PDB-5oat: PINK1 structure

Basic information

• Entry: Database: PDB / ID: 5oat
• Title: PINK1 structure
• Components: Serine/threonine-protein kinase PINK1, mitochondrial-like Protein
• Keywords: Kinase / Kinase for phosphorylation

Function / homology

Function:

positive regulation of free ubiquitin chain polymerization / autophagy of mitochondrion / positive regulation of mitochondrial fission / positive regulation of protein ubiquitination / peptidyl-serine phosphorylation / protein autophosphorylation / regulation of apoptotic process / mitochondrial outer membrane / mitochondrial inner membrane / non-specific serine/threonine protein kinase / protein serine/threonine kinase activity / ubiquitin protein ligase binding / mitochondrion / ATP binding / metal ion binding / cytosol

Domain/homology:

: / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily

Component:

Serine/threonine-protein kinase Pink1, mitochondrial

• Biological species: Tribolium castaneum (red flour beetle)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.78 Å
• Authors: Kumar, A. / Tamjar, J. / Woodroof, H.I. / Raimi, O.G. / Waddell, A.Y. / Peggie, M. / Muqit, M.M.K. / van Aalten, D.M.F.

Funding support

United Kingdom, 2items

Organization	Grant number	Country
Wellcome Trust	101022/Z/13/Z	United Kingdom
Wellcome Trust	110061	United Kingdom

• Citation: Journal: Elife / Year: 2017; Title: Structure of PINK1 and mechanisms of Parkinson's disease associated mutations.; Authors: Kumar, A. / Tamjar, J. / Waddell, A.D. / Woodroof, H.I. / Raimi, O.G. / Shaw, A.M. / Peggie, M. / Muqit, M.M. / van Aalten, D.M.

History

Deposition	Jun 23, 2017	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Oct 11, 2017	Provider: repository / Type: Initial release
Revision 1.1	Oct 18, 2017	Group: Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2	Oct 16, 2024	Group: Data collection / Database references / Derived calculations / Refinement description / Structure summary Category: chem_comp_atom / chem_comp_bond / database_2 / entity_name_com / pdbx_entry_details / pdbx_modification_feature / struct_conn / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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_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

Assembly

Deposited unit

A: Serine/threonine-protein kinase PINK1, mitochondrial-like Protein

B: Serine/threonine-protein kinase PINK1, mitochondrial-like Protein

C: Serine/threonine-protein kinase PINK1, mitochondrial-like Protein

D: Serine/threonine-protein kinase PINK1, mitochondrial-like Protein

E: Serine/threonine-protein kinase PINK1, mitochondrial-like Protein

F: Serine/threonine-protein kinase PINK1, mitochondrial-like Protein

hetero molecules

Summary:

• 279 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	279,081	12
Polymers	278,935	6
Non-polymers	146	6
Water	540	30

1

Summary:

• Idetical with deposited unit
• defined by author&software

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Method	PISA

Unit cell

Length a, b, c (Å)	84.915, 116.736, 179.344
Angle α, β, γ (deg.)	90.00, 94.29, 90.00
Int Tables number	4
Space group name H-M	P1211

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
1	2	A
2	2	B
1	3	A
2	3	B
1	4	A
2	4	B
1	5	A
2	5	B
1	6	A
2	6	C
1	7	A
2	7	C
1	8	A
2	8	C
1	9	A
2	9	C
1	10	A
2	10	C
1	11	A
2	11	D
1	12	A
2	12	D
1	13	A
2	13	D
1	14	A
2	14	D
1	15	A
2	15	D
1	16	A
2	16	E
1	17	A
2	17	E
1	18	A
2	18	E
1	19	A
2	19	E
1	20	A
2	20	E
1	21	A
2	21	F
1	22	A
2	22	F
1	23	A
2	23	F
1	24	A
2	24	F
1	25	A
2	25	F
1	26	B
2	26	C
1	27	B
2	27	D
1	28	B
2	28	E
1	29	B
2	29	F
1	30	B
2	30	C
1	31	B
2	31	D
1	32	B
2	32	E
1	33	B
2	33	F
1	34	B
2	34	C
1	35	B
2	35	D
1	36	B
2	36	E
1	37	B
2	37	F
1	38	B
2	38	C
1	39	B
2	39	D
1	40	B
2	40	E
1	41	B
2	41	F
1	42	B
2	42	C
1	43	B
2	43	D
1	44	B
2	44	E
1	45	B
2	45	F
1	46	C
2	46	D
1	47	C
2	47	E
1	48	C
2	48	F
1	49	C
2	49	D
1	50	C
2	50	E
1	51	C
2	51	F
1	52	C
2	52	D
1	53	C
2	53	E
1	54	C
2	54	F
1	55	C
2	55	D
1	56	C
2	56	E
1	57	C
2	57	F
1	58	C
2	58	D
1	59	C
2	59	E
1	60	C
2	60	F
1	61	D
2	61	E
1	62	D
2	62	F
1	63	D
2	63	E
1	64	D
2	64	F
1	65	D
2	65	E
1	66	D
2	66	F
1	67	D
2	67	E
1	68	D
2	68	F
1	69	D
2	69	E
1	70	D
2	70	F
1	71	E
2	71	F
1	72	E
2	72	F
1	73	E
2	73	F
1	74	E
2	74	F
1	75	E
2	75	F

NCS domain segments:

Component-ID: 1 / Refine code: 1

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	PRO	PRO	VAL	VAL	A	A	156 - 181	7 - 32
2	1	PRO	PRO	VAL	VAL	B	B	156 - 181	7 - 32
1	2	TYR	TYR	ASP	ASP	A	A	191 - 259	42 - 110
2	2	TYR	TYR	ASP	ASP	B	B	191 - 259	42 - 110
1	3	ASN	ASN	PRO	PRO	A	A	287 - 493	128 - 334
2	3	ASN	ASN	PRO	PRO	B	B	287 - 493	128 - 334
1	4	LYS	LYS	VAL	VAL	A	A	496 - 514	337 - 355
2	4	LYS	LYS	VAL	VAL	B	B	496 - 514	337 - 355
1	5	THR	THR	ASN	ASN	A	A	536 - 565	377 - 406
2	5	THR	THR	ASN	ASN	B	B	536 - 565	377 - 406
1	6	PRO	PRO	VAL	VAL	A	A	156 - 181	7 - 32
2	6	PRO	PRO	VAL	VAL	C	C	156 - 181	7 - 32
1	7	TYR	TYR	ASP	ASP	A	A	191 - 259	42 - 110
2	7	TYR	TYR	ASP	ASP	C	C	191 - 259	42 - 110
1	8	ASN	ASN	PRO	PRO	A	A	287 - 493	128 - 334
2	8	ASN	ASN	PRO	PRO	C	C	287 - 493	128 - 334
1	9	LYS	LYS	VAL	VAL	A	A	496 - 514	337 - 355
2	9	LYS	LYS	VAL	VAL	C	C	496 - 514	337 - 355
1	10	THR	THR	ASN	ASN	A	A	536 - 565	377 - 406
2	10	THR	THR	ASN	ASN	C	C	536 - 565	377 - 406
1	11	PRO	PRO	VAL	VAL	A	A	156 - 181	7 - 32
2	11	PRO	PRO	VAL	VAL	D	D	156 - 181	7 - 32
1	12	TYR	TYR	ASP	ASP	A	A	191 - 259	42 - 110
2	12	TYR	TYR	ASP	ASP	D	D	191 - 259	42 - 110
1	13	ASN	ASN	PRO	PRO	A	A	287 - 493	128 - 334
2	13	ASN	ASN	PRO	PRO	D	D	287 - 493	128 - 334
1	14	LYS	LYS	VAL	VAL	A	A	496 - 514	337 - 355
2	14	LYS	LYS	VAL	VAL	D	D	496 - 514	337 - 355
1	15	THR	THR	ASN	ASN	A	A	536 - 565	377 - 406
2	15	THR	THR	ASN	ASN	D	D	536 - 565	377 - 406
1	16	PRO	PRO	VAL	VAL	A	A	156 - 181	7 - 32
2	16	PRO	PRO	VAL	VAL	E	E	156 - 181	7 - 32
1	17	TYR	TYR	ASP	ASP	A	A	191 - 259	42 - 110
2	17	TYR	TYR	ASP	ASP	E	E	191 - 259	42 - 110
1	18	ASN	ASN	PRO	PRO	A	A	287 - 493	128 - 334
2	18	ASN	ASN	PRO	PRO	E	E	287 - 493	128 - 334
1	19	LYS	LYS	VAL	VAL	A	A	496 - 514	337 - 355
2	19	LYS	LYS	VAL	VAL	E	E	496 - 514	337 - 355
1	20	THR	THR	ASN	ASN	A	A	536 - 565	377 - 406
2	20	THR	THR	ASN	ASN	E	E	536 - 565	377 - 406
1	21	PRO	PRO	VAL	VAL	A	A	156 - 181	7 - 32
2	21	PRO	PRO	VAL	VAL	F	F	156 - 181	7 - 32
1	22	TYR	TYR	ASP	ASP	A	A	191 - 259	42 - 110
2	22	TYR	TYR	ASP	ASP	F	F	191 - 259	42 - 110
1	23	ASN	ASN	PRO	PRO	A	A	287 - 493	128 - 334
2	23	ASN	ASN	PRO	PRO	F	F	287 - 493	128 - 334
1	24	LYS	LYS	VAL	VAL	A	A	496 - 514	337 - 355
2	24	LYS	LYS	VAL	VAL	F	F	496 - 514	337 - 355
1	25	THR	THR	ASN	ASN	A	A	536 - 565	377 - 406
2	25	THR	THR	ASN	ASN	F	F	536 - 565	377 - 406
1	26	PRO	PRO	LYS	LYS	B	B	156 - 182	7 - 33
2	26	PRO	PRO	LYS	LYS	C	C	156 - 182	7 - 33
1	27	PRO	PRO	LYS	LYS	B	B	156 - 182	7 - 33
2	27	PRO	PRO	LYS	LYS	D	D	156 - 182	7 - 33
1	28	PRO	PRO	LYS	LYS	B	B	156 - 182	7 - 33
2	28	PRO	PRO	LYS	LYS	E	E	156 - 182	7 - 33
1	29	PRO	PRO	LYS	LYS	B	B	156 - 182	7 - 33
2	29	PRO	PRO	LYS	LYS	F	F	156 - 182	7 - 33
1	30	TYR	TYR	LEU	LEU	B	B	191 - 260	42 - 111
2	30	TYR	TYR	LEU	LEU	C	C	191 - 260	42 - 111
1	31	TYR	TYR	LEU	LEU	B	B	191 - 260	42 - 111
2	31	TYR	TYR	LEU	LEU	D	D	191 - 260	42 - 111
1	32	TYR	TYR	LEU	LEU	B	B	191 - 260	42 - 111
2	32	TYR	TYR	LEU	LEU	E	E	191 - 260	42 - 111
1	33	TYR	TYR	LEU	LEU	B	B	191 - 260	42 - 111
2	33	TYR	TYR	LEU	LEU	F	F	191 - 260	42 - 111
1	34	ASN	ASN	GLY	GLY	B	B	287 - 494	128 - 335
2	34	ASN	ASN	GLY	GLY	C	C	287 - 494	128 - 335
1	35	ASN	ASN	GLY	GLY	B	B	287 - 494	128 - 335
2	35	ASN	ASN	GLY	GLY	D	D	287 - 494	128 - 335
1	36	ASN	ASN	GLY	GLY	B	B	287 - 494	128 - 335
2	36	ASN	ASN	GLY	GLY	E	E	287 - 494	128 - 335
1	37	ASN	ASN	GLY	GLY	B	B	287 - 494	128 - 335
2	37	ASN	ASN	GLY	GLY	F	F	287 - 494	128 - 335
1	38	LYS	LYS	LEU	LEU	B	B	496 - 515	337 - 356
2	38	LYS	LYS	LEU	LEU	C	C	496 - 515	337 - 356
1	39	LYS	LYS	LEU	LEU	B	B	496 - 515	337 - 356
2	39	LYS	LYS	LEU	LEU	D	D	496 - 515	337 - 356
1	40	LYS	LYS	LEU	LEU	B	B	496 - 515	337 - 356
2	40	LYS	LYS	LEU	LEU	E	E	496 - 515	337 - 356
1	41	LYS	LYS	LEU	LEU	B	B	496 - 515	337 - 356
2	41	LYS	LYS	LEU	LEU	F	F	496 - 515	337 - 356
1	42	THR	THR	LEU	LEU	B	B	536 - 566	377 - 407
2	42	THR	THR	LEU	LEU	C	C	536 - 566	377 - 407
1	43	THR	THR	LEU	LEU	B	B	536 - 566	377 - 407
2	43	THR	THR	LEU	LEU	D	D	536 - 566	377 - 407
1	44	THR	THR	LEU	LEU	B	B	536 - 566	377 - 407
2	44	THR	THR	LEU	LEU	E	E	536 - 566	377 - 407
1	45	THR	THR	LEU	LEU	B	B	536 - 566	377 - 407
2	45	THR	THR	LEU	LEU	F	F	536 - 566	377 - 407
1	46	PRO	PRO	LYS	LYS	C	C	156 - 182	7 - 33
2	46	PRO	PRO	LYS	LYS	D	D	156 - 182	7 - 33
1	47	PRO	PRO	LYS	LYS	C	C	156 - 182	7 - 33
2	47	PRO	PRO	LYS	LYS	E	E	156 - 182	7 - 33
1	48	PRO	PRO	LYS	LYS	C	C	156 - 182	7 - 33
2	48	PRO	PRO	LYS	LYS	F	F	156 - 182	7 - 33
1	49	TYR	TYR	LEU	LEU	C	C	191 - 260	42 - 111
2	49	TYR	TYR	LEU	LEU	D	D	191 - 260	42 - 111
1	50	TYR	TYR	LEU	LEU	C	C	191 - 260	42 - 111
2	50	TYR	TYR	LEU	LEU	E	E	191 - 260	42 - 111
1	51	TYR	TYR	LEU	LEU	C	C	191 - 260	42 - 111
2	51	TYR	TYR	LEU	LEU	F	F	191 - 260	42 - 111
1	52	ASN	ASN	GLY	GLY	C	C	287 - 494	128 - 335
2	52	ASN	ASN	GLY	GLY	D	D	287 - 494	128 - 335
1	53	ASN	ASN	GLY	GLY	C	C	287 - 494	128 - 335
2	53	ASN	ASN	GLY	GLY	E	E	287 - 494	128 - 335
1	54	ASN	ASN	GLY	GLY	C	C	287 - 494	128 - 335
2	54	ASN	ASN	GLY	GLY	F	F	287 - 494	128 - 335
1	55	LYS	LYS	LEU	LEU	C	C	496 - 515	337 - 356
2	55	LYS	LYS	LEU	LEU	D	D	496 - 515	337 - 356
1	56	LYS	LYS	LEU	LEU	C	C	496 - 515	337 - 356
2	56	LYS	LYS	LEU	LEU	E	E	496 - 515	337 - 356
1	57	LYS	LYS	LEU	LEU	C	C	496 - 515	337 - 356
2	57	LYS	LYS	LEU	LEU	F	F	496 - 515	337 - 356
1	58	THR	THR	LEU	LEU	C	C	536 - 566	377 - 407
2	58	THR	THR	LEU	LEU	D	D	536 - 566	377 - 407
1	59	THR	THR	LEU	LEU	C	C	536 - 566	377 - 407
2	59	THR	THR	LEU	LEU	E	E	536 - 566	377 - 407
1	60	THR	THR	LEU	LEU	C	C	536 - 566	377 - 407
2	60	THR	THR	LEU	LEU	F	F	536 - 566	377 - 407
1	61	PRO	PRO	LYS	LYS	D	D	156 - 182	7 - 33
2	61	PRO	PRO	LYS	LYS	E	E	156 - 182	7 - 33
1	62	PRO	PRO	LYS	LYS	D	D	156 - 182	7 - 33
2	62	PRO	PRO	LYS	LYS	F	F	156 - 182	7 - 33
1	63	TYR	TYR	LEU	LEU	D	D	191 - 260	42 - 111
2	63	TYR	TYR	LEU	LEU	E	E	191 - 260	42 - 111
1	64	TYR	TYR	LEU	LEU	D	D	191 - 260	42 - 111
2	64	TYR	TYR	LEU	LEU	F	F	191 - 260	42 - 111
1	65	ASN	ASN	GLY	GLY	D	D	287 - 494	128 - 335
2	65	ASN	ASN	GLY	GLY	E	E	287 - 494	128 - 335
1	66	ASN	ASN	GLY	GLY	D	D	287 - 494	128 - 335
2	66	ASN	ASN	GLY	GLY	F	F	287 - 494	128 - 335
1	67	LYS	LYS	LEU	LEU	D	D	496 - 515	337 - 356
2	67	LYS	LYS	LEU	LEU	E	E	496 - 515	337 - 356
1	68	LYS	LYS	LEU	LEU	D	D	496 - 515	337 - 356
2	68	LYS	LYS	LEU	LEU	F	F	496 - 515	337 - 356
1	69	THR	THR	LEU	LEU	D	D	536 - 566	377 - 407
2	69	THR	THR	LEU	LEU	E	E	536 - 566	377 - 407
1	70	THR	THR	LEU	LEU	D	D	536 - 566	377 - 407
2	70	THR	THR	LEU	LEU	F	F	536 - 566	377 - 407
1	71	PRO	PRO	LYS	LYS	E	E	156 - 182	7 - 33
2	71	PRO	PRO	LYS	LYS	F	F	156 - 182	7 - 33
1	72	TYR	TYR	LEU	LEU	E	E	191 - 260	42 - 111
2	72	TYR	TYR	LEU	LEU	F	F	191 - 260	42 - 111
1	73	ASN	ASN	GLY	GLY	E	E	287 - 494	128 - 335
2	73	ASN	ASN	GLY	GLY	F	F	287 - 494	128 - 335
1	74	LYS	LYS	LEU	LEU	E	E	496 - 515	337 - 356
2	74	LYS	LYS	LEU	LEU	F	F	496 - 515	337 - 356
1	75	THR	THR	LEU	LEU	E	E	536 - 566	377 - 407
2	75	THR	THR	LEU	LEU	F	F	536 - 566	377 - 407

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

NCS oper:

ID	Code	Matrix	Vector
1	given	(0.995592, 0.09251, -0.015417), (0.057675, -0.474306, 0.878469), (0.073955, -0.875486, -0.477551)	28.41683, -60.01979, 165.45854
2	given	(0.996265, 0.086091, -0.006731), (0.045689, -0.459364, 0.887072), (0.073277, -0.884066, -0.461582)	27.62628, -59.92745, 164.14888
3	given	(0.997254, 0.066407, -0.032767), (0.060443, -0.474342, 0.878263), (0.04278, -0.877832, -0.477054)	30.4757, -60.04947, 168.4165
4	given	(0.998168, 0.059098, -0.012977), (0.039368, -0.471466, 0.881005), (0.045948, -0.879902, -0.472929)	28.08702, -58.50647, 167.54953
5	given	(0.998308, 0.05155, -0.026905), (0.048427, -0.480911, 0.875431), (0.032189, -0.875253, -0.482593)	29.57728, -58.84623, 169.88838
6	given	(0.995059, -0.041746, 0.090085), (0.065305, -0.408253, -0.91053), (0.074788, 0.911914, -0.403509)	48.3651, 124.6976, 118.84543
7	given	(0.995485, -0.055918, 0.076705), (0.046852, -0.413336, -0.909373), (0.082556, 0.90886, -0.408849)	49.99892, 125.85579, 118.97699
8	given	(0.995372, -0.023763, 0.093108), (0.07634, -0.392926, -0.916396), (0.058361, 0.919263, -0.389294)	47.55735, 124.16548, 118.21523
9	given	(0.996272, -0.026752, 0.082021), (0.065821, -0.37891, -0.92309), (0.055773, 0.925047, -0.375736)	48.40938, 124.75771, 117.13657
10	given	(0.996536, -0.023965, 0.07963), (0.064482, -0.381982, -0.921917), (0.052511, 0.923859, -0.379114)	48.40635, 124.84362, 117.61876
11	given	(-0.995972, 0.089101, 0.010067), (-0.050081, -0.459624, -0.886701), (-0.074379, -0.883633, 0.462234)	174.47696, 187.43269, 54.10045
12	given	(-0.997249, 0.073334, 0.010814), (-0.042504, -0.446178, -0.893934), (-0.060731, -0.891935, 0.448067)	174.71968, 188.08467, 55.93037
13	given	(-0.99699, 0.074338, 0.022005), (-0.052919, -0.445122, -0.893905), (-0.056656, -0.892379, 0.447716)	172.88831, 188.80759, 55.7837
14	given	(-0.996777, 0.079974, 0.006285), (-0.041564, -0.447851, -0.893141), (-0.068614, -0.890524, 0.449732)	175.39119, 187.75586, 56.36553
15	given	(-0.997679, 0.065827, 0.017405), (-0.045161, -0.448421, -0.892681), (-0.050958, -0.891395, 0.450353)	173.5856, 187.98726, 55.06374
16	given	(-0.999645, -0.025935, 0.006043), (-0.026431, 0.993983, -0.106297), (-0.00325, -0.106419, -0.994316)	149.77829, 15.0525, 271.73584
17	given	(-0.999691, -0.024802, 0.001372), (-0.024825, 0.995651, -0.089788), (0.000861, -0.089794, -0.99596)	150.4454, 12.36825, 271.53592
18	given	(-0.999649, -0.026271, -0.003469), (-0.025835, 0.995327, -0.093043), (0.005897, -0.092921, -0.995656)	151.24353, 12.9845, 271.42752
19	given	(-0.999688, -0.024935, -0.001401), (-0.024666, 0.994586, -0.100951), (0.003911, -0.100885, -0.99489)	150.80978, 14.26114, 271.75012
20	given	(-0.999666, -0.025719, -0.00248), (-0.025378, 0.995364, -0.092771), (0.004855, -0.092677, -0.995684)	151.07394, 12.96904, 271.44266
21	given	(-0.992625, -0.057312, -0.106818), (-0.076459, -0.387792, 0.91857), (-0.094069, 0.919963, 0.380551)	225.15512, -110.10123, 23.23346
22	given	(-0.993449, -0.07232, -0.088477), (-0.052677, -0.397256, 0.916195), (-0.101407, 0.914854, 0.390844)	222.5544, -111.49461, 22.26297
23	given	(-0.993664, -0.04295, -0.103858), (-0.080624, -0.371402, 0.924965), (-0.0783, 0.927478, 0.365586)	224.33752, -111.36979, 24.19684
24	given	(-0.994768, -0.045668, -0.091387), (-0.069681, -0.35086, 0.933832), (-0.07471, 0.935314, 0.345842)	222.01207, -114.93782, 27.5215
25	given	(-0.994804, -0.043695, -0.091955), (-0.070237, -0.359294, 0.930578), (-0.073701, 0.932201, 0.354358)	222.08292, -113.90993, 25.75983
26	given	(0.99997, 0.002496, 0.007361), (-0.004321, -0.60872, 0.793373), (0.006461, -0.793381, -0.608691)	27.0581, -44.94761, 184.22339
27	given	(-0.99997, -0.003129, -0.007112), (-0.003249, 0.999851, 0.016968), (0.007058, 0.016991, -0.999831)	151.48251, -6.38999, 268.29153
28	given	(-0.996996, 0.023495, -0.073805), (-0.077187, -0.380534, 0.92154), (-0.006433, 0.924468, 0.381205)	133.04396, -117.43245, 13.35614
29	given	(-0.999618, -0.011219, -0.025276), (0.026723, -0.626978, -0.778578), (-0.007113, -0.778956, 0.627038)	182.4671, 166.45876, 20.87132
30	given	(0.999958, -0.007867, 0.004808), (-0.008644, -0.618478, 0.785755), (-0.003208, -0.785763, -0.618519)	27.4739, -43.48745, 185.50475
31	given	(-0.999917, -0.012541, 0.003014), (-0.012493, 0.999803, 0.015416), (-0.003207, 0.015377, -0.999877)	149.90355, -5.5959, 268.98248
32	given	(-0.997033, 0.014166, -0.075656), (-0.075353, -0.380092, 0.921874), (-0.015697, 0.92484, 0.380032)	133.52431, -117.58001, 13.74195
33	given	(-0.999582, -0.022987, -0.017531), (0.028121, -0.632483, -0.774064), (0.006705, -0.774233, 0.632865)	181.42259, 165.93102, 18.45298
34	given	(0.999752, -0.008134, 0.020734), (-0.021292, -0.62217, 0.782593), (0.006535, -0.78284, -0.622189)	26.02759, -42.17961, 185.18187
35	given	(-0.999875, 0.009021, -0.012982), (0.008596, 0.999437, 0.03243), (0.013268, 0.032314, -0.99939)	152.25293, -9.70679, 267.62399
36	given	(-0.998213, 0.030004, -0.05167), (-0.059305, -0.392233, 0.917952), (0.007275, 0.919377, 0.393311)	129.25537, -117.05778, 11.05207
37	given	(-0.999161, -0.025617, -0.031966), (0.040955, -0.640875, -0.766552), (-0.00085, -0.767218, 0.641386)	184.04681, 163.81908, 17.36568
38	given	(0.999607, 0.000953, 0.02801), (-0.020988, -0.636861, 0.770693), (0.018573, -0.770978, -0.636591)	25.19455, -40.86082, 185.04382
39	given	(-0.999735, 0.021283, -0.008808), (0.021049, 0.999442, 0.025919), (0.009355, 0.025727, -0.999625)	151.70627, -9.59274, 267.59088
40	given	(-0.998682, 0.009225, -0.050495), (-0.050197, -0.381177, 0.923138), (-0.010731, 0.924456, 0.381137)	130.10268, -118.82602, 13.29095
41	given	(-0.999154, -0.016379, -0.037721), (0.03914, -0.660194, -0.750074), (-0.012617, -0.750916, 0.660277)	184.73534, 161.35313, 13.964
42	given	(0.999644, -0.013598, 0.022941), (-0.026399, -0.62636, 0.779087), (0.003775, -0.779416, -0.626496)	26.02232, -41.55217, 185.56796
43	given	(-0.999802, 0.016044, -0.011757), (0.015614, 0.999237, 0.035804), (0.012323, 0.035613, -0.99929)	152.08643, -10.79545, 267.59683
44	given	(-0.99907, 0.019807, -0.038304), (-0.043026, -0.398624, 0.916105), (0.002876, 0.916901, 0.399105)	127.92292, -117.21579, 10.60359
45	given	(-0.998903, -0.03098, -0.035107), (0.046812, -0.645429, -0.762384), (0.000959, -0.763192, 0.646172)	184.82863, 162.56711, 16.15036
46	given	(-0.99988, -0.007334, -0.013632), (-0.00611, -0.622135, 0.782886), (-0.014222, 0.782876, 0.622015)	124.79475, -89.85591, -19.66874
47	given	(-0.996673, 0.031125, -0.075328), (0.049601, -0.501756, -0.863586), (-0.064675, -0.864449, 0.498542)	105.19261, 179.95061, 47.27906
48	given	(-0.999749, -0.013555, -0.017845), (-0.013132, 0.999635, -0.023621), (0.018159, -0.023381, -0.999562)	153.43358, 1.30455, 268.30087
49	given	(-0.999756, -0.021224, 0.006097), (0.018115, -0.630341, 0.776107), (-0.012629, 0.776028, 0.630572)	121.82757, -89.9918, -21.27138
50	given	(-0.996289, 0.014485, -0.084846), (0.066786, -0.491738, -0.868178), (-0.054297, -0.870623, 0.488945)	107.23815, 179.95503, 48.53013
51	given	(-0.999804, -0.015032, -0.012873), (-0.014794, 0.999721, -0.0184), (0.013146, -0.018206, -0.999748)	152.66826, 0.5305, 268.61618
52	given	(-0.999723, -0.012049, -0.020205), (-0.007606, -0.647191, 0.76229), (-0.022261, 0.762233, 0.64692)	126.042, -85.76876, -23.26443
53	given	(-0.996655, 0.044362, -0.068631), (0.039318, -0.475926, -0.878606), (-0.071639, -0.878366, 0.47259)	103.65802, 182.0636, 51.8843
54	given	(-0.99979, -0.016975, -0.011446), (-0.016685, 0.99955, -0.024919), (0.011864, -0.024723, -0.999624)	152.49724, 1.92168, 268.90277
55	given	(-0.99961, 0.000786, -0.027915), (-0.021577, -0.656323, 0.754172), (-0.017728, 0.75448, 0.656084)	127.3391, -83.4341, -24.90791
56	given	(-0.997431, 0.034408, -0.062825), (0.039329, -0.469985, -0.881798), (-0.059868, -0.882003, 0.467425)	103.3193, 182.16878, 52.18711
57	given	(-0.999818, -0.016453, -0.009691), (-0.016141, 0.999376, -0.031407), (0.010201, -0.031245, -0.99946)	152.05418, 3.26884, 269.2225
58	given	(-0.999812, -0.010226, -0.016464), (-0.005772, -0.653856, 0.756597), (-0.018502, 0.75655, 0.653674)	125.51589, -84.91496, -24.53562
59	given	(-0.997568, 0.033785, -0.060968), (0.038292, -0.465237, -0.884358), (-0.058243, -0.884541, 0.462811)	103.20113, 182.377, 53.00321
60	given	(-0.99978, -0.016811, -0.012524), (-0.016485, 0.999535, -0.025633), (0.012949, -0.025421, -0.999593)	152.72072, 2.03527, 268.80969
61	given	(0.997171, -0.015741, 0.073495), (-0.074164, -0.364837, 0.928113), (0.012205, -0.930938, -0.364972)	17.00023, -115.30032, 253.13855
62	given	(0.999451, 0.007764, 0.032224), (0.029725, -0.6401, -0.767716), (0.014666, 0.768252, -0.639979)	-33.29072, 168.5208, 250.09482
63	given	(0.997942, -0.012368, 0.062923), (-0.06308, -0.36597, 0.928486), (0.011545, -0.930544, -0.365997)	18.59344, -115.68173, 253.4321
64	given	(0.999126, 0.033368, 0.025165), (0.040749, -0.643978, -0.763958), (-0.009286, 0.764316, -0.644775)	-32.85495, 167.24565, 253.23853
65	given	(0.997675, -0.021173, 0.064773), (-0.068042, -0.362033, 0.929679), (0.003766, -0.931925, -0.362632)	18.66776, -115.78884, 253.23259
66	given	(0.999376, 0.009919, 0.033886), (0.031889, -0.665539, -0.745681), (0.015156, 0.746297, -0.665441)	-33.61906, 165.62808, 255.31978
67	given	(0.997257, -0.008611, 0.073511), (-0.071736, -0.356977, 0.931355), (0.018222, -0.934074, -0.356616)	16.91619, -116.17356, 251.56296
68	given	(0.999595, -0.004566, 0.028086), (0.017505, -0.679497, -0.733469), (0.022433, 0.733664, -0.679142)	-31.79103, 165.03023, 257.67209
69	given	(0.998236, -0.014726, 0.057509), (-0.058911, -0.365348, 0.929005), (0.00733, -0.930754, -0.365572)	19.33146, -115.87961, 253.28467
70	given	(0.999448, 0.011506, 0.03117), (0.030801, -0.672613, -0.739353), (0.012458, 0.739905, -0.672596)	-33.13006, 164.799, 257.09015
71	given	(0.994596, 0.064601, 0.081271), (-0.040235, -0.481789, 0.875363), (0.095705, -0.873903, -0.476586)	-71.23752, -99.9222, 260.8317
72	given	(0.994392, 0.082733, 0.065883), (-0.018655, -0.475966, 0.879266), (0.104102, -0.875564, -0.471753)	-69.19513, -102.72418, 259.52744
73	given	(0.994941, 0.05799, 0.08204), (-0.046831, -0.454751, 0.889387), (0.088883, -0.888729, -0.449734)	-71.3057, -102.7207, 257.48282
74	given	(0.996005, 0.05758, 0.068253), (-0.035804, -0.442696, 0.895957), (0.081805, -0.894821, -0.438866)	-68.63625, -105.67027, 256.13992
75	given	(0.995963, 0.056529, 0.069733), (-0.037563, -0.443099, 0.895685), (0.081531, -0.894689, -0.439186)	-68.87456, -105.31569, 256.34393

Components

#1: Protein

A B C D E F
Serine/threonine-protein kinase PINK1, mitochondrial-like Protein / PINK1

Details:

Mass: 46489.184 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Details: Ser is phosphorylated / Source: (gene. exp.) Tribolium castaneum (red flour beetle) / Gene: TcasGA2_TC013202 / Production host: Escherichia coli (E. coli) / References: UniProt: D6WMX4

#2: Chemical

A-601 C-601 C-602 E-601 E-602 F-601
ChemComp-MG / MAGNESIUM ION

Details:

Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg

#3: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 30 / 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: 3.64 ų/Da / Density % sol: 66.21 %
• Crystal grow: Temperature: 285 K / Method: vapor diffusion, sitting drop / Details: 200 mM MgCl2, 100 mM HEPES pH 7.0, 20% PEG 6000

Data collection

• Diffraction: Mean temperature: 100 K
• Diffraction source: Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 1.03 Å
• Detector: Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 10, 2017
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 1.03 Å / Relative weight: 1
• Reflection: Resolution: 2.78→178.84 Å / Num. obs: 87762 / % possible obs: 99.9 % / Redundancy: 6.7 % / R_merge(I) obs: 0.085 / Net I/σ(I): 13
• Reflection shell: Resolution: 2.78→2.83 Å / R_merge(I) obs: 1.224

Processing

Software

Name	Version	Classification
REFMAC	5.8.0135	refinement
XDS		data reduction
Aimless		data scaling
CRANK2		phasing

Refinement

Method to determine structure: SAD / Resolution: 2.78→178.84 Å / Cor.coef. F_o:F_c: 0.949 / Cor.coef. F_o:F_c free: 0.938 / SU B: 14.476 / SU ML: 0.275 / Cross valid method: THROUGHOUT / ESU R: 0.583 / ESU R Free: 0.312 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.24619	4195	4.8 %	RANDOM
Rwork	0.20466	-	-	-
obs	0.20661	83545	99.75 %	-

• Solvent computation: Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å

Displacement parameters

B_iso mean: 78.641 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	1.59 Å2	0 Å2	0.72 Å2
2-	-	-2 Å2	0 Å2
3-	-	-	0.31 Å2

Refinement step

Cycle: 1 / Resolution: 2.78→178.84 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	16722	0	6	30	16758

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.014	0.019	17118
X-RAY DIFFRACTION	r_bond_other_d	0.003	0.02	16304
X-RAY DIFFRACTION	r_angle_refined_deg	1.826	1.976	23364
X-RAY DIFFRACTION	r_angle_other_deg	1.164	3	37427
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	7.286	5	2124
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	39.628	24.348	690
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	21.645	15	2700
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.232	15	72
X-RAY DIFFRACTION	r_chiral_restr	0.105	0.2	2712
X-RAY DIFFRACTION	r_gen_planes_refined	0.009	0.021	19128
X-RAY DIFFRACTION	r_gen_planes_other	0.003	0.02	3792
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	6.507	7.726	8604
X-RAY DIFFRACTION	r_mcbond_other	6.503	7.725	8603
X-RAY DIFFRACTION	r_mcangle_it	9.782	11.565	10692
X-RAY DIFFRACTION	r_mcangle_other	9.782	11.566	10693
X-RAY DIFFRACTION	r_scbond_it	7.353	8.295	8514
X-RAY DIFFRACTION	r_scbond_other	7.352	8.295	8515
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	11.122	12.262	12673
X-RAY DIFFRACTION	r_long_range_B_refined	14.483	61.909	18639
X-RAY DIFFRACTION	r_long_range_B_other	14.483	61.912	18640
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

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

Ens-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	273	TIGHT POSITIONAL	0.1	0.25
1	A	215	TIGHT POSITIONAL	0.09	0.25
1	A	665	TIGHT POSITIONAL	0.1	0.25
1	A	1833	TIGHT POSITIONAL	0.1	0.25
1	A	175	TIGHT POSITIONAL	0.08	0.25
1	A	273	TIGHT POSITIONAL	0.1	0.25
1	A	215	TIGHT POSITIONAL	0.08	0.25
1	A	665	TIGHT POSITIONAL	0.09	0.25
1	A	1833	TIGHT POSITIONAL	0.09	0.25
1	A	175	TIGHT POSITIONAL	0.07	0.25
1	A	215	TIGHT THERMAL	5.98	2.5
2	A	273	TIGHT POSITIONAL	0.09	0.25
2	A	215	TIGHT POSITIONAL	0.09	0.25
2	A	665	TIGHT POSITIONAL	0.14	0.25
2	A	1833	TIGHT POSITIONAL	0.11	0.25
2	A	175	TIGHT POSITIONAL	0.08	0.25
2	A	273	TIGHT POSITIONAL	0.1	0.25
2	A	220	TIGHT POSITIONAL	0.06	0.11
2	A	220	TIGHT POSITIONAL	0.04	0.11
2	A	220	TIGHT POSITIONAL	0.06	0.11
2	A	220	TIGHT POSITIONAL	0.07	0.11
2	A	665	TIGHT THERMAL	6.22	2.5
3	A	687	TIGHT POSITIONAL	0.08	0.11
3	A	687	TIGHT POSITIONAL	0.07	0.11
3	A	687	TIGHT POSITIONAL	0.07	0.11
3	A	687	TIGHT POSITIONAL	0.08	0.11
3	A	1854	TIGHT POSITIONAL	0.07	0.11
3	A	1854	TIGHT POSITIONAL	0.06	0.11
3	A	1854	TIGHT POSITIONAL	0.08	0.11
3	A	1854	TIGHT POSITIONAL	0.07	0.11
3	A	191	TIGHT POSITIONAL	0.05	0.11
3	A	191	TIGHT POSITIONAL	0.05	0.11
3	A	1833	TIGHT THERMAL	5.94	2.5
4	A	191	TIGHT POSITIONAL	0.04	0.11
4	A	191	TIGHT POSITIONAL	0.05	0.11
4	A	290	TIGHT POSITIONAL	0.05	0.11
4	A	290	TIGHT POSITIONAL	0.05	0.11
4	A	290	TIGHT POSITIONAL	0.05	0.11
4	A	290	TIGHT POSITIONAL	0.05	0.11
4	A	220	TIGHT POSITIONAL	0.07	0.11
4	A	220	TIGHT POSITIONAL	0.05	0.11
4	A	220	TIGHT POSITIONAL	0.04	0.11
4	A	687	TIGHT POSITIONAL	0.09	0.11
4	A	175	TIGHT THERMAL	7.37	2.5
5	A	687	TIGHT POSITIONAL	0.08	0.11
5	A	687	TIGHT POSITIONAL	0.05	0.11
5	A	1854	TIGHT POSITIONAL	0.07	0.11
5	A	1854	TIGHT POSITIONAL	0.07	0.11
5	A	1854	TIGHT POSITIONAL	0.05	0.11
5	A	191	TIGHT POSITIONAL	0.05	0.11
5	A	191	TIGHT POSITIONAL	0.05	0.11
5	A	191	TIGHT POSITIONAL	0.04	0.11
5	A	290	TIGHT POSITIONAL	0.05	0.11
5	A	290	TIGHT POSITIONAL	0.05	0.11
5	A	273	TIGHT THERMAL	7.37	2.5
6	A	290	TIGHT POSITIONAL	0.05	0.11
6	A	220	TIGHT POSITIONAL	0.06	0.11
6	A	220	TIGHT POSITIONAL	0.08	0.11
6	A	687	TIGHT POSITIONAL	0.06	0.11
6	A	687	TIGHT POSITIONAL	0.1	0.11
6	A	1854	TIGHT POSITIONAL	0.07	0.11
6	A	1854	TIGHT POSITIONAL	0.07	0.11
6	A	191	TIGHT POSITIONAL	0.06	0.11
6	A	191	TIGHT POSITIONAL	0.05	0.11
6	A	290	TIGHT POSITIONAL	0.05	0.11
6	A	215	TIGHT THERMAL	9.81	2.5
7	A	290	TIGHT POSITIONAL	0.05	0.11
7	A	220	TIGHT POSITIONAL	0.05	0.11
7	A	687	TIGHT POSITIONAL	0.08	0.11
7	A	1854	TIGHT POSITIONAL	0.07	0.11
7	A	191	TIGHT POSITIONAL	0.05	0.11
7	A	290	TIGHT POSITIONAL	0.05	0.11
7	A	665	TIGHT THERMAL	6.12	2.5
8	A	1833	TIGHT THERMAL	6.53	2.5
9	A	175	TIGHT THERMAL	5.25	2.5
10	A	273	TIGHT THERMAL	5.47	2.5
11	A	215	TIGHT THERMAL	6.73	2.5
12	A	665	TIGHT THERMAL	5.93	2.5
13	A	1833	TIGHT THERMAL	4.75	2.5
14	A	175	TIGHT THERMAL	6.99	2.5
15	A	273	TIGHT THERMAL	6.73	2.5
16	A	215	TIGHT THERMAL	5.66	2.5
17	A	665	TIGHT THERMAL	4.84	2.5
18	A	1833	TIGHT THERMAL	5.64	2.5
19	A	175	TIGHT THERMAL	6.03	2.5
20	A	273	TIGHT THERMAL	7.99	2.5
21	A	215	TIGHT THERMAL	7.58	2.5
22	A	665	TIGHT THERMAL	6.14	2.5
23	A	1833	TIGHT THERMAL	6.26	2.5
24	A	175	TIGHT THERMAL	5.77	2.5
25	A	273	TIGHT THERMAL	4.9	2.5
26	B	220	TIGHT THERMAL	8.99	1.12
27	B	220	TIGHT THERMAL	4.8	1.12
28	B	220	TIGHT THERMAL	6.65	1.12
29	B	220	TIGHT THERMAL	7.46	1.12
30	B	687	TIGHT THERMAL	6.59	1.12
31	B	687	TIGHT THERMAL	6.26	1.12
32	B	687	TIGHT THERMAL	5.49	1.12
33	B	687	TIGHT THERMAL	6.3	1.12
34	B	1854	TIGHT THERMAL	6.67	1.12
35	B	1854	TIGHT THERMAL	4.41	1.12
36	B	1854	TIGHT THERMAL	7.42	1.12
37	B	1854	TIGHT THERMAL	4.87	1.12
38	B	191	TIGHT THERMAL	5.94	1.12
39	B	191	TIGHT THERMAL	3.89	1.12
40	B	191	TIGHT THERMAL	8.96	1.12
41	B	191	TIGHT THERMAL	5.03	1.12
42	B	290	TIGHT THERMAL	7.36	1.12
43	B	290	TIGHT THERMAL	5.07	1.12
44	B	290	TIGHT THERMAL	11.27	1.12
45	B	290	TIGHT THERMAL	6.26	1.12
46	C	220	TIGHT THERMAL	8.91	1.12
47	C	220	TIGHT THERMAL	8.4	1.12
48	C	220	TIGHT THERMAL	5.63	1.12
49	C	687	TIGHT THERMAL	6.82	1.12
50	C	687	TIGHT THERMAL	5.48	1.12
51	C	687	TIGHT THERMAL	4.44	1.12
52	C	1854	TIGHT THERMAL	6.7	1.12
53	C	1854	TIGHT THERMAL	5.87	1.12
54	C	1854	TIGHT THERMAL	4.77	1.12
55	C	191	TIGHT THERMAL	6.16	1.12
56	C	191	TIGHT THERMAL	5.93	1.12
57	C	191	TIGHT THERMAL	4.76	1.12
58	C	290	TIGHT THERMAL	6.53	1.12
59	C	290	TIGHT THERMAL	7.3	1.12
60	C	290	TIGHT THERMAL	4.76	1.12
61	D	220	TIGHT THERMAL	6.34	1.12
62	D	220	TIGHT THERMAL	7.71	1.12
63	D	687	TIGHT THERMAL	6.33	1.12
64	D	687	TIGHT THERMAL	7.22	1.12
65	D	1854	TIGHT THERMAL	6.6	1.12
66	D	1854	TIGHT THERMAL	5.81	1.12
67	D	191	TIGHT THERMAL	8.56	1.12
68	D	191	TIGHT THERMAL	5.63	1.12
69	D	290	TIGHT THERMAL	10.16	1.12
70	D	290	TIGHT THERMAL	4.97	1.12
71	E	220	TIGHT THERMAL	6.41	1.12
72	E	687	TIGHT THERMAL	6.29	1.12
73	E	1854	TIGHT THERMAL	6.94	1.12
74	E	191	TIGHT THERMAL	7.66	1.12
75	E	290	TIGHT THERMAL	7.93	1.12

LS refinement shell

Resolution: 2.78→2.852 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.357	339	-
Rwork	0.332	6080	-
obs	-	-	99.52 %