PDB-9zb8: Crystal Structure of Human GGPPS Bound to Selective Inhibitor CML...

Basic information

• Entry: Database: PDB / ID: 9zb8
• Title: Crystal Structure of Human GGPPS Bound to Selective Inhibitor CML-07-119
• Components: Geranylgeranyl pyrophosphate synthase
• Keywords: TRANSFERASE/INHIBITOR / Inhibitor / complex / isoprenoid / synthesis / TRANSFERASE / TRANSFERASE-INHIBITOR complex

Function / homology

Function:

isoprenoid metabolic process / geranylgeranyl diphosphate synthase / geranyl diphosphate biosynthetic process / dimethylallyltranstransferase / Transferases; Transferring alkyl or aryl groups, other than methyl groups / (2E,6E)-farnesyl diphosphate synthase / Lanosterol biosynthesis / geranylgeranyl diphosphate biosynthetic process / geranylgeranyl diphosphate synthase activity / isoprenoid biosynthetic process / trans, trans-farnesyl diphosphate biosynthetic process / dimethylallyltranstransferase activity / (2E,6E)-farnesyl diphosphate synthase activity / Activation of gene expression by SREBF (SREBP) / Z disc / perinuclear region of cytoplasm / metal ion binding / identical protein binding / cytosol / cytoplasm

Domain/homology:

Polyprenyl synthases signature 1. / Polyprenyl synthases signature 2. / Polyprenyl synthetase, conserved site / Polyprenyl synthetase / Polyprenyl synthetase / Isoprenoid synthase domain superfamily

Component:

: / Geranylgeranyl pyrophosphate synthase

• Biological species: Homo sapiens (human)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.641 Å
• Authors: Ferens, F.G. / Tsantrizos, Y.S. / Lemieux, M.J.

Funding support

Canada, 2items

Organization	Grant number	Country
Natural Sciences and Engineering Research Council (NSERC, Canada)	RGPIN-2023-04396	Canada
Canadian Institutes of Health Research (CIHR)	PJT-159743	Canada

• Citation: Journal: To Be Published; Title: Crystal Structure of Human GGPPS Bound to Selective Inhibitor CML-07-119; Authors: Ferens, F.G. / Tsantrizos, Y.S. / Lemieux, M.J.

History

Deposition	Nov 20, 2025	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 9, 2026	Provider: repository / Type: Initial release

Assembly

Deposited unit

A: Geranylgeranyl pyrophosphate synthase

B: Geranylgeranyl pyrophosphate synthase

C: Geranylgeranyl pyrophosphate synthase

D: Geranylgeranyl pyrophosphate synthase

E: Geranylgeranyl pyrophosphate synthase

F: Geranylgeranyl pyrophosphate synthase

G: Geranylgeranyl pyrophosphate synthase

H: Geranylgeranyl pyrophosphate synthase

I: Geranylgeranyl pyrophosphate synthase

J: Geranylgeranyl pyrophosphate synthase

K: Geranylgeranyl pyrophosphate synthase

L: Geranylgeranyl pyrophosphate synthase

hetero molecules

Summary:

• 427 kDa, 12 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	427,370	60
Polymers	419,675	12
Non-polymers	7,696	48
Water	1,639	91

1

A: Geranylgeranyl pyrophosphate synthase

B: Geranylgeranyl pyrophosphate synthase

C: Geranylgeranyl pyrophosphate synthase

D: Geranylgeranyl pyrophosphate synthase

E: Geranylgeranyl pyrophosphate synthase

F: Geranylgeranyl pyrophosphate synthase

hetero molecules

Summary:

• defined by author
• Evidence: electron microscopy, Hexameric assembly was observed using single particle Cryo-EM., assay for oligomerization, Predominantly Hexameric mass was observed using Mass-Photometry of the protein in solution.
• 214 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	213,685	30
Polymers	209,837	6
Non-polymers	3,848	24
Water	108	6

Symmetry operations:

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

2

G: Geranylgeranyl pyrophosphate synthase

H: Geranylgeranyl pyrophosphate synthase

I: Geranylgeranyl pyrophosphate synthase

J: Geranylgeranyl pyrophosphate synthase

K: Geranylgeranyl pyrophosphate synthase

L: Geranylgeranyl pyrophosphate synthase

hetero molecules

Summary:

• defined by author
• Evidence: electron microscopy, Hexameric assembly was observed using single particle Cryo-EM., assay for oligomerization, Predominantly Hexameric mass was observed using Mass Photometry of the protein in solution.
• 214 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	213,685	30
Polymers	209,837	6
Non-polymers	3,848	24
Water	108	6

Symmetry operations:

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

Unit cell

Length a, b, c (Å)	84.413, 116.167, 214.406
Angle α, β, γ (deg.)	90, 99.272, 90
Int Tables number	4
Space group name H-M	P1211

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details (eV)
1	1	A
2	1	B
3	2	A
4	2	C
5	3	A
6	3	D
7	4	A
8	4	E
9	5	A
10	5	F
11	6	A
12	6	G
13	7	A
14	7	H
15	8	A
16	8	I
17	9	A
18	9	J
19	10	A
20	10	K
21	11	A
22	11	L
23	12	B
24	12	C
25	13	B
26	13	D
27	14	B
28	14	E
29	15	B
30	15	F
31	16	B
32	16	G
33	17	B
34	17	H
35	18	B
36	18	I
37	19	B
38	19	J
39	20	B
40	20	K
41	21	B
42	21	L
43	22	C
44	22	D
45	23	C
46	23	E
47	24	C
48	24	F
49	25	C
50	25	G
51	26	C
52	26	H
53	27	C
54	27	I
55	28	C
56	28	J
57	29	C
58	29	K
59	30	C
60	30	L
61	31	D
62	31	E
63	32	D
64	32	F
65	33	D
66	33	G
67	34	D
68	34	H
69	35	D
70	35	I
71	36	D
72	36	J
73	37	D
74	37	K
75	38	D
76	38	L
77	39	E
78	39	F
79	40	E
80	40	G
81	41	E
82	41	H
83	42	E
84	42	I
85	43	E
86	43	J
87	44	E
88	44	K
89	45	E
90	45	L
91	46	F
92	46	G
93	47	F
94	47	H
95	48	F
96	48	I
97	49	F
98	49	J
99	50	F
100	50	K
101	51	F
102	51	L
103	52	G
104	52	H
105	53	G
106	53	I
107	54	G
108	54	J
109	55	G
110	55	K
111	56	G
112	56	L
113	57	H
114	57	I
115	58	H
116	58	J
117	59	H
118	59	K
119	60	H
120	60	L
121	61	I
122	61	J
123	62	I
124	62	K
125	63	I
126	63	L
127	64	J
128	64	K
129	65	J
130	65	L
131	66	K
132	66	L

NCS domain segments:

Dom-ID	Component-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	1	MET	MET	GLU	GLU	A	A	1 - 297	2 - 298
2	1	1	MET	MET	GLU	GLU	B	B	1 - 297	2 - 298
3	2	2	MET	MET	LYS	LYS	A	A	1 - 296	2 - 297
4	2	2	MET	MET	LYS	LYS	C	C	1 - 296	2 - 297
5	3	3	LYS	LYS	GLU	GLU	A	A	3 - 297	4 - 298
6	3	3	LYS	LYS	GLU	GLU	D	D	3 - 297	4 - 298
7	4	4	THR	THR	GLU	GLU	A	A	4 - 297	5 - 298
8	4	4	THR	THR	GLU	GLU	E	E	4 - 297	5 - 298
9	5	5	MET	MET	LYS	LYS	A	A	1 - 296	2 - 297
10	5	5	MET	MET	LYS	LYS	F	F	1 - 296	2 - 297
11	6	6	MET	MET	GLU	GLU	A	A	1 - 297	2 - 298
12	6	6	MET	MET	GLU	GLU	G	G	1 - 297	2 - 298
13	7	7	MET	MET	GLU	GLU	A	A	1 - 297	2 - 298
14	7	7	MET	MET	GLU	GLU	H	H	1 - 297	2 - 298
15	8	8	MET	MET	LYS	LYS	A	A	1 - 296	2 - 297
16	8	8	MET	MET	LYS	LYS	I	I	1 - 296	2 - 297
17	9	9	THR	THR	GLU	GLU	A	A	4 - 297	5 - 298
18	9	9	THR	THR	GLU	GLU	J	J	4 - 297	5 - 298
19	10	10	THR	THR	GLU	GLU	A	A	4 - 297	5 - 298
20	10	10	THR	THR	GLU	GLU	K	K	4 - 297	5 - 298
21	11	11	MET	MET	LYS	LYS	A	A	1 - 296	2 - 297
22	11	11	MET	MET	LYS	LYS	L	L	1 - 296	2 - 297
23	12	12	MET	MET	LYS	LYS	B	B	1 - 296	2 - 297
24	12	12	MET	MET	LYS	LYS	C	C	1 - 296	2 - 297
25	13	13	LYS	LYS	GLU	GLU	B	B	3 - 297	4 - 298
26	13	13	LYS	LYS	GLU	GLU	D	D	3 - 297	4 - 298
27	14	14	THR	THR	GLU	GLU	B	B	4 - 297	5 - 298
28	14	14	THR	THR	GLU	GLU	E	E	4 - 297	5 - 298
29	15	15	MET	MET	LYS	LYS	B	B	1 - 296	2 - 297
30	15	15	MET	MET	LYS	LYS	F	F	1 - 296	2 - 297
31	16	16	MET	MET	GLU	GLU	B	B	1 - 297	2 - 298
32	16	16	MET	MET	GLU	GLU	G	G	1 - 297	2 - 298
33	17	17	MET	MET	GLU	GLU	B	B	1 - 297	2 - 298
34	17	17	MET	MET	GLU	GLU	H	H	1 - 297	2 - 298
35	18	18	MET	MET	LYS	LYS	B	B	1 - 296	2 - 297
36	18	18	MET	MET	LYS	LYS	I	I	1 - 296	2 - 297
37	19	19	THR	THR	GLU	GLU	B	B	4 - 297	5 - 298
38	19	19	THR	THR	GLU	GLU	J	J	4 - 297	5 - 298
39	20	20	THR	THR	GLU	GLU	B	B	4 - 297	5 - 298
40	20	20	THR	THR	GLU	GLU	K	K	4 - 297	5 - 298
41	21	21	MET	MET	LYS	LYS	B	B	1 - 296	2 - 297
42	21	21	MET	MET	LYS	LYS	L	L	1 - 296	2 - 297
43	22	22	LYS	LYS	LYS	LYS	C	C	3 - 296	4 - 297
44	22	22	LYS	LYS	LYS	LYS	D	D	3 - 296	4 - 297
45	23	23	THR	THR	PHE	PHE	C	C	4 - 295	5 - 296
46	23	23	THR	THR	PHE	PHE	E	E	4 - 295	5 - 296
47	24	24	MET	MET	LYS	LYS	C	C	1 - 296	2 - 297
48	24	24	MET	MET	LYS	LYS	F	F	1 - 296	2 - 297
49	25	25	MET	MET	LYS	LYS	C	C	1 - 296	2 - 297
50	25	25	MET	MET	LYS	LYS	G	G	1 - 296	2 - 297
51	26	26	MET	MET	LYS	LYS	C	C	1 - 296	2 - 297
52	26	26	MET	MET	LYS	LYS	H	H	1 - 296	2 - 297
53	27	27	MET	MET	LYS	LYS	C	C	1 - 296	2 - 297
54	27	27	MET	MET	LYS	LYS	I	I	1 - 296	2 - 297
55	28	28	THR	THR	PHE	PHE	C	C	4 - 295	5 - 296
56	28	28	THR	THR	PHE	PHE	J	J	4 - 295	5 - 296
57	29	29	THR	THR	PHE	PHE	C	C	4 - 295	5 - 296
58	29	29	THR	THR	PHE	PHE	K	K	4 - 295	5 - 296
59	30	30	MET	MET	LYS	LYS	C	C	1 - 296	2 - 297
60	30	30	MET	MET	LYS	LYS	L	L	1 - 296	2 - 297
61	31	31	THR	THR	LYS	LYS	D	D	4 - 296	5 - 297
62	31	31	THR	THR	LYS	LYS	E	E	4 - 296	5 - 297
63	32	32	LYS	LYS	LYS	LYS	D	D	3 - 296	4 - 297
64	32	32	LYS	LYS	LYS	LYS	F	F	3 - 296	4 - 297
65	33	33	LYS	LYS	GLU	GLU	D	D	3 - 297	4 - 298
66	33	33	LYS	LYS	GLU	GLU	G	G	3 - 297	4 - 298
67	34	34	LYS	LYS	GLU	GLU	D	D	3 - 297	4 - 298
68	34	34	LYS	LYS	GLU	GLU	H	H	3 - 297	4 - 298
69	35	35	LYS	LYS	LYS	LYS	D	D	3 - 296	4 - 297
70	35	35	LYS	LYS	LYS	LYS	I	I	3 - 296	4 - 297
71	36	36	THR	THR	LYS	LYS	D	D	4 - 296	5 - 297
72	36	36	THR	THR	LYS	LYS	J	J	4 - 296	5 - 297
73	37	37	THR	THR	GLU	GLU	D	D	4 - 297	5 - 298
74	37	37	THR	THR	GLU	GLU	K	K	4 - 297	5 - 298
75	38	38	LYS	LYS	LYS	LYS	D	D	3 - 296	4 - 297
76	38	38	LYS	LYS	LYS	LYS	L	L	3 - 296	4 - 297
77	39	39	THR	THR	PHE	PHE	E	E	4 - 295	5 - 296
78	39	39	THR	THR	PHE	PHE	F	F	4 - 295	5 - 296
79	40	40	THR	THR	GLU	GLU	E	E	4 - 297	5 - 298
80	40	40	THR	THR	GLU	GLU	G	G	4 - 297	5 - 298
81	41	41	THR	THR	GLU	GLU	E	E	4 - 297	5 - 298
82	41	41	THR	THR	GLU	GLU	H	H	4 - 297	5 - 298
83	42	42	THR	THR	PHE	PHE	E	E	4 - 295	5 - 296
84	42	42	THR	THR	PHE	PHE	I	I	4 - 295	5 - 296
85	43	43	THR	THR	GLU	GLU	E	E	4 - 297	5 - 298
86	43	43	THR	THR	GLU	GLU	J	J	4 - 297	5 - 298
87	44	44	THR	THR	GLU	GLU	E	E	4 - 297	5 - 298
88	44	44	THR	THR	GLU	GLU	K	K	4 - 297	5 - 298
89	45	45	THR	THR	PHE	PHE	E	E	4 - 295	5 - 296
90	45	45	THR	THR	PHE	PHE	L	L	4 - 295	5 - 296
91	46	46	MET	MET	LYS	LYS	F	F	1 - 296	2 - 297
92	46	46	MET	MET	LYS	LYS	G	G	1 - 296	2 - 297
93	47	47	MET	MET	LYS	LYS	F	F	1 - 296	2 - 297
94	47	47	MET	MET	LYS	LYS	H	H	1 - 296	2 - 297
95	48	48	MET	MET	LYS	LYS	F	F	1 - 296	2 - 297
96	48	48	MET	MET	LYS	LYS	I	I	1 - 296	2 - 297
97	49	49	THR	THR	PHE	PHE	F	F	4 - 295	5 - 296
98	49	49	THR	THR	PHE	PHE	J	J	4 - 295	5 - 296
99	50	50	THR	THR	PHE	PHE	F	F	4 - 295	5 - 296
100	50	50	THR	THR	PHE	PHE	K	K	4 - 295	5 - 296
101	51	51	MET	MET	LYS	LYS	F	F	1 - 296	2 - 297
102	51	51	MET	MET	LYS	LYS	L	L	1 - 296	2 - 297
103	52	52	MET	MET	GLU	GLU	G	G	1 - 297	2 - 298
104	52	52	MET	MET	GLU	GLU	H	H	1 - 297	2 - 298
105	53	53	MET	MET	LYS	LYS	G	G	1 - 296	2 - 297
106	53	53	MET	MET	LYS	LYS	I	I	1 - 296	2 - 297
107	54	54	THR	THR	GLU	GLU	G	G	4 - 297	5 - 298
108	54	54	THR	THR	GLU	GLU	J	J	4 - 297	5 - 298
109	55	55	THR	THR	GLU	GLU	G	G	4 - 297	5 - 298
110	55	55	THR	THR	GLU	GLU	K	K	4 - 297	5 - 298
111	56	56	MET	MET	LYS	LYS	G	G	1 - 296	2 - 297
112	56	56	MET	MET	LYS	LYS	L	L	1 - 296	2 - 297
113	57	57	MET	MET	LYS	LYS	H	H	1 - 296	2 - 297
114	57	57	MET	MET	LYS	LYS	I	I	1 - 296	2 - 297
115	58	58	THR	THR	GLU	GLU	H	H	4 - 297	5 - 298
116	58	58	THR	THR	GLU	GLU	J	J	4 - 297	5 - 298
117	59	59	THR	THR	GLU	GLU	H	H	4 - 297	5 - 298
118	59	59	THR	THR	GLU	GLU	K	K	4 - 297	5 - 298
119	60	60	MET	MET	LYS	LYS	H	H	1 - 296	2 - 297
120	60	60	MET	MET	LYS	LYS	L	L	1 - 296	2 - 297
121	61	61	THR	THR	PHE	PHE	I	I	4 - 295	5 - 296
122	61	61	THR	THR	PHE	PHE	J	J	4 - 295	5 - 296
123	62	62	THR	THR	PHE	PHE	I	I	4 - 295	5 - 296
124	62	62	THR	THR	PHE	PHE	K	K	4 - 295	5 - 296
125	63	63	MET	MET	LYS	LYS	I	I	1 - 296	2 - 297
126	63	63	MET	MET	LYS	LYS	L	L	1 - 296	2 - 297
127	64	64	THR	THR	GLU	GLU	J	J	4 - 297	5 - 298
128	64	64	THR	THR	GLU	GLU	K	K	4 - 297	5 - 298
129	65	65	THR	THR	PHE	PHE	J	J	4 - 295	5 - 296
130	65	65	THR	THR	PHE	PHE	L	L	4 - 295	5 - 296
131	66	66	THR	THR	PHE	PHE	K	K	4 - 295	5 - 296
132	66	66	THR	THR	PHE	PHE	L	L	4 - 295	5 - 296

NCS ensembles :

ID	Details (eV)
1	Local NCS retraints between domains: 1 2
2	Local NCS retraints between domains: 3 4
3	Local NCS retraints between domains: 5 6
4	Local NCS retraints between domains: 7 8
5	Local NCS retraints between domains: 9 10
6	Local NCS retraints between domains: 11 12
7	Local NCS retraints between domains: 13 14
8	Local NCS retraints between domains: 15 16
9	Local NCS retraints between domains: 17 18
10	Local NCS retraints between domains: 19 20
11	Local NCS retraints between domains: 21 22
12	Local NCS retraints between domains: 23 24
13	Local NCS retraints between domains: 25 26
14	Local NCS retraints between domains: 27 28
15	Local NCS retraints between domains: 29 30
16	Local NCS retraints between domains: 31 32
17	Local NCS retraints between domains: 33 34
18	Local NCS retraints between domains: 35 36
19	Local NCS retraints between domains: 37 38
20	Local NCS retraints between domains: 39 40
21	Local NCS retraints between domains: 41 42
22	Local NCS retraints between domains: 43 44
23	Local NCS retraints between domains: 45 46
24	Local NCS retraints between domains: 47 48
25	Local NCS retraints between domains: 49 50
26	Local NCS retraints between domains: 51 52
27	Local NCS retraints between domains: 53 54
28	Local NCS retraints between domains: 55 56
29	Local NCS retraints between domains: 57 58
30	Local NCS retraints between domains: 59 60
31	Local NCS retraints between domains: 61 62
32	Local NCS retraints between domains: 63 64
33	Local NCS retraints between domains: 65 66
34	Local NCS retraints between domains: 67 68
35	Local NCS retraints between domains: 69 70
36	Local NCS retraints between domains: 71 72
37	Local NCS retraints between domains: 73 74
38	Local NCS retraints between domains: 75 76
39	Local NCS retraints between domains: 77 78
40	Local NCS retraints between domains: 79 80
41	Local NCS retraints between domains: 81 82
42	Local NCS retraints between domains: 83 84
43	Local NCS retraints between domains: 85 86
44	Local NCS retraints between domains: 87 88
45	Local NCS retraints between domains: 89 90
46	Local NCS retraints between domains: 91 92
47	Local NCS retraints between domains: 93 94
48	Local NCS retraints between domains: 95 96
49	Local NCS retraints between domains: 97 98
50	Local NCS retraints between domains: 99 100
51	Local NCS retraints between domains: 101 102
52	Local NCS retraints between domains: 103 104
53	Local NCS retraints between domains: 105 106
54	Local NCS retraints between domains: 107 108
55	Local NCS retraints between domains: 109 110
56	Local NCS retraints between domains: 111 112
57	Local NCS retraints between domains: 113 114
58	Local NCS retraints between domains: 115 116
59	Local NCS retraints between domains: 117 118
60	Local NCS retraints between domains: 119 120
61	Local NCS retraints between domains: 121 122
62	Local NCS retraints between domains: 123 124
63	Local NCS retraints between domains: 125 126
64	Local NCS retraints between domains: 127 128
65	Local NCS retraints between domains: 129 130
66	Local NCS retraints between domains: 131 132

Components

#1: Protein

A B C D E F G H I J K L
Geranylgeranyl pyrophosphate synthase / GGPP synthase / GGPPSase / (2E / 6E)-farnesyl diphosphate synthase / Dimethylallyltranstransferase / Farnesyl diphosphate synthase / Farnesyltranstransferase / Geranylgeranyl diphosphate synthase / Geranyltranstransferase

Details:

Mass: 34972.883 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GGPS1 / Production host: Escherichia coli (E. coli)
References: UniProt: O95749, Transferases; Transferring alkyl or aryl groups, other than methyl groups, dimethylallyltranstransferase, geranylgeranyl diphosphate synthase, (2E,6E)-farnesyl diphosphate synthase

#2: Chemical

A-401 B-401 C-401 D-401 E-401 F-401 G-401 H-401 I-401 J-401 K-401 L-401
ChemComp-A1C1E / {[(2-{3-[(3-fluoro-4-methoxyphenyl)carbamoyl]phenyl}thieno[2,3-d]pyrimidin-4-yl)amino]methylene}bis(phosphonic acid)

Details:

Mass: 568.408 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C₂₁H₁₉FN₄O₈P₂S / Feature type: SUBJECT OF INVESTIGATION

#3: Chemical

A-402 A-403 A-404 B-402 B-403 B-404 C-402 C-403 C-404 D-402 D-403 D-404 E-402 E-403 E-404 F-402 F-403 F-404 G-402 G-403 ...
ChemComp-MG / MAGNESIUM ION

Details:

Mass: 24.305 Da / Num. of mol.: 36 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION

#4: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 91 / Source method: isolated from a natural source / Formula: H₂O

• Has ligand of interest: Y
• Has protein modification: N

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 2.48 ų/Da / Density % sol: 50.42 %
• Crystal grow: Temperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 8 ; Details: 100 mM Tris-HCl pH 8.0, 42% 2-Methyl-2,4-pentanediol

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: SSRL / Beamline: BL12-1 / Wavelength: 0.97946 Å
• Detector: Type: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Mar 24, 2024 / Details: Microfocus
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.97946 Å / Relative weight: 1
• Reflection: Resolution: 2.64→106.03 Å / Num. obs: 54508 / % possible obs: 45.6 % / Redundancy: 6.9 % / B_iso Wilson estimate: 32.88 Ų / CC_1/2: 0.996 / R_merge(I) obs: 0.167 / R_pim(I) all: 0.067 / R_rim(I) all: 0.18 / Net I/σ(I): 4.3
• Reflection shell: Resolution: 2.64→3.26 Å / Redundancy: 6.5 % / R_merge(I) obs: 0.483 / Mean I/σ(I) obs: 1.6 / Num. unique obs: 5073 / CC_1/2: 0.809 / R_pim(I) all: 0.202 / R_rim(I) all: 0.524 / % possible all: 9.1

Processing

Software

Name	Version	Classification
REFMAC	5.8.0430 (refmacat 0.4.105)	refinement
DIALS		data reduction
STARANISO		data scaling
PHASER		phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.641→106.027 Å / Cor.coef. F_o:F_c: 0.909 / Cor.coef. F_o:F_c free: 0.865 / SU B: 41.568 / SU ML: 0.402 / Cross valid method: FREE R-VALUE / ESU R Free: 0.647
Details: Hydrogens have been used if present in the input file

	Rfactor	Num. reflection	% reflection
Rfree	0.2473	2757	5.058 %
Rwork	0.2088	51748	-
all	0.211	-	-
obs	-	54505	45.448 %

• Solvent computation: Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT

Displacement parameters

B_iso mean: 54.025 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	0.601 Å2	-0 Å2	1.08 Å2
2-	-	-2.576 Å2	-0 Å2
3-	-	-	1.54 Å2

Refinement step

Cycle: LAST / Resolution: 2.641→106.027 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	28451	0	480	91	29022

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.008	0.012	29654
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.016	28108
X-RAY DIFFRACTION	r_angle_refined_deg	1.61	1.868	40014
X-RAY DIFFRACTION	r_angle_other_deg	0.522	1.778	64779
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.503	5	3455
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	10.791	5	144
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.702	10	5363
X-RAY DIFFRACTION	r_dihedral_angle_6_deg	14.108	10	1418
X-RAY DIFFRACTION	r_chiral_restr	0.067	0.2	4364
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	33899
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	6733
X-RAY DIFFRACTION	r_nbd_refined	0.243	0.2	7454
X-RAY DIFFRACTION	r_symmetry_nbd_other	0.189	0.2	25651
X-RAY DIFFRACTION	r_nbtor_refined	0.197	0.2	14773
X-RAY DIFFRACTION	r_symmetry_nbtor_other	0.077	0.2	16392
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.22	0.2	455
X-RAY DIFFRACTION	r_symmetry_xyhbond_nbd_other	0.152	0.2	8
X-RAY DIFFRACTION	r_metal_ion_refined	0.119	0.2	4
X-RAY DIFFRACTION	r_symmetry_nbd_refined	0.386	0.2	32
X-RAY DIFFRACTION	r_nbd_other	0.274	0.2	53
X-RAY DIFFRACTION	r_mcbond_it	1.614	1.886	13883
X-RAY DIFFRACTION	r_mcbond_other	1.614	1.886	13883
X-RAY DIFFRACTION	r_mcangle_it	2.794	3.374	17317
X-RAY DIFFRACTION	r_mcangle_other	2.794	3.374	17318
X-RAY DIFFRACTION	r_scbond_it	1.946	2.099	15771
X-RAY DIFFRACTION	r_scbond_other	1.946	2.099	15771
X-RAY DIFFRACTION	r_scangle_it	3.346	3.764	22697
X-RAY DIFFRACTION	r_scangle_other	3.346	3.764	22698
X-RAY DIFFRACTION	r_lrange_it	5.525	18.266	34805
X-RAY DIFFRACTION	r_lrange_other	5.525	18.266	34802
X-RAY DIFFRACTION	r_ncsr_local_group_1	0.065	0.05	10258
X-RAY DIFFRACTION	r_ncsr_local_group_2	0.068	0.05	9949
X-RAY DIFFRACTION	r_ncsr_local_group_3	0.058	0.05	10057
X-RAY DIFFRACTION	r_ncsr_local_group_4	0.056	0.05	10044
X-RAY DIFFRACTION	r_ncsr_local_group_5	0.062	0.05	10031
X-RAY DIFFRACTION	r_ncsr_local_group_6	0.057	0.05	10401
X-RAY DIFFRACTION	r_ncsr_local_group_7	0.065	0.05	10344
X-RAY DIFFRACTION	r_ncsr_local_group_8	0.053	0.05	10026
X-RAY DIFFRACTION	r_ncsr_local_group_9	0.056	0.05	10014
X-RAY DIFFRACTION	r_ncsr_local_group_10	0.054	0.05	10014
X-RAY DIFFRACTION	r_ncsr_local_group_11	0.082	0.05	9725
X-RAY DIFFRACTION	r_ncsr_local_group_12	0.077	0.05	9934
X-RAY DIFFRACTION	r_ncsr_local_group_13	0.062	0.05	10088
X-RAY DIFFRACTION	r_ncsr_local_group_14	0.061	0.05	10058
X-RAY DIFFRACTION	r_ncsr_local_group_15	0.066	0.05	10006
X-RAY DIFFRACTION	r_ncsr_local_group_16	0.062	0.05	10259
X-RAY DIFFRACTION	r_ncsr_local_group_17	0.062	0.05	10286
X-RAY DIFFRACTION	r_ncsr_local_group_18	0.066	0.05	9998
X-RAY DIFFRACTION	r_ncsr_local_group_19	0.064	0.05	10036
X-RAY DIFFRACTION	r_ncsr_local_group_20	0.057	0.05	10030
X-RAY DIFFRACTION	r_ncsr_local_group_21	0.09	0.05	9712
X-RAY DIFFRACTION	r_ncsr_local_group_22	0.073	0.05	9867
X-RAY DIFFRACTION	r_ncsr_local_group_23	0.073	0.05	9801
X-RAY DIFFRACTION	r_ncsr_local_group_24	0.074	0.05	9966
X-RAY DIFFRACTION	r_ncsr_local_group_25	0.068	0.05	9937
X-RAY DIFFRACTION	r_ncsr_local_group_26	0.071	0.05	9947
X-RAY DIFFRACTION	r_ncsr_local_group_27	0.068	0.05	10005
X-RAY DIFFRACTION	r_ncsr_local_group_28	0.072	0.05	9775
X-RAY DIFFRACTION	r_ncsr_local_group_29	0.07	0.05	9770
X-RAY DIFFRACTION	r_ncsr_local_group_30	0.091	0.05	9716
X-RAY DIFFRACTION	r_ncsr_local_group_31	0.054	0.05	10124
X-RAY DIFFRACTION	r_ncsr_local_group_32	0.059	0.05	9956
X-RAY DIFFRACTION	r_ncsr_local_group_33	0.061	0.05	10051
X-RAY DIFFRACTION	r_ncsr_local_group_34	0.057	0.05	10070
X-RAY DIFFRACTION	r_ncsr_local_group_35	0.058	0.05	9956
X-RAY DIFFRACTION	r_ncsr_local_group_36	0.046	0.05	10155
X-RAY DIFFRACTION	r_ncsr_local_group_37	0.049	0.05	10097
X-RAY DIFFRACTION	r_ncsr_local_group_38	0.085	0.05	9653
X-RAY DIFFRACTION	r_ncsr_local_group_39	0.057	0.05	9879
X-RAY DIFFRACTION	r_ncsr_local_group_40	0.057	0.05	10022
X-RAY DIFFRACTION	r_ncsr_local_group_41	0.057	0.05	10059
X-RAY DIFFRACTION	r_ncsr_local_group_42	0.059	0.05	9879
X-RAY DIFFRACTION	r_ncsr_local_group_43	0.059	0.05	10113
X-RAY DIFFRACTION	r_ncsr_local_group_44	0.045	0.05	10134
X-RAY DIFFRACTION	r_ncsr_local_group_45	0.084	0.05	9575
X-RAY DIFFRACTION	r_ncsr_local_group_46	0.059	0.05	10016
X-RAY DIFFRACTION	r_ncsr_local_group_47	0.061	0.05	10006
X-RAY DIFFRACTION	r_ncsr_local_group_48	0.054	0.05	10073
X-RAY DIFFRACTION	r_ncsr_local_group_49	0.06	0.05	9866
X-RAY DIFFRACTION	r_ncsr_local_group_50	0.051	0.05	9862
X-RAY DIFFRACTION	r_ncsr_local_group_51	0.075	0.05	9819
X-RAY DIFFRACTION	r_ncsr_local_group_52	0.059	0.05	10364
X-RAY DIFFRACTION	r_ncsr_local_group_53	0.055	0.05	10002
X-RAY DIFFRACTION	r_ncsr_local_group_54	0.058	0.05	10006
X-RAY DIFFRACTION	r_ncsr_local_group_55	0.051	0.05	10015
X-RAY DIFFRACTION	r_ncsr_local_group_56	0.082	0.05	9748
X-RAY DIFFRACTION	r_ncsr_local_group_57	0.056	0.05	9999
X-RAY DIFFRACTION	r_ncsr_local_group_58	0.055	0.05	10020
X-RAY DIFFRACTION	r_ncsr_local_group_59	0.05	0.05	10022
X-RAY DIFFRACTION	r_ncsr_local_group_60	0.085	0.05	9717
X-RAY DIFFRACTION	r_ncsr_local_group_61	0.055	0.05	9870
X-RAY DIFFRACTION	r_ncsr_local_group_62	0.057	0.05	9865
X-RAY DIFFRACTION	r_ncsr_local_group_63	0.083	0.05	9757
X-RAY DIFFRACTION	r_ncsr_local_group_64	0.052	0.05	10104
X-RAY DIFFRACTION	r_ncsr_local_group_65	0.084	0.05	9566
X-RAY DIFFRACTION	r_ncsr_local_group_66	0.082	0.05	9568

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Refine-ID	Type	Rms dev position (Å)	Weight position
1	1	A	X-RAY DIFFRACTION	Local ncs	0.06489	0.0501
1	2	B	X-RAY DIFFRACTION	Local ncs	0.06489	0.0501
2	3	A	X-RAY DIFFRACTION	Local ncs	0.06795	0.0501
2	4	C	X-RAY DIFFRACTION	Local ncs	0.06795	0.0501
3	5	A	X-RAY DIFFRACTION	Local ncs	0.05791	0.0501
3	6	D	X-RAY DIFFRACTION	Local ncs	0.05791	0.0501
4	7	A	X-RAY DIFFRACTION	Local ncs	0.05635	0.0501
4	8	E	X-RAY DIFFRACTION	Local ncs	0.05635	0.0501
5	9	A	X-RAY DIFFRACTION	Local ncs	0.06206	0.0501
5	10	F	X-RAY DIFFRACTION	Local ncs	0.06206	0.0501
6	11	A	X-RAY DIFFRACTION	Local ncs	0.05665	0.0501
6	12	G	X-RAY DIFFRACTION	Local ncs	0.05665	0.0501
7	13	A	X-RAY DIFFRACTION	Local ncs	0.06512	0.0501
7	14	H	X-RAY DIFFRACTION	Local ncs	0.06512	0.0501
8	15	A	X-RAY DIFFRACTION	Local ncs	0.05329	0.0501
8	16	I	X-RAY DIFFRACTION	Local ncs	0.05329	0.0501
9	17	A	X-RAY DIFFRACTION	Local ncs	0.05592	0.0501
9	18	J	X-RAY DIFFRACTION	Local ncs	0.05592	0.0501
10	19	A	X-RAY DIFFRACTION	Local ncs	0.05402	0.0501
10	20	K	X-RAY DIFFRACTION	Local ncs	0.05402	0.0501
11	21	A	X-RAY DIFFRACTION	Local ncs	0.0824	0.05009
11	22	L	X-RAY DIFFRACTION	Local ncs	0.0824	0.05009
12	23	B	X-RAY DIFFRACTION	Local ncs	0.07705	0.05009
12	24	C	X-RAY DIFFRACTION	Local ncs	0.07705	0.05009
13	25	B	X-RAY DIFFRACTION	Local ncs	0.06244	0.0501
13	26	D	X-RAY DIFFRACTION	Local ncs	0.06244	0.0501
14	27	B	X-RAY DIFFRACTION	Local ncs	0.06055	0.0501
14	28	E	X-RAY DIFFRACTION	Local ncs	0.06055	0.0501
15	29	B	X-RAY DIFFRACTION	Local ncs	0.06604	0.0501
15	30	F	X-RAY DIFFRACTION	Local ncs	0.06604	0.0501
16	31	B	X-RAY DIFFRACTION	Local ncs	0.062	0.0501
16	32	G	X-RAY DIFFRACTION	Local ncs	0.062	0.0501
17	33	B	X-RAY DIFFRACTION	Local ncs	0.06234	0.0501
17	34	H	X-RAY DIFFRACTION	Local ncs	0.06234	0.0501
18	35	B	X-RAY DIFFRACTION	Local ncs	0.06561	0.0501
18	36	I	X-RAY DIFFRACTION	Local ncs	0.06561	0.0501
19	37	B	X-RAY DIFFRACTION	Local ncs	0.06413	0.0501
19	38	J	X-RAY DIFFRACTION	Local ncs	0.06413	0.0501
20	39	B	X-RAY DIFFRACTION	Local ncs	0.05744	0.0501
20	40	K	X-RAY DIFFRACTION	Local ncs	0.05744	0.0501
21	41	B	X-RAY DIFFRACTION	Local ncs	0.0895	0.05009
21	42	L	X-RAY DIFFRACTION	Local ncs	0.0895	0.05009
22	43	C	X-RAY DIFFRACTION	Local ncs	0.07258	0.0501
22	44	D	X-RAY DIFFRACTION	Local ncs	0.07258	0.0501
23	45	C	X-RAY DIFFRACTION	Local ncs	0.07344	0.05009
23	46	E	X-RAY DIFFRACTION	Local ncs	0.07344	0.05009
24	47	C	X-RAY DIFFRACTION	Local ncs	0.07357	0.0501
24	48	F	X-RAY DIFFRACTION	Local ncs	0.07357	0.0501
25	49	C	X-RAY DIFFRACTION	Local ncs	0.06795	0.0501
25	50	G	X-RAY DIFFRACTION	Local ncs	0.06795	0.0501
26	51	C	X-RAY DIFFRACTION	Local ncs	0.07105	0.05009
26	52	H	X-RAY DIFFRACTION	Local ncs	0.07105	0.05009
27	53	C	X-RAY DIFFRACTION	Local ncs	0.06847	0.0501
27	54	I	X-RAY DIFFRACTION	Local ncs	0.06847	0.0501
28	55	C	X-RAY DIFFRACTION	Local ncs	0.07165	0.0501
28	56	J	X-RAY DIFFRACTION	Local ncs	0.07165	0.0501
29	57	C	X-RAY DIFFRACTION	Local ncs	0.06993	0.0501
29	58	K	X-RAY DIFFRACTION	Local ncs	0.06993	0.0501
30	59	C	X-RAY DIFFRACTION	Local ncs	0.09136	0.05009
30	60	L	X-RAY DIFFRACTION	Local ncs	0.09136	0.05009
31	61	D	X-RAY DIFFRACTION	Local ncs	0.05388	0.0501
31	62	E	X-RAY DIFFRACTION	Local ncs	0.05388	0.0501
32	63	D	X-RAY DIFFRACTION	Local ncs	0.05876	0.0501
32	64	F	X-RAY DIFFRACTION	Local ncs	0.05876	0.0501
33	65	D	X-RAY DIFFRACTION	Local ncs	0.06096	0.0501
33	66	G	X-RAY DIFFRACTION	Local ncs	0.06096	0.0501
34	67	D	X-RAY DIFFRACTION	Local ncs	0.05696	0.0501
34	68	H	X-RAY DIFFRACTION	Local ncs	0.05696	0.0501
35	69	D	X-RAY DIFFRACTION	Local ncs	0.05835	0.0501
35	70	I	X-RAY DIFFRACTION	Local ncs	0.05835	0.0501
36	71	D	X-RAY DIFFRACTION	Local ncs	0.0462	0.0501
36	72	J	X-RAY DIFFRACTION	Local ncs	0.0462	0.0501
37	73	D	X-RAY DIFFRACTION	Local ncs	0.04857	0.0501
37	74	K	X-RAY DIFFRACTION	Local ncs	0.04857	0.0501
38	75	D	X-RAY DIFFRACTION	Local ncs	0.08547	0.05009
38	76	L	X-RAY DIFFRACTION	Local ncs	0.08547	0.05009
39	77	E	X-RAY DIFFRACTION	Local ncs	0.0573	0.0501
39	78	F	X-RAY DIFFRACTION	Local ncs	0.0573	0.0501
40	79	E	X-RAY DIFFRACTION	Local ncs	0.05736	0.0501
40	80	G	X-RAY DIFFRACTION	Local ncs	0.05736	0.0501
41	81	E	X-RAY DIFFRACTION	Local ncs	0.0573	0.0501
41	82	H	X-RAY DIFFRACTION	Local ncs	0.0573	0.0501
42	83	E	X-RAY DIFFRACTION	Local ncs	0.05933	0.0501
42	84	I	X-RAY DIFFRACTION	Local ncs	0.05933	0.0501
43	85	E	X-RAY DIFFRACTION	Local ncs	0.05938	0.0501
43	86	J	X-RAY DIFFRACTION	Local ncs	0.05938	0.0501
44	87	E	X-RAY DIFFRACTION	Local ncs	0.04526	0.0501
44	88	K	X-RAY DIFFRACTION	Local ncs	0.04526	0.0501
45	89	E	X-RAY DIFFRACTION	Local ncs	0.0845	0.05009
45	90	L	X-RAY DIFFRACTION	Local ncs	0.0845	0.05009
46	91	F	X-RAY DIFFRACTION	Local ncs	0.0588	0.0501
46	92	G	X-RAY DIFFRACTION	Local ncs	0.0588	0.0501
47	93	F	X-RAY DIFFRACTION	Local ncs	0.06066	0.0501
47	94	H	X-RAY DIFFRACTION	Local ncs	0.06066	0.0501
48	95	F	X-RAY DIFFRACTION	Local ncs	0.05383	0.0501
48	96	I	X-RAY DIFFRACTION	Local ncs	0.05383	0.0501
49	97	F	X-RAY DIFFRACTION	Local ncs	0.06027	0.0501
49	98	J	X-RAY DIFFRACTION	Local ncs	0.06027	0.0501
50	99	F	X-RAY DIFFRACTION	Local ncs	0.05129	0.0501
50	100	K	X-RAY DIFFRACTION	Local ncs	0.05129	0.0501
51	101	F	X-RAY DIFFRACTION	Local ncs	0.07457	0.05009
51	102	L	X-RAY DIFFRACTION	Local ncs	0.07457	0.05009
52	103	G	X-RAY DIFFRACTION	Local ncs	0.05929	0.0501
52	104	H	X-RAY DIFFRACTION	Local ncs	0.05929	0.0501
53	105	G	X-RAY DIFFRACTION	Local ncs	0.05526	0.0501
53	106	I	X-RAY DIFFRACTION	Local ncs	0.05526	0.0501
54	107	G	X-RAY DIFFRACTION	Local ncs	0.05799	0.0501
54	108	J	X-RAY DIFFRACTION	Local ncs	0.05799	0.0501
55	109	G	X-RAY DIFFRACTION	Local ncs	0.05059	0.0501
55	110	K	X-RAY DIFFRACTION	Local ncs	0.05059	0.0501
56	111	G	X-RAY DIFFRACTION	Local ncs	0.08224	0.05009
56	112	L	X-RAY DIFFRACTION	Local ncs	0.08224	0.05009
57	113	H	X-RAY DIFFRACTION	Local ncs	0.05615	0.0501
57	114	I	X-RAY DIFFRACTION	Local ncs	0.05615	0.0501
58	115	H	X-RAY DIFFRACTION	Local ncs	0.05455	0.0501
58	116	J	X-RAY DIFFRACTION	Local ncs	0.05455	0.0501
59	117	H	X-RAY DIFFRACTION	Local ncs	0.05012	0.0501
59	118	K	X-RAY DIFFRACTION	Local ncs	0.05012	0.0501
60	119	H	X-RAY DIFFRACTION	Local ncs	0.08539	0.05009
60	120	L	X-RAY DIFFRACTION	Local ncs	0.08539	0.05009
61	121	I	X-RAY DIFFRACTION	Local ncs	0.05524	0.0501
61	122	J	X-RAY DIFFRACTION	Local ncs	0.05524	0.0501
62	123	I	X-RAY DIFFRACTION	Local ncs	0.05699	0.0501
62	124	K	X-RAY DIFFRACTION	Local ncs	0.05699	0.0501
63	125	I	X-RAY DIFFRACTION	Local ncs	0.08292	0.05009
63	126	L	X-RAY DIFFRACTION	Local ncs	0.08292	0.05009
64	127	J	X-RAY DIFFRACTION	Local ncs	0.05181	0.0501
64	128	K	X-RAY DIFFRACTION	Local ncs	0.05181	0.0501
65	129	J	X-RAY DIFFRACTION	Local ncs	0.08394	0.05009
65	130	L	X-RAY DIFFRACTION	Local ncs	0.08394	0.05009
66	131	K	X-RAY DIFFRACTION	Local ncs	0.08248	0.05009
66	132	L	X-RAY DIFFRACTION	Local ncs	0.08248	0.05009

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)	Rfactor Rfree	Num. reflection Rfree	Rfactor Rwork	Num. reflection Rwork	Rfactor all	Num. reflection all	Fsc work	% reflection obs (%)	WRfactor Rwork	Fsc free
2.641-2.71		0	0.374	21	0.374	8831	0.901	0.2378	0.364
2.71-2.784	0.224	12	0.328	82	0.316	8556	0.944	1.0986	0.339	0.957
2.784-2.865	0.323	14	0.312	250	0.312	8378	0.938	3.1511	0.318	0.941
2.865-2.953	0.219	30	0.305	517	0.3	8094	0.938	6.7581	0.3	0.97
2.953-3.05	0.269	50	0.281	838	0.281	7928	0.95	11.2008	0.273	0.954
3.05-3.157	0.371	62	0.286	1328	0.29	7613	0.947	18.2582	0.28	0.895
3.157-3.276	0.332	112	0.276	2015	0.279	7354	0.951	28.923	0.266	0.932
3.276-3.409	0.288	140	0.254	2687	0.255	7104	0.96	39.7945	0.238	0.95
3.409-3.561	0.272	199	0.241	3154	0.243	6766	0.962	49.5566	0.228	0.947
3.561-3.734	0.231	200	0.221	3833	0.222	6538	0.969	61.6855	0.206	0.965
3.734-3.936	0.26	250	0.221	4269	0.223	6173	0.967	73.2059	0.202	0.939
3.936-4.175	0.217	229	0.203	4639	0.204	5872	0.973	82.9019	0.185	0.969
4.175-4.462	0.207	245	0.188	4831	0.189	5548	0.976	91.4924	0.17	0.972
4.462-4.819	0.216	212	0.168	4748	0.17	5104	0.981	97.1787	0.153	0.97
4.819-5.278	0.251	239	0.186	4487	0.189	4763	0.978	99.2232	0.17	0.961
5.278-5.899	0.254	246	0.227	3970	0.229	4262	0.97	98.9207	0.213	0.96
5.899-6.808	0.262	183	0.233	3504	0.235	3820	0.968	96.5183	0.222	0.962
6.808-8.33	0.238	149	0.198	2854	0.2	3231	0.977	92.9434	0.2	0.97
8.33-11.744	0.215	106	0.16	2388	0.162	2513	0.984	99.2439	0.169	0.97
11.744-106.027	0.357	79	0.297	1333	0.3	1438	0.932	98.1919	0.54	0.899

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	1.797	-0.7225	0.4375	1.1102	0.6386	2.2686	-0.0239	0.395	0.1069	-0.1888	0.068	-0.327	0.1443	0.4233	-0.0441	0.1683	-0.0356	0.1103	0.3376	-0.0049	0.1481	-1.517	-50.952	-35.601
2	1.5199	-0.7432	0.4338	1.648	-0.395	1.9066	-0.0921	-0.0371	-0.1193	0.1805	0.105	0.3976	-0.0484	-0.5268	-0.0129	0.0458	0.0035	0.0712	0.3615	-0.0246	0.1348	-26.487	7.994	-23.574
3	1.976	0.4636	0.4473	1.2682	0.3142	2.8792	0.0141	0.0036	0.1924	0.2286	0.0061	0.4769	0.1267	-1.0357	-0.0202	0.1563	-0.1368	0.079	0.6714	0.0492	0.1873	-36.088	-46.879	-34.474
4	1.3079	0.7772	1.0462	1.7787	0.5092	2.5778	0.3388	-0.321	0.0845	0.679	-0.2693	0.2929	0.2416	-0.5449	-0.0695	0.4367	-0.079	0.0842	0.3029	0.0125	0.0681	-12.918	-29.104	8.349
5	0.893	0.0088	0.4632	2.1073	-1.0155	2.537	0.0303	0.2183	-0.0844	0.1666	-0.253	-0.6061	-0.0544	0.6814	0.2227	0.1213	-0.0391	-0.0858	0.3161	0.0408	0.1956	15.259	-13.676	-5.136
6	2.097	-0.2688	0.4141	1.6152	0.0529	2.7257	0.1468	0.9956	-0.079	-0.3575	-0.0236	-0.4297	-0.0456	0.5141	-0.1233	0.1059	0.0211	0.0777	0.7386	-0.0315	0.14	-3.709	4.262	-49.701
7	2.2006	0.0505	0.9797	1.3932	-0.406	3.2922	-0.2353	0.5419	0.5542	-0.0319	-0.1867	-0.6274	-0.214	0.9011	0.4219	0.0496	-0.1251	-0.056	0.4354	0.2496	0.4394	-35.523	19.876	-89.438
8	1.8827	-0.0069	0.7229	1.566	-0.891	2.8152	0.1976	-0.5211	0.0159	0.2125	0.0432	0.4421	0.0132	-0.1586	-0.2409	0.0654	-0.0711	0.0564	0.2801	-0.0001	0.1304	-56.946	-38.971	-71.806
9	3.2953	0.0365	1.5479	1.49	-0.1695	3.1835	-0.2369	-1.3016	0.1051	0.6466	-0.0409	0.2194	-0.347	-0.6135	0.2778	0.3772	0.0715	-0.0008	0.7133	-0.0577	0.142	-51.187	15.99	-58.655
10	1.2746	-0.6354	0.942	2.0058	0.3103	2.2593	0.1084	-0.3204	-0.2647	-0.0412	-0.2146	0.7368	0.039	-0.5184	0.1062	0.0197	-0.0534	-0.0328	0.262	-0.0245	0.2949	-80.263	-1.937	-97.437
11	1.6182	-0.9019	0.9514	2.1141	-0.8276	1.8978	0.515	0.606	-0.1496	-0.8413	-0.3987	0.013	0.1832	0.7255	-0.1162	0.433	0.153	-0.0405	0.4075	-0.0768	0.0344	-56.388	-17.38	-117.443
12	1.8304	0.8424	0.9515	3.3642	0.2878	4.6226	0.0546	0.2944	-0.1919	-0.3761	0.0192	-0.6905	-0.0081	2.0309	-0.0737	0.0565	-0.0032	0.0757	1.1848	-0.033	0.1439	-23.591	-35.456	-81.404

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	ALL	Ap	4 - 301
2	X-RAY DIFFRACTION	2	ALL	Bp	4 - 301
3	X-RAY DIFFRACTION	3	ALL	Cp	4 - 301
4	X-RAY DIFFRACTION	4	ALL	Dp	4 - 301
5	X-RAY DIFFRACTION	5	ALL	Ep	4 - 301
6	X-RAY DIFFRACTION	6	ALL	Fp	4 - 301
7	X-RAY DIFFRACTION	7	ALL	Gp	4 - 301
8	X-RAY DIFFRACTION	8	ALL	Hp	4 - 301
9	X-RAY DIFFRACTION	9	ALL	Ip	1 - 301
10	X-RAY DIFFRACTION	10	ALL	Jp	4 - 301
11	X-RAY DIFFRACTION	11	ALL	Kp	4 - 301
12	X-RAY DIFFRACTION	12	ALL	Lp	4 - 301