PDB-6s3y: CBDP35 SeMet structure

Basic information

• Entry: Database: PDB / ID: 6s3y
• Title: CBDP35 SeMet structure
• Components: PlyP35
• Keywords: HYDROLASE
• Function / homology: PSA endolysin, cell wall binding domain / PSA endolysin C-terminal cell wall binding domain / Peptidase M15C / D-alanyl-D-alanine carboxypeptidase / Hedgehog signalling/DD-peptidase zinc-binding domain superfamily / peptidase activity / PlyP35
• Biological species: Listeria phage P35 (virus)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.043 Å
• Authors: Hermoso, J.A. / Bartual, S.G.
• Citation: Journal: To Be Published; Title: CBDP35 SeMet structure; Authors: Hermoso, J.A. / Bartual, S.G.

History

Deposition	Jun 26, 2019	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jul 15, 2020	Provider: repository / Type: Initial release
Revision 1.1	Nov 13, 2024	Group: Data collection / Database references / Refinement description / Structure summary Category: chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_entry_details.has_protein_modification / _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: PlyP35

B: PlyP35

C: PlyP35

D: PlyP35

E: PlyP35

F: PlyP35

G: PlyP35

H: PlyP35

I: PlyP35

J: PlyP35

L: PlyP35

K: PlyP35

Summary:

• 197 kDa, 12 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	196,995	12
Polymers	196,995	12
Non-polymers	0	0
Water	27,239	1512

1

A: PlyP35

Summary:

• defined by author
• Evidence: gel filtration
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

2

B: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

3

C: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

4

D: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

5

E: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

6

F: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

7

G: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

8

H: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

9

I: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

10

J: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

11

L: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

12

K: PlyP35

Summary:

• defined by author
• 16.4 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	16,416	1
Polymers	16,416	1
Non-polymers	0	0
Water	18	1

Symmetry operations:

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

Unit cell

Length a, b, c (Å)	335.878, 95.565, 84.408
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	5
Space group name H-M	C121

Components on special symmetry positions

ID	Model	Components
1	1	A-437- HOH
2	1	B-406- 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	L
1	11	A
2	11	K
1	12	B
2	12	C
1	13	B
2	13	D
1	14	B
2	14	E
1	15	B
2	15	F
1	16	B
2	16	G
1	17	B
2	17	H
1	18	B
2	18	I
1	19	B
2	19	J
1	20	B
2	20	L
1	21	B
2	21	K
1	22	C
2	22	D
1	23	C
2	23	E
1	24	C
2	24	F
1	25	C
2	25	G
1	26	C
2	26	H
1	27	C
2	27	I
1	28	C
2	28	J
1	29	C
2	29	L
1	30	C
2	30	K
1	31	D
2	31	E
1	32	D
2	32	F
1	33	D
2	33	G
1	34	D
2	34	H
1	35	D
2	35	I
1	36	D
2	36	J
1	37	D
2	37	L
1	38	D
2	38	K
1	39	E
2	39	F
1	40	E
2	40	G
1	41	E
2	41	H
1	42	E
2	42	I
1	43	E
2	43	J
1	44	E
2	44	L
1	45	E
2	45	K
1	46	F
2	46	G
1	47	F
2	47	H
1	48	F
2	48	I
1	49	F
2	49	J
1	50	F
2	50	L
1	51	F
2	51	K
1	52	G
2	52	H
1	53	G
2	53	I
1	54	G
2	54	J
1	55	G
2	55	L
1	56	G
2	56	K
1	57	H
2	57	I
1	58	H
2	58	J
1	59	H
2	59	L
1	60	H
2	60	K
1	61	I
2	61	J
1	62	I
2	62	L
1	63	I
2	63	K
1	64	J
2	64	L
1	65	J
2	65	K
1	66	L
2	66	K

NCS domain segments:

Component-ID: _ / Refine code: _

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	MSE	MSE	LYS	LYS	A	A	153 - 290	2 - 139
2	1	MSE	MSE	LYS	LYS	B	B	153 - 290	2 - 139
1	2	MSE	MSE	ILE	ILE	A	A	153 - 289	2 - 138
2	2	MSE	MSE	ILE	ILE	C	C	153 - 289	2 - 138
1	3	MSE	MSE	LYS	LYS	A	A	153 - 291	2 - 140
2	3	MSE	MSE	LYS	LYS	D	D	153 - 291	2 - 140
1	4	MSE	MSE	LYS	LYS	A	A	154 - 290	3 - 139
2	4	MSE	MSE	LYS	LYS	E	E	154 - 290	3 - 139
1	5	MSE	MSE	LYS	LYS	A	A	153 - 291	2 - 140
2	5	MSE	MSE	LYS	LYS	F	F	153 - 291	2 - 140
1	6	MSE	MSE	LYS	LYS	A	A	153 - 291	2 - 140
2	6	MSE	MSE	LYS	LYS	G	G	153 - 291	2 - 140
1	7	MSE	MSE	LYS	LYS	A	A	153 - 291	2 - 140
2	7	MSE	MSE	LYS	LYS	H	H	153 - 291	2 - 140
1	8	MSE	MSE	LYS	LYS	A	A	154 - 290	3 - 139
2	8	MSE	MSE	LYS	LYS	I	I	154 - 290	3 - 139
1	9	MSE	MSE	ILE	ILE	A	A	154 - 289	3 - 138
2	9	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
1	10	MSE	MSE	LYS	LYS	A	A	153 - 291	2 - 140
2	10	MSE	MSE	LYS	LYS	L	K	153 - 291	2 - 140
1	11	MSE	MSE	LYS	LYS	A	A	153 - 291	2 - 140
2	11	MSE	MSE	LYS	LYS	K	L	153 - 291	2 - 140
1	12	HIS	HIS	ILE	ILE	B	B	152 - 289	1 - 138
2	12	HIS	HIS	ILE	ILE	C	C	152 - 289	1 - 138
1	13	MSE	MSE	LYS	LYS	B	B	153 - 290	2 - 139
2	13	MSE	MSE	LYS	LYS	D	D	153 - 290	2 - 139
1	14	MSE	MSE	LYS	LYS	B	B	154 - 290	3 - 139
2	14	MSE	MSE	LYS	LYS	E	E	154 - 290	3 - 139
1	15	MSE	MSE	LYS	LYS	B	B	153 - 290	2 - 139
2	15	MSE	MSE	LYS	LYS	F	F	153 - 290	2 - 139
1	16	MSE	MSE	LYS	LYS	B	B	153 - 290	2 - 139
2	16	MSE	MSE	LYS	LYS	G	G	153 - 290	2 - 139
1	17	MSE	MSE	LYS	LYS	B	B	153 - 290	2 - 139
2	17	MSE	MSE	LYS	LYS	H	H	153 - 290	2 - 139
1	18	MSE	MSE	LYS	LYS	B	B	154 - 290	3 - 139
2	18	MSE	MSE	LYS	LYS	I	I	154 - 290	3 - 139
1	19	MSE	MSE	ILE	ILE	B	B	154 - 289	3 - 138
2	19	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
1	20	MSE	MSE	LYS	LYS	B	B	153 - 290	2 - 139
2	20	MSE	MSE	LYS	LYS	L	K	153 - 290	2 - 139
1	21	MSE	MSE	LYS	LYS	B	B	153 - 290	2 - 139
2	21	MSE	MSE	LYS	LYS	K	L	153 - 290	2 - 139
1	22	MSE	MSE	ILE	ILE	C	C	153 - 289	2 - 138
2	22	MSE	MSE	ILE	ILE	D	D	153 - 289	2 - 138
1	23	MSE	MSE	ILE	ILE	C	C	154 - 289	3 - 138
2	23	MSE	MSE	ILE	ILE	E	E	154 - 289	3 - 138
1	24	MSE	MSE	ILE	ILE	C	C	153 - 289	2 - 138
2	24	MSE	MSE	ILE	ILE	F	F	153 - 289	2 - 138
1	25	MSE	MSE	ILE	ILE	C	C	153 - 289	2 - 138
2	25	MSE	MSE	ILE	ILE	G	G	153 - 289	2 - 138
1	26	MSE	MSE	ILE	ILE	C	C	153 - 289	2 - 138
2	26	MSE	MSE	ILE	ILE	H	H	153 - 289	2 - 138
1	27	MSE	MSE	ILE	ILE	C	C	154 - 289	3 - 138
2	27	MSE	MSE	ILE	ILE	I	I	154 - 289	3 - 138
1	28	MSE	MSE	ILE	ILE	C	C	154 - 289	3 - 138
2	28	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
1	29	MSE	MSE	ILE	ILE	C	C	153 - 289	2 - 138
2	29	MSE	MSE	ILE	ILE	L	K	153 - 289	2 - 138
1	30	MSE	MSE	ILE	ILE	C	C	153 - 289	2 - 138
2	30	MSE	MSE	ILE	ILE	K	L	153 - 289	2 - 138
1	31	MSE	MSE	LYS	LYS	D	D	154 - 290	3 - 139
2	31	MSE	MSE	LYS	LYS	E	E	154 - 290	3 - 139
1	32	MSE	MSE	LYS	LYS	D	D	153 - 291	2 - 140
2	32	MSE	MSE	LYS	LYS	F	F	153 - 291	2 - 140
1	33	MSE	MSE	LYS	LYS	D	D	153 - 291	2 - 140
2	33	MSE	MSE	LYS	LYS	G	G	153 - 291	2 - 140
1	34	MSE	MSE	LYS	LYS	D	D	153 - 291	2 - 140
2	34	MSE	MSE	LYS	LYS	H	H	153 - 291	2 - 140
1	35	MSE	MSE	LYS	LYS	D	D	154 - 290	3 - 139
2	35	MSE	MSE	LYS	LYS	I	I	154 - 290	3 - 139
1	36	MSE	MSE	ILE	ILE	D	D	154 - 289	3 - 138
2	36	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
1	37	MSE	MSE	LYS	LYS	D	D	153 - 291	2 - 140
2	37	MSE	MSE	LYS	LYS	L	K	153 - 291	2 - 140
1	38	MSE	MSE	LYS	LYS	D	D	153 - 291	2 - 140
2	38	MSE	MSE	LYS	LYS	K	L	153 - 291	2 - 140
1	39	MSE	MSE	LYS	LYS	E	E	154 - 290	3 - 139
2	39	MSE	MSE	LYS	LYS	F	F	154 - 290	3 - 139
1	40	MSE	MSE	LYS	LYS	E	E	154 - 290	3 - 139
2	40	MSE	MSE	LYS	LYS	G	G	154 - 290	3 - 139
1	41	MSE	MSE	LYS	LYS	E	E	154 - 290	3 - 139
2	41	MSE	MSE	LYS	LYS	H	H	154 - 290	3 - 139
1	42	MSE	MSE	LYS	LYS	E	E	154 - 291	3 - 140
2	42	MSE	MSE	LYS	LYS	I	I	154 - 291	3 - 140
1	43	MSE	MSE	ILE	ILE	E	E	154 - 289	3 - 138
2	43	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
1	44	MSE	MSE	LYS	LYS	E	E	154 - 290	3 - 139
2	44	MSE	MSE	LYS	LYS	L	K	154 - 290	3 - 139
1	45	MSE	MSE	LYS	LYS	E	E	154 - 290	3 - 139
2	45	MSE	MSE	LYS	LYS	K	L	154 - 290	3 - 139
1	46	MSE	MSE	LYS	LYS	F	F	153 - 291	2 - 140
2	46	MSE	MSE	LYS	LYS	G	G	153 - 291	2 - 140
1	47	MSE	MSE	LYS	LYS	F	F	153 - 291	2 - 140
2	47	MSE	MSE	LYS	LYS	H	H	153 - 291	2 - 140
1	48	MSE	MSE	LYS	LYS	F	F	154 - 290	3 - 139
2	48	MSE	MSE	LYS	LYS	I	I	154 - 290	3 - 139
1	49	MSE	MSE	ILE	ILE	F	F	154 - 289	3 - 138
2	49	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
1	50	MSE	MSE	LYS	LYS	F	F	153 - 291	2 - 140
2	50	MSE	MSE	LYS	LYS	L	K	153 - 291	2 - 140
1	51	MSE	MSE	LYS	LYS	F	F	153 - 291	2 - 140
2	51	MSE	MSE	LYS	LYS	K	L	153 - 291	2 - 140
1	52	MSE	MSE	LYS	LYS	G	G	153 - 291	2 - 140
2	52	MSE	MSE	LYS	LYS	H	H	153 - 291	2 - 140
1	53	MSE	MSE	LYS	LYS	G	G	154 - 290	3 - 139
2	53	MSE	MSE	LYS	LYS	I	I	154 - 290	3 - 139
1	54	MSE	MSE	ILE	ILE	G	G	154 - 289	3 - 138
2	54	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
1	55	MSE	MSE	LYS	LYS	G	G	153 - 291	2 - 140
2	55	MSE	MSE	LYS	LYS	L	K	153 - 291	2 - 140
1	56	MSE	MSE	LYS	LYS	G	G	153 - 291	2 - 140
2	56	MSE	MSE	LYS	LYS	K	L	153 - 291	2 - 140
1	57	MSE	MSE	LYS	LYS	H	H	154 - 290	3 - 139
2	57	MSE	MSE	LYS	LYS	I	I	154 - 290	3 - 139
1	58	MSE	MSE	ILE	ILE	H	H	154 - 289	3 - 138
2	58	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
1	59	MSE	MSE	LYS	LYS	H	H	153 - 291	2 - 140
2	59	MSE	MSE	LYS	LYS	L	K	153 - 291	2 - 140
1	60	MSE	MSE	LYS	LYS	H	H	153 - 291	2 - 140
2	60	MSE	MSE	LYS	LYS	K	L	153 - 291	2 - 140
1	61	MSE	MSE	ILE	ILE	I	I	154 - 289	3 - 138
2	61	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
1	62	MSE	MSE	LYS	LYS	I	I	154 - 290	3 - 139
2	62	MSE	MSE	LYS	LYS	L	K	154 - 290	3 - 139
1	63	MSE	MSE	LYS	LYS	I	I	154 - 290	3 - 139
2	63	MSE	MSE	LYS	LYS	K	L	154 - 290	3 - 139
1	64	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
2	64	MSE	MSE	ILE	ILE	L	K	154 - 289	3 - 138
1	65	MSE	MSE	ILE	ILE	J	J	154 - 289	3 - 138
2	65	MSE	MSE	ILE	ILE	K	L	154 - 289	3 - 138
1	66	MSE	MSE	LYS	LYS	L	K	153 - 291	2 - 140
2	66	MSE	MSE	LYS	LYS	K	L	153 - 291	2 - 140

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

Components

#1: Protein

A B C D E F G H I J L K
PlyP35

Details:

Mass: 16416.248 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Listeria phage P35 (virus) / Gene: ply
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: A8ATR6

#2: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 1512 / Source method: isolated from a natural source / Formula: H₂O

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

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 3.48 ų/Da / Density % sol: 64.64 %
• Crystal grow: Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: 4M Na Formate

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.8726 Å
• Detector: Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Sep 26, 2013
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.8726 Å / Relative weight: 1
• Reflection: Resolution: 2.043→19.84 Å / Num. obs: 168452 / % possible obs: 99.58 % / Redundancy: 7.5 % / R_merge(I) obs: 0.121 / Net I/σ(I): 13.01
• Reflection shell: Resolution: 2.043→2.116 Å / Redundancy: 7.5 % / R_merge(I) obs: 0.6468 / Mean I/σ(I) obs: 2.93 / Num. unique obs: 16483 / % possible all: 98.29

Processing

Software

Name	Version	Classification
REFMAC	5.8.0238	refinement
XDS		data reduction
Aimless		data scaling
PHENIX		phasing

Refinement

Method to determine structure: SAD / Resolution: 2.043→19.84 Å / Cor.coef. F_o:F_c: 0.946 / Cor.coef. F_o:F_c free: 0.933 / SU B: 4.252 / SU ML: 0.112 / Cross valid method: THROUGHOUT / ESU R: 0.165 / ESU R Free: 0.145 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.22591	8475	5 %	RANDOM
Rwork	0.20274	-	-	-
obs	0.20393	160162	99.76 %	-

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

Displacement parameters

B_iso mean: 28.62 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	-1.96 Å2	0 Å2	0.58 Å2
2-	-	0.17 Å2	0 Å2
3-	-	-	1.79 Å2

Refinement step

Cycle: LAST / Resolution: 2.043→19.84 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13598	0	0	1512	15110

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.01	0.013	14014
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.017	12853
X-RAY DIFFRACTION	r_angle_refined_deg	1.639	1.649	18827
X-RAY DIFFRACTION	r_angle_other_deg	1.284	1.594	29879
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	7.667	5	1659
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	30.426	22.23	713
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.916	15	2388
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	11.587	15	60
X-RAY DIFFRACTION	r_chiral_restr	0.077	0.2	1728
X-RAY DIFFRACTION	r_gen_planes_refined	0.008	0.02	15465
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	3199
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	2.771	2.802	6663
X-RAY DIFFRACTION	r_mcbond_other	2.771	2.801	6662
X-RAY DIFFRACTION	r_mcangle_it	4.089	4.182	8313
X-RAY DIFFRACTION	r_mcangle_other	4.089	4.182	8314
X-RAY DIFFRACTION	r_scbond_it	3.578	3.074	7351
X-RAY DIFFRACTION	r_scbond_other	3.577	3.074	7352
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	5.406	4.434	10515
X-RAY DIFFRACTION	r_long_range_B_refined	7.949	32.064	15820
X-RAY DIFFRACTION	r_long_range_B_other	7.857	31.689	15462
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 / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	A	4381	0.11
1	2	B	4381	0.11
2	1	A	4476	0.07
2	2	C	4476	0.07
3	1	A	4479	0.09
3	2	D	4479	0.09
4	1	A	4431	0.09
4	2	E	4431	0.09
5	1	A	4487	0.09
5	2	F	4487	0.09
6	1	A	4538	0.08
6	2	G	4538	0.08
7	1	A	4531	0.09
7	2	H	4531	0.09
8	1	A	4452	0.09
8	2	I	4452	0.09
9	1	A	4454	0.08
9	2	J	4454	0.08
10	1	A	4461	0.1
10	2	L	4461	0.1
11	1	A	4500	0.09
11	2	K	4500	0.09
12	1	B	4417	0.09
12	2	C	4417	0.09
13	1	B	4355	0.1
13	2	D	4355	0.1
14	1	B	4365	0.09
14	2	E	4365	0.09
15	1	B	4429	0.09
15	2	F	4429	0.09
16	1	B	4402	0.1
16	2	G	4402	0.1
17	1	B	4376	0.09
17	2	H	4376	0.09
18	1	B	4341	0.1
18	2	I	4341	0.1
19	1	B	4374	0.08
19	2	J	4374	0.08
20	1	B	4375	0.1
20	2	L	4375	0.1
21	1	B	4400	0.1
21	2	K	4400	0.1
22	1	C	4360	0.09
22	2	D	4360	0.09
23	1	C	4372	0.09
23	2	E	4372	0.09
24	1	C	4423	0.08
24	2	F	4423	0.08
25	1	C	4411	0.08
25	2	G	4411	0.08
26	1	C	4444	0.08
26	2	H	4444	0.08
27	1	C	4351	0.09
27	2	I	4351	0.09
28	1	C	4374	0.09
28	2	J	4374	0.09
29	1	C	4386	0.1
29	2	L	4386	0.1
30	1	C	4382	0.09
30	2	K	4382	0.09
31	1	D	4404	0.08
31	2	E	4404	0.08
32	1	D	4457	0.09
32	2	F	4457	0.09
33	1	D	4419	0.1
33	2	G	4419	0.1
34	1	D	4411	0.11
34	2	H	4411	0.11
35	1	D	4386	0.09
35	2	I	4386	0.09
36	1	D	4381	0.09
36	2	J	4381	0.09
37	1	D	4386	0.11
37	2	L	4386	0.11
38	1	D	4410	0.1
38	2	K	4410	0.1
39	1	E	4474	0.08
39	2	F	4474	0.08
40	1	E	4376	0.09
40	2	G	4376	0.09
41	1	E	4385	0.09
41	2	H	4385	0.09
42	1	E	4440	0.09
42	2	I	4440	0.09
43	1	E	4373	0.09
43	2	J	4373	0.09
44	1	E	4365	0.1
44	2	L	4365	0.1
45	1	E	4398	0.09
45	2	K	4398	0.09
46	1	F	4430	0.09
46	2	G	4430	0.09
47	1	F	4444	0.1
47	2	H	4444	0.1
48	1	F	4415	0.09
48	2	I	4415	0.09
49	1	F	4438	0.08
49	2	J	4438	0.08
50	1	F	4423	0.1
50	2	L	4423	0.1
51	1	F	4499	0.08
51	2	K	4499	0.08
52	1	G	4564	0.08
52	2	H	4564	0.08
53	1	G	4439	0.09
53	2	I	4439	0.09
54	1	G	4519	0.07
54	2	J	4519	0.07
55	1	G	4524	0.09
55	2	L	4524	0.09
56	1	G	4561	0.07
56	2	K	4561	0.07
57	1	H	4405	0.09
57	2	I	4405	0.09
58	1	H	4469	0.07
58	2	J	4469	0.07
59	1	H	4451	0.1
59	2	L	4451	0.1
60	1	H	4483	0.09
60	2	K	4483	0.09
61	1	I	4372	0.1
61	2	J	4372	0.1
62	1	I	4408	0.09
62	2	L	4408	0.09
63	1	I	4381	0.1
63	2	K	4381	0.1
64	1	J	4477	0.08
64	2	L	4477	0.08
65	1	J	4553	0.06
65	2	K	4553	0.06
66	1	L	4480	0.09
66	2	K	4480	0.09

LS refinement shell

Resolution: 2.043→2.096 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.293	589	-
Rwork	0.274	11521	-
obs	-	-	97.71 %