	Display	wwPDB validaton report
Full document	1xs6_full_validation.pdf.gz	2.4 MB	Display
Data in XML	1xs6_validation.xml.gz	49.1 KB	Display
Data in CIF	1xs6_validation.cif.gz	66.3 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/xs/1xs6 ftp://data.pdbj.org/pub/pdb/validation_reports/xs/1xs6	HTTPS FTP

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Related structure data

Related structure data	1xs1SC 1xs4C S: Starting model for refinement C: citing same article (ref.)
Similar structure data	1xs1-2 1xs1-1 1xs4-2 1xs4-1 2nt8-1 2j4q-1 2qlp-1 2qlp-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) 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

1xs1SC

1xs4C

S: Starting model for refinement

C: citing same article (ref.)

Similar structure data

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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

130 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
65.1 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
65.2 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

A: Deoxycytidine triphosphate deaminase

B: Deoxycytidine triphosphate deaminase

C: Deoxycytidine triphosphate deaminase

hetero molecules

A: Deoxycytidine triphosphate deaminase

B: Deoxycytidine triphosphate deaminase

C: Deoxycytidine triphosphate deaminase

hetero molecules

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

4

D: Deoxycytidine triphosphate deaminase

E: Deoxycytidine triphosphate deaminase

F: Deoxycytidine triphosphate deaminase

hetero molecules

D: Deoxycytidine triphosphate deaminase

E: Deoxycytidine triphosphate deaminase

F: Deoxycytidine triphosphate deaminase

hetero molecules

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

Unit cell

Length a, b, c (Å)	179.930, 63.073, 96.363
Angle α, β, γ (deg.)	90.00, 102.18, 90.00
Int Tables number	5
Space group name H-M	C121

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Ens-ID: 1 / Refine code: 4

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	MET	MET	ASP	ASP	A	A	1 - 5	1 - 5
2	1	MET	MET	ASP	ASP	B	B	1 - 5	1 - 5
3	1	MET	MET	ASP	ASP	C	C	1 - 5	1 - 5
4	1	MET	MET	ASP	ASP	D	D	1 - 5	1 - 5
5	1	MET	MET	ASP	ASP	E	E	1 - 5	1 - 5
6	1	MET	MET	ASP	ASP	F	F	1 - 5	1 - 5
7	2	ASP	ASP	ASP	ASP	A	A	7 - 13	7 - 13
8	2	ASP	ASP	ASP	ASP	B	B	7 - 13	7 - 13
9	2	ASP	ASP	ASP	ASP	C	C	7 - 13	7 - 13
10	2	ASP	ASP	ASP	ASP	D	D	7 - 13	7 - 13
11	2	ASP	ASP	ASP	ASP	E	E	7 - 13	7 - 13
12	2	ASP	ASP	ASP	ASP	F	F	7 - 13	7 - 13
13	3	PRO	PRO	PRO	PRO	A	A	21 - 24	21 - 24
14	3	PRO	PRO	PRO	PRO	B	B	21 - 24	21 - 24
15	3	PRO	PRO	PRO	PRO	C	C	21 - 24	21 - 24
16	3	PRO	PRO	PRO	PRO	D	D	21 - 24	21 - 24
17	3	PRO	PRO	PRO	PRO	E	E	21 - 24	21 - 24
18	3	PRO	PRO	PRO	PRO	F	F	21 - 24	21 - 24
19	4	ILE	ILE	VAL	VAL	A	A	28 - 35	28 - 35
20	4	ILE	ILE	VAL	VAL	B	B	28 - 35	28 - 35
21	4	ILE	ILE	VAL	VAL	C	C	28 - 35	28 - 35
22	4	ILE	ILE	VAL	VAL	D	D	28 - 35	28 - 35
23	4	ILE	ILE	VAL	VAL	E	E	28 - 35	28 - 35
24	4	ILE	ILE	VAL	VAL	F	F	28 - 35	28 - 35
25	5	LEU	LEU	GLY	GLY	A	A	37 - 38	37 - 38
26	5	LEU	LEU	GLY	GLY	B	B	37 - 38	37 - 38
27	5	LEU	LEU	GLY	GLY	C	C	37 - 38	37 - 38
28	5	LEU	LEU	GLY	GLY	D	D	37 - 38	37 - 38
29	5	LEU	LEU	GLY	GLY	E	E	37 - 38	37 - 38
30	5	LEU	LEU	GLY	GLY	F	F	37 - 38	37 - 38
31	6	LYS	LYS	LEU	LEU	A	A	40 - 54	40 - 54
32	6	LYS	LYS	LEU	LEU	B	B	40 - 54	40 - 54
33	6	LYS	LYS	LEU	LEU	C	C	40 - 54	40 - 54
34	6	LYS	LYS	LEU	LEU	D	D	40 - 54	40 - 54
35	6	LYS	LYS	LEU	LEU	E	E	40 - 54	40 - 54
36	6	LYS	LYS	LEU	LEU	F	F	40 - 54	40 - 54
37	7	VAL	VAL	SER	SER	A	A	61 - 70	61 - 70
38	7	VAL	VAL	SER	SER	B	B	61 - 70	61 - 70
39	7	VAL	VAL	SER	SER	C	C	61 - 70	61 - 70
40	7	VAL	VAL	SER	SER	D	D	61 - 70	61 - 70
41	7	VAL	VAL	SER	SER	E	E	61 - 70	61 - 70
42	7	VAL	VAL	SER	SER	F	F	61 - 70	61 - 70
43	8	GLU	GLU	LEU	LEU	A	A	72 - 75	72 - 75
44	8	GLU	GLU	LEU	LEU	B	B	72 - 75	72 - 75
45	8	GLU	GLU	LEU	LEU	C	C	72 - 75	72 - 75
46	8	GLU	GLU	LEU	LEU	D	D	72 - 75	72 - 75
47	8	GLU	GLU	LEU	LEU	E	E	72 - 75	72 - 75
48	8	GLU	GLU	LEU	LEU	F	F	72 - 75	72 - 75
49	9	ALA	ALA	LEU	LEU	A	A	80 - 118	80 - 118
50	9	ALA	ALA	LEU	LEU	B	B	80 - 118	80 - 118
51	9	ALA	ALA	LEU	LEU	C	C	80 - 118	80 - 118
52	9	ALA	ALA	LEU	LEU	D	D	80 - 118	80 - 118
53	9	ALA	ALA	LEU	LEU	E	E	80 - 118	80 - 118
54	9	ALA	ALA	LEU	LEU	F	F	80 - 118	80 - 118
55	10	VAL	VAL	ALA	ALA	A	A	122 - 124	122 - 124
56	10	VAL	VAL	ALA	ALA	B	B	122 - 124	122 - 124
57	10	VAL	VAL	ALA	ALA	C	C	122 - 124	122 - 124
58	10	VAL	VAL	ALA	ALA	D	D	122 - 124	122 - 124
59	10	VAL	VAL	ALA	ALA	E	E	122 - 124	122 - 124
60	10	VAL	VAL	ALA	ALA	F	F	122 - 124	122 - 124
61	11	ARG	ARG	GLY	GLY	A	A	126 - 143	126 - 143
62	11	ARG	ARG	GLY	GLY	B	B	126 - 143	126 - 143
63	11	ARG	ARG	GLY	GLY	C	C	126 - 143	126 - 143
64	11	ARG	ARG	GLY	GLY	D	D	126 - 143	126 - 143
65	11	ARG	ARG	GLY	GLY	E	E	126 - 143	126 - 143
66	11	ARG	ARG	GLY	GLY	F	F	126 - 143	126 - 143
67	12	LEU	LEU	LEU	LEU	A	A	145 - 149	145 - 149
68	12	LEU	LEU	LEU	LEU	B	B	145 - 149	145 - 149
69	12	LEU	LEU	LEU	LEU	C	C	145 - 149	145 - 149
70	12	LEU	LEU	LEU	LEU	D	D	145 - 149	145 - 149
71	12	LEU	LEU	LEU	LEU	E	E	145 - 149	145 - 149
72	12	LEU	LEU	LEU	LEU	F	F	145 - 149	145 - 149
73	13	PRO	PRO	GLY	GLY	A	A	151 - 165	151 - 165
74	13	PRO	PRO	GLY	GLY	B	B	151 - 165	151 - 165
75	13	PRO	PRO	GLY	GLY	C	C	151 - 165	151 - 165
76	13	PRO	PRO	GLY	GLY	D	D	151 - 165	151 - 165
77	13	PRO	PRO	GLY	GLY	E	E	151 - 165	151 - 165
78	13	PRO	PRO	GLY	GLY	F	F	151 - 165	151 - 165
79	14	ALA	ALA	ASN	ASN	A	A	167 - 172	167 - 172
80	14	ALA	ALA	ASN	ASN	B	B	167 - 172	167 - 172
81	14	ALA	ALA	ASN	ASN	C	C	167 - 172	167 - 172
82	14	ALA	ALA	ASN	ASN	D	D	167 - 172	167 - 172
83	14	ALA	ALA	ASN	ASN	E	E	167 - 172	167 - 172
84	14	ALA	ALA	ASN	ASN	F	F	167 - 172	167 - 172
85	15	ASP	ASP	ALA	ALA	A	A	176 - 177	176 - 177
86	15	ASP	ASP	ALA	ALA	B	B	176 - 177	176 - 177
87	15	ASP	ASP	ALA	ALA	C	C	176 - 177	176 - 177
88	15	ASP	ASP	ALA	ALA	D	D	176 - 177	176 - 177
89	15	ASP	ASP	ALA	ALA	E	E	176 - 177	176 - 177
90	15	ASP	ASP	ALA	ALA	F	F	176 - 177	176 - 177
91	16	TYR	TYR	ARG	ARG	A	A	179 - 180	179 - 180
92	16	TYR	TYR	ARG	ARG	B	B	179 - 180	179 - 180
93	16	TYR	TYR	ARG	ARG	C	C	179 - 180	179 - 180
94	16	TYR	TYR	ARG	ARG	D	D	179 - 180	179 - 180
95	16	TYR	TYR	ARG	ARG	E	E	179 - 180	179 - 180
96	16	TYR	TYR	ARG	ARG	F	F	179 - 180	179 - 180
97	17	GLY	GLY	ASP	ASP	A	A	184 - 191	184 - 191
98	17	GLY	GLY	ASP	ASP	B	B	184 - 191	184 - 191
99	17	GLY	GLY	ASP	ASP	C	C	184 - 191	184 - 191
100	17	GLY	GLY	ASP	ASP	D	D	184 - 191	184 - 191
101	17	GLY	GLY	ASP	ASP	E	E	184 - 191	184 - 191
102	17	GLY	GLY	ASP	ASP	F	F	184 - 191	184 - 191
103	18	DUT	DUT	MG	MG	A - C	H - K	1194 - 1195
104	18	DUT	DUT	MG	MG	B - A	J - G	2194 - 2195
105	18	DUT	DUT	MG	MG	C - B	L - I	3194 - 3195
106	18	DUT	DUT	MG	MG	D - F	O - R	4194 - 4195
107	18	DUT	DUT	MG	MG	E - D	Q - M	5194 - 5195
108	18	DUT	DUT	MG	MG	F - E	S - P	6194 - 6195

Details

The biological assembly is a trimer. There are two trimers in the asymmetric unit. 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: 21218.221 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.: 7 / Source method: obtained synthetically / Formula: Mg
#3: Chemical	ChemComp-DUT / DEOXYURIDINE-5'-TRIPHOSPHATE Mass: 468.142 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₉H₁₅N₂O₁₄P₃
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 391 / 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: 2.1 Å³/Da / Density % sol: 41 %
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: 120 K
Diffraction source	Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å
Detector	Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 23, 2004
Radiation	Monochromator: osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.5418 Å / Relative weight: 1
Reflection	Resolution: 2→25 Å / Num. all: 71843 / Num. obs: 71843 / % possible obs: 97.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.9 % / R_sym value: 0.108 / Net I/σ(I): 8
Reflection shell	Resolution: 2→2.05 Å / Mean I/σ(I) obs: 2.6 / R_sym value: 0.454 / % possible all: 95.5

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0001	refinement
DENZO		data reduction
SCALEPACK		data scaling
AMoRE		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1XS1

1xs1

Resolution: 2→25 Å / Cor.coef. F_o:F_c: 0.934 / Cor.coef. F_o:F_c free: 0.895 / SU B: 6.105 / SU ML: 0.176 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.309 / ESU R Free: 0.244 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.31288	3527	5.1 %	RANDOM
R_work	0.25809	-	-	-
obs	0.26088	66024	97.14 %	-

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: 19.091 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.91 Å²	0 Å²	0.64 Å²
2-	-	0.19 Å²	0 Å²
3-	-	-	0.99 Å²

Refinement step

Cycle: LAST / Resolution: 2→25 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8952	0	175	391	9518

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.014	0.021	9312
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	8646
X-RAY DIFFRACTION	r_angle_refined_deg	1.593	1.984	12672
X-RAY DIFFRACTION	r_angle_other_deg	0.903	3	19944
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	7.131	5	1152
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	30.204	22.319	414
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.705	15	1500
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	21.194	15	108
X-RAY DIFFRACTION	r_chiral_restr	0.089	0.2	1392
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	10368
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	1938
X-RAY DIFFRACTION	r_nbd_refined	0.2	0.2	1718
X-RAY DIFFRACTION	r_nbd_other	0.192	0.2	8992
X-RAY DIFFRACTION	r_nbtor_other	0.084	0.2	5695
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.185	0.2	477
X-RAY DIFFRACTION	r_xyhbond_nbd_other	0.18	0.2	1
X-RAY DIFFRACTION	r_metal_ion_refined	0.121	0.2	10
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.224	0.2	24
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.223	0.2	119
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.261	0.2	18
X-RAY DIFFRACTION	r_mcbond_it	0.791	1.5	5994
X-RAY DIFFRACTION	r_mcbond_other	0.19	1.5	2358
X-RAY DIFFRACTION	r_mcangle_it	1.147	2	9228
X-RAY DIFFRACTION	r_scbond_it	1.702	3	3834
X-RAY DIFFRACTION	r_scangle_it	2.544	4.5	3444

Refine LS restraints NCS

Ens-ID: 1 / Number: 2325 / Refine-ID: X-RAY DIFFRACTION

Dom-ID	Auth asym-ID	Type	Rms dev position (Å)	Weight position
1	A	medium positional	0.2	0.5
2	B	medium positional	0.18	0.5
3	C	medium positional	0.2	0.5
4	D	medium positional	0.19	0.5
5	E	medium positional	0.22	0.5
6	F	medium positional	0.19	0.5
1	A	medium thermal	0.49	2
2	B	medium thermal	0.47	2
3	C	medium thermal	0.54	2
4	D	medium thermal	0.49	2
5	E	medium thermal	0.49	2
6	F	medium thermal	0.46	2

LS refinement shell

Resolution: 2→2.052 Å / Total num. of bins used: 20 /

	R_factor	Num. reflection
R_free	0.349	263
R_work	0.313	4723

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About Yorodumi

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Yorodumi