PDB-6i9g: Crystal structure of encapsulin from Mycolicibacterium hassiacum

Basic information

• Entry: Database: PDB / ID: 6i9g
• Title: Crystal structure of encapsulin from Mycolicibacterium hassiacum
• Components: Linocin-M18
• Keywords: VIRUS LIKE PARTICLE / Nanocompartment / nanocage / packaging of biocatalysts / bacteriocin

Function / homology

Function:

encapsulin nanocompartment / Hydrolases; Acting on peptide bonds (peptidases) / hydrolase activity

Domain/homology:

Major capsid protein gp5 fold - #30 / Major capsid protein gp5 fold / Type 1 encapsulin shell protein / Encapsulating protein for peroxidase / : / 2-Layer Sandwich / Alpha Beta

Component:

Linocin-M18

• Biological species: Mycolicibacterium hassiacum DSM 44199 (bacteria)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
• Authors: Rozeboom, H.J. / Fraaije, M.W.
• Citation: Journal: Biochem.Biophys.Res.Commun. / Year: 2020; Title: Structure of a robust bacterial protein cage and its application as a versatile biocatalytic platform through enzyme encapsulation.; Authors: Loncar, N. / Rozeboom, H.J. / Franken, L.E. / Stuart, M.C.A. / Fraaije, M.W.

History

Deposition	Nov 23, 2018	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Dec 4, 2019	Provider: repository / Type: Initial release
Revision 1.1	Jul 22, 2020	Group: Database references / Category: citation Item: _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2	Aug 12, 2020	Group: Database references / Category: citation / citation_author Item: _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.3	Jan 24, 2024	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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 1.4	Nov 6, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Assembly

Deposited unit

A: Linocin-M18

B: Linocin-M18

C: Linocin-M18

D: Linocin-M18

E: Linocin-M18

F: Linocin-M18

G: Linocin-M18

H: Linocin-M18

I: Linocin-M18

J: Linocin-M18

K: Linocin-M18

L: Linocin-M18

M: Linocin-M18

N: Linocin-M18

O: Linocin-M18

hetero molecules

Summary:

• 447 kDa, 15 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	446,810	136
Polymers	435,202	15
Non-polymers	11,608	121
Water	50,388	2797

1

A: Linocin-M18

B: Linocin-M18

C: Linocin-M18

D: Linocin-M18

E: Linocin-M18

F: Linocin-M18

G: Linocin-M18

H: Linocin-M18

I: Linocin-M18

J: Linocin-M18

K: Linocin-M18

L: Linocin-M18

M: Linocin-M18

N: Linocin-M18

O: Linocin-M18

hetero molecules

A: Linocin-M18

B: Linocin-M18

C: Linocin-M18

D: Linocin-M18

E: Linocin-M18

F: Linocin-M18

G: Linocin-M18

H: Linocin-M18

I: Linocin-M18

J: Linocin-M18

K: Linocin-M18

L: Linocin-M18

M: Linocin-M18

N: Linocin-M18

O: Linocin-M18

hetero molecules

A: Linocin-M18

B: Linocin-M18

C: Linocin-M18

D: Linocin-M18

E: Linocin-M18

F: Linocin-M18

G: Linocin-M18

H: Linocin-M18

I: Linocin-M18

J: Linocin-M18

K: Linocin-M18

L: Linocin-M18

M: Linocin-M18

N: Linocin-M18

O: Linocin-M18

hetero molecules

A: Linocin-M18

B: Linocin-M18

C: Linocin-M18

D: Linocin-M18

E: Linocin-M18

F: Linocin-M18

G: Linocin-M18

H: Linocin-M18

I: Linocin-M18

J: Linocin-M18

K: Linocin-M18

L: Linocin-M18

M: Linocin-M18

N: Linocin-M18

O: Linocin-M18

hetero molecules

Summary:

• defined by author&software
• Evidence: light scattering
• 1.79 MDa, 60 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	1,787,239	544
Polymers	1,740,808	60
Non-polymers	46,431	484
Water	1,081	60

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1
crystal symmetry operation	2_455	-x-1,-y,z	1
crystal symmetry operation	3_455	-x-1,y,-z	1
crystal symmetry operation	4_555	x,-y,-z	1

Calculated values:

Buried area	298320 Å2
ΔGint	-587 kcal/mol
Surface area	523010 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	231.272, 242.149, 271.557
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	23
Space group name H-M	I222

Components on special symmetry positions

ID	Model	Components
1	1	D-558- HOH
2	1	K-536- HOH

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
1	2	A
2	2	C
1	3	A
2	3	D
1	4	A
2	4	E
1	5	A
2	5	F
1	6	A
2	6	G
1	7	A
2	7	H
1	8	A
2	8	I
1	9	A
2	9	J
1	10	A
2	10	K
1	11	A
2	11	L
1	12	A
2	12	M
1	13	A
2	13	N
1	14	A
2	14	O
1	15	B
2	15	C
1	16	B
2	16	D
1	17	B
2	17	E
1	18	B
2	18	F
1	19	B
2	19	G
1	20	B
2	20	H
1	21	B
2	21	I
1	22	B
2	22	J
1	23	B
2	23	K
1	24	B
2	24	L
1	25	B
2	25	M
1	26	B
2	26	N
1	27	B
2	27	O
1	28	C
2	28	D
1	29	C
2	29	E
1	30	C
2	30	F
1	31	C
2	31	G
1	32	C
2	32	H
1	33	C
2	33	I
1	34	C
2	34	J
1	35	C
2	35	K
1	36	C
2	36	L
1	37	C
2	37	M
1	38	C
2	38	N
1	39	C
2	39	O
1	40	D
2	40	E
1	41	D
2	41	F
1	42	D
2	42	G
1	43	D
2	43	H
1	44	D
2	44	I
1	45	D
2	45	J
1	46	D
2	46	K
1	47	D
2	47	L
1	48	D
2	48	M
1	49	D
2	49	N
1	50	D
2	50	O
1	51	E
2	51	F
1	52	E
2	52	G
1	53	E
2	53	H
1	54	E
2	54	I
1	55	E
2	55	J
1	56	E
2	56	K
1	57	E
2	57	L
1	58	E
2	58	M
1	59	E
2	59	N
1	60	E
2	60	O
1	61	F
2	61	G
1	62	F
2	62	H
1	63	F
2	63	I
1	64	F
2	64	J
1	65	F
2	65	K
1	66	F
2	66	L
1	67	F
2	67	M
1	68	F
2	68	N
1	69	F
2	69	O
1	70	G
2	70	H
1	71	G
2	71	I
1	72	G
2	72	J
1	73	G
2	73	K
1	74	G
2	74	L
1	75	G
2	75	M
1	76	G
2	76	N
1	77	G
2	77	O
1	78	H
2	78	I
1	79	H
2	79	J
1	80	H
2	80	K
1	81	H
2	81	L
1	82	H
2	82	M
1	83	H
2	83	N
1	84	H
2	84	O
1	85	I
2	85	J
1	86	I
2	86	K
1	87	I
2	87	L
1	88	I
2	88	M
1	89	I
2	89	N
1	90	I
2	90	O
1	91	J
2	91	K
1	92	J
2	92	L
1	93	J
2	93	M
1	94	J
2	94	N
1	95	J
2	95	O
1	96	K
2	96	L
1	97	K
2	97	M
1	98	K
2	98	N
1	99	K
2	99	O
1	100	L
2	100	M
1	101	L
2	101	N
1	102	L
2	102	O
1	103	M
2	103	N
1	104	M
2	104	O
1	105	N
2	105	O

NCS domain segments:

Component-ID: _ / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: PRO / End label comp-ID: PRO / Refine code: _ / Auth seq-ID: 1 - 265 / Label seq-ID: 1 - 265

Dom-ID	Ens-ID	Auth asym-ID	Label asym-ID
1	1	A	A
2	1	B	B
1	2	A	A
2	2	C	C
1	3	A	A
2	3	D	D
1	4	A	A
2	4	E	E
1	5	A	A
2	5	F	F
1	6	A	A
2	6	G	G
1	7	A	A
2	7	H	H
1	8	A	A
2	8	I	I
1	9	A	A
2	9	J	J
1	10	A	A
2	10	K	K
1	11	A	A
2	11	L	L
1	12	A	A
2	12	M	M
1	13	A	A
2	13	N	N
1	14	A	A
2	14	O	O
1	15	B	B
2	15	C	C
1	16	B	B
2	16	D	D
1	17	B	B
2	17	E	E
1	18	B	B
2	18	F	F
1	19	B	B
2	19	G	G
1	20	B	B
2	20	H	H
1	21	B	B
2	21	I	I
1	22	B	B
2	22	J	J
1	23	B	B
2	23	K	K
1	24	B	B
2	24	L	L
1	25	B	B
2	25	M	M
1	26	B	B
2	26	N	N
1	27	B	B
2	27	O	O
1	28	C	C
2	28	D	D
1	29	C	C
2	29	E	E
1	30	C	C
2	30	F	F
1	31	C	C
2	31	G	G
1	32	C	C
2	32	H	H
1	33	C	C
2	33	I	I
1	34	C	C
2	34	J	J
1	35	C	C
2	35	K	K
1	36	C	C
2	36	L	L
1	37	C	C
2	37	M	M
1	38	C	C
2	38	N	N
1	39	C	C
2	39	O	O
1	40	D	D
2	40	E	E
1	41	D	D
2	41	F	F
1	42	D	D
2	42	G	G
1	43	D	D
2	43	H	H
1	44	D	D
2	44	I	I
1	45	D	D
2	45	J	J
1	46	D	D
2	46	K	K
1	47	D	D
2	47	L	L
1	48	D	D
2	48	M	M
1	49	D	D
2	49	N	N
1	50	D	D
2	50	O	O
1	51	E	E
2	51	F	F
1	52	E	E
2	52	G	G
1	53	E	E
2	53	H	H
1	54	E	E
2	54	I	I
1	55	E	E
2	55	J	J
1	56	E	E
2	56	K	K
1	57	E	E
2	57	L	L
1	58	E	E
2	58	M	M
1	59	E	E
2	59	N	N
1	60	E	E
2	60	O	O
1	61	F	F
2	61	G	G
1	62	F	F
2	62	H	H
1	63	F	F
2	63	I	I
1	64	F	F
2	64	J	J
1	65	F	F
2	65	K	K
1	66	F	F
2	66	L	L
1	67	F	F
2	67	M	M
1	68	F	F
2	68	N	N
1	69	F	F
2	69	O	O
1	70	G	G
2	70	H	H
1	71	G	G
2	71	I	I
1	72	G	G
2	72	J	J
1	73	G	G
2	73	K	K
1	74	G	G
2	74	L	L
1	75	G	G
2	75	M	M
1	76	G	G
2	76	N	N
1	77	G	G
2	77	O	O
1	78	H	H
2	78	I	I
1	79	H	H
2	79	J	J
1	80	H	H
2	80	K	K
1	81	H	H
2	81	L	L
1	82	H	H
2	82	M	M
1	83	H	H
2	83	N	N
1	84	H	H
2	84	O	O
1	85	I	I
2	85	J	J
1	86	I	I
2	86	K	K
1	87	I	I
2	87	L	L
1	88	I	I
2	88	M	M
1	89	I	I
2	89	N	N
1	90	I	I
2	90	O	O
1	91	J	J
2	91	K	K
1	92	J	J
2	92	L	L
1	93	J	J
2	93	M	M
1	94	J	J
2	94	N	N
1	95	J	J
2	95	O	O
1	96	K	K
2	96	L	L
1	97	K	K
2	97	M	M
1	98	K	K
2	98	N	N
1	99	K	K
2	99	O	O
1	100	L	L
2	100	M	M
1	101	L	L
2	101	N	N
1	102	L	L
2	102	O	O
1	103	M	M
2	103	N	N
1	104	M	M
2	104	O	O
1	105	N	N
2	105	O	O

NCS ensembles :

ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84
85
86
87
88
89
90
91
92
93
94
95
96
97
98
99
100
101
102
103
104
105

Components

#1: Protein

A B C D E F G H I J K L M N O
Linocin-M18

Details:

Mass: 29013.471 Da / Num. of mol.: 15
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium hassiacum DSM 44199 (bacteria)
Gene: lin, C731_3737 / Production host: Escherichia coli (E. coli) / Strain (production host): NEB 10 beta
References: UniProt: K5BEG2, Hydrolases; Acting on peptide bonds (peptidases)

#2: Chemical

A-301 A-302 A-303 A-304 A-305 A-306 A-307 A-308 B-301 B-302 B-303 B-304 B-305 B-306 B-307 B-308 C-301 C-302 C-303 C-304 ...
ChemComp-SO4 / SULFATE ION

Details:

Mass: 96.063 Da / Num. of mol.: 117 / Source method: obtained synthetically / Formula: SO₄

#3: Chemical

C-311 F-309 L-308 N-308
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL

Details:

Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₃H₈O₃

#4: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 2797 / Source method: isolated from a natural source / Formula: H₂O

• Has protein modification: Y

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 4.4 ų/Da / Density % sol: 72 %
• Crystal grow: Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 5.5 ; Details: 6.0 mg/ml encapsulin. 1.3 -1.6 M ammonium sulfate, 0.1 MES buffer pH 5.5

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P13 (MX1) / Wavelength: 0.97625 Å
• Detector: Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 17, 2015
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.97625 Å / Relative weight: 1
• Reflection: Resolution: 2.5→47.8 Å / Num. obs: 255440 / % possible obs: 98.2 % / Redundancy: 3.6 % / CC_1/2: 0.979 / R_merge(I) obs: 0.12 / R_pim(I) all: 0.084 / Net I/σ(I): 7.1
• Reflection shell: Resolution: 2.5→2.54 Å / Redundancy: 3.5 % / R_merge(I) obs: 0.509 / Mean I/σ(I) obs: 2.4 / Num. unique obs: 12672 / CC_1/2: 0.497 / R_pim(I) all: 0.365 / % possible all: 98.8

Processing

Software

Name	Version	Classification
REFMAC	5.8.0073	refinement
XDS		data reduction
Aimless		data scaling
PHASER		phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: 3DKT

3dkt

Resolution: 2.5→47.8 Å / Cor.coef. F_o:F_c: 0.948 / Cor.coef. F_o:F_c free: 0.921 / SU B: 7.576 / SU ML: 0.155 / Cross valid method: THROUGHOUT / ESU R: 0.25 / ESU R Free: 0.202 / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.21048	12567	4.9 %	RANDOM
Rwork	0.17236	-	-	-
obs	0.17422	242842	97.99 %	-

• Solvent computation: Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å

Displacement parameters

B_iso mean: 28.932 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	1.05 Å2	0 Å2	-0 Å2
2-	-	0.41 Å2	0 Å2
3-	-	-	-1.46 Å2

Refinement step

Cycle: 1 / Resolution: 2.5→47.8 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	30675	0	609	2798	34082

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.019	31808
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.277	1.981	43487
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.688	5	3960
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	33.918	23.368	1425
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.935	15	4920
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	15.972	15	285
X-RAY DIFFRACTION	r_chiral_restr	0.08	0.2	5101
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.021	24000
X-RAY DIFFRACTION	r_gen_planes_other
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	1.456	2.578	15885
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	2.313	3.863	19830
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	3.446	3.064	15923
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined	8.07	22.813	50558
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

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Rms dev position: 0 Å / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number
1	1	A	360
1	2	B	360
2	1	A	364
2	2	C	364
3	1	A	364
3	2	D	364
4	1	A	360
4	2	E	360
5	1	A	362
5	2	F	362
6	1	A	365
6	2	G	365
7	1	A	361
7	2	H	361
8	1	A	357
8	2	I	357
9	1	A	361
9	2	J	361
10	1	A	360
10	2	K	360
11	1	A	363
11	2	L	363
12	1	A	362
12	2	M	362
13	1	A	361
13	2	N	361
14	1	A	360
14	2	O	360
15	1	B	360
15	2	C	360
16	1	B	364
16	2	D	364
17	1	B	360
17	2	E	360
18	1	B	363
18	2	F	363
19	1	B	360
19	2	G	360
20	1	B	359
20	2	H	359
21	1	B	357
21	2	I	357
22	1	B	360
22	2	J	360
23	1	B	360
23	2	K	360
24	1	B	361
24	2	L	361
25	1	B	361
25	2	M	361
26	1	B	360
26	2	N	360
27	1	B	357
27	2	O	357
28	1	C	365
28	2	D	365
29	1	C	361
29	2	E	361
30	1	C	362
30	2	F	362
31	1	C	363
31	2	G	363
32	1	C	360
32	2	H	360
33	1	C	360
33	2	I	360
34	1	C	362
34	2	J	362
35	1	C	361
35	2	K	361
36	1	C	363
36	2	L	363
37	1	C	362
37	2	M	362
38	1	C	364
38	2	N	364
39	1	C	359
39	2	O	359
40	1	D	365
40	2	E	365
41	1	D	366
41	2	F	366
42	1	D	363
42	2	G	363
43	1	D	361
43	2	H	361
44	1	D	362
44	2	I	362
45	1	D	363
45	2	J	363
46	1	D	363
46	2	K	363
47	1	D	366
47	2	L	366
48	1	D	364
48	2	M	364
49	1	D	362
49	2	N	362
50	1	D	361
50	2	O	361
51	1	E	361
51	2	F	361
52	1	E	362
52	2	G	362
53	1	E	356
53	2	H	356
54	1	E	360
54	2	I	360
55	1	E	360
55	2	J	360
56	1	E	363
56	2	K	363
57	1	E	362
57	2	L	362
58	1	E	364
58	2	M	364
59	1	E	361
59	2	N	361
60	1	E	359
60	2	O	359
61	1	F	362
61	2	G	362
62	1	F	361
62	2	H	361
63	1	F	360
63	2	I	360
64	1	F	361
64	2	J	361
65	1	F	362
65	2	K	362
66	1	F	362
66	2	L	362
67	1	F	362
67	2	M	362
68	1	F	362
68	2	N	362
69	1	F	359
69	2	O	359
70	1	G	360
70	2	H	360
71	1	G	360
71	2	I	360
72	1	G	362
72	2	J	362
73	1	G	362
73	2	K	362
74	1	G	362
74	2	L	362
75	1	G	364
75	2	M	364
76	1	G	364
76	2	N	364
77	1	G	358
77	2	O	358
78	1	H	355
78	2	I	355
79	1	H	361
79	2	J	361
80	1	H	357
80	2	K	357
81	1	H	358
81	2	L	358
82	1	H	359
82	2	M	359
83	1	H	360
83	2	N	360
84	1	H	357
84	2	O	357
85	1	I	361
85	2	J	361
86	1	I	362
86	2	K	362
87	1	I	364
87	2	L	364
88	1	I	362
88	2	M	362
89	1	I	362
89	2	N	362
90	1	I	360
90	2	O	360
91	1	J	364
91	2	K	364
92	1	J	365
92	2	L	365
93	1	J	366
93	2	M	366
94	1	J	365
94	2	N	365
95	1	J	361
95	2	O	361
96	1	K	365
96	2	L	365
97	1	K	365
97	2	M	365
98	1	K	363
98	2	N	363
99	1	K	363
99	2	O	363
100	1	L	365
100	2	M	365
101	1	L	363
101	2	N	363
102	1	L	363
102	2	O	363
103	1	M	365
103	2	N	365
104	1	M	362
104	2	O	362
105	1	N	362
105	2	O	362

LS refinement shell

Resolution: 2.5→2.565 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.307	966	-
Rwork	0.279	17978	-
obs	-	-	98.85 %