PDB-8z4v: LH2 complex from Ectothiorhodospira haloalkaliphila at near-atomi...

ID or keywords:

Entry

Database: PDB / ID: 8z4v

Title

LH2 complex from Ectothiorhodospira haloalkaliphila at near-atomic resolution

Components

Light-harvesting protein B-800/850 alpha chain
Light-harvesting protein B:800-850 subunit beta

Keywords

PHOTOSYNTHESIS / Light-harvesing / purple sulfur bacteria / cryo-EM

Function / homology

Function and homology information

plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthesis, light reaction / : / metal ion binding / plasma membrane
Similarity search - Function

Biological species

Ectothiorhodospira haloalkaliphila ATCC 51935 (bacteria)

Method

ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 1.7 Å

Authors

Burtseva, A.D. / Baymukhametov, T.N. / Popov, V.O. / Ashikhmin, A.A. / Boyko, K.M.

Funding support

Russian Federation, 1items

Citation

Journal: Structure / Year: 2025
Title: Near-atomic cryo-EM structure of the light-harvesting complex LH2 from the sulfur purple bacterium Ectothiorhodospira haloalkaliphila.
Authors: Anna D Burtseva / Timur N Baymukhametov / Maxim A Bolshakov / Zoya К Makhneva / Andrey V Mardanov / Andrey M Tsedilin / Huawei Zhang / Vladimir O Popov / Aleksandr A Ashikhmin / Konstantin M Boyko /

Abstract: Bacteria with the simplest system for solar energy absorption and conversion use various types of light-harvesting complexes for these purposes. Light-harvesting complex 2 (LH2), an important ...

History

Deposition	Apr 17, 2024	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Jan 1, 2025	Provider: repository / Type: Initial release
Revision 1.1	Feb 19, 2025	Group: Data collection / Database references / Category: citation / em_admin Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year / _em_admin.last_update

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	8z4v.cif.gz	213.1 KB	Display	PDBx/mmCIF format
PDB format	pdb8z4v.ent.gz		Display	PDB format
PDBx/mmJSON format	8z4v.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	8z4v_validation.pdf.gz	2.2 MB	Display	wwPDB validaton report
Full document	8z4v_full_validation.pdf.gz	2.3 MB	Display
Data in XML	8z4v_validation.xml.gz	62.5 KB	Display
Data in CIF	8z4v_validation.cif.gz	72.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/z4/8z4v ftp://data.pdbj.org/pub/pdb/validation_reports/z4/8z4v	HTTPS FTP

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Related structure data

Related structure data	39770MC M: map data used to model this data C: citing same article (ref.)
Similar structure data	Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Light-harvesting protein B:800-850 subunit beta

C: Light-harvesting protein B-800/850 alpha chain

D: Light-harvesting protein B:800-850 subunit beta

E: Light-harvesting protein B-800/850 alpha chain

G: Light-harvesting protein B:800-850 subunit beta

H: Light-harvesting protein B-800/850 alpha chain

J: Light-harvesting protein B:800-850 subunit beta

K: Light-harvesting protein B-800/850 alpha chain

M: Light-harvesting protein B:800-850 subunit beta

N: Light-harvesting protein B-800/850 alpha chain

P: Light-harvesting protein B:800-850 subunit beta

Q: Light-harvesting protein B-800/850 alpha chain

S: Light-harvesting protein B:800-850 subunit beta

T: Light-harvesting protein B-800/850 alpha chain

V: Light-harvesting protein B:800-850 subunit beta

W: Light-harvesting protein B-800/850 alpha chain

hetero molecules

133 kDa, 16 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author
Evidence: gel filtration, not applicable

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: 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	ASN	ASN	TYR	TYR	A	A	4 - 46	4 - 46
2	1	ASN	ASN	TYR	TYR	D	C	4 - 46	4 - 46
3	2	ASN	ASN	TYR	TYR	A	A	4 - 46	4 - 46
4	2	ASN	ASN	TYR	TYR	G	E	4 - 46	4 - 46
5	3	ASN	ASN	TYR	TYR	A	A	4 - 46	4 - 46
6	3	ASN	ASN	TYR	TYR	J	G	4 - 46	4 - 46
7	4	ASN	ASN	TYR	TYR	A	A	4 - 46	4 - 46
8	4	ASN	ASN	TYR	TYR	M	I	4 - 46	4 - 46
9	5	ASN	ASN	TYR	TYR	A	A	4 - 46	4 - 46
10	5	ASN	ASN	TYR	TYR	P	K	4 - 46	4 - 46
11	6	ASN	ASN	TYR	TYR	A	A	4 - 46	4 - 46
12	6	ASN	ASN	TYR	TYR	S	M	4 - 46	4 - 46
13	7	ASN	ASN	TYR	TYR	A	A	4 - 46	4 - 46
14	7	ASN	ASN	TYR	TYR	V	O	4 - 46	4 - 46
15	8	GLU	GLU	PHE	PHE	C	B	3 - 57	3 - 57
16	8	GLU	GLU	PHE	PHE	E	D	3 - 57	3 - 57
17	9	GLU	GLU	PHE	PHE	C	B	3 - 57	3 - 57
18	9	GLU	GLU	PHE	PHE	H	F	3 - 57	3 - 57
19	10	GLU	GLU	PHE	PHE	C	B	3 - 57	3 - 57
20	10	GLU	GLU	PHE	PHE	K	H	3 - 57	3 - 57
21	11	GLU	GLU	PHE	PHE	C	B	3 - 57	3 - 57
22	11	GLU	GLU	PHE	PHE	N	J	3 - 57	3 - 57
23	12	GLU	GLU	PHE	PHE	C	B	3 - 57	3 - 57
24	12	GLU	GLU	PHE	PHE	Q	L	3 - 57	3 - 57
25	13	GLU	GLU	PHE	PHE	C	B	3 - 57	3 - 57
26	13	GLU	GLU	PHE	PHE	T	N	3 - 57	3 - 57
27	14	GLU	GLU	PHE	PHE	C	B	3 - 57	3 - 57
28	14	GLU	GLU	PHE	PHE	W	P	3 - 57	3 - 57
29	15	ASN	ASN	TYR	TYR	D	C	4 - 46	4 - 46
30	15	ASN	ASN	TYR	TYR	G	E	4 - 46	4 - 46
31	16	ASN	ASN	TYR	TYR	D	C	4 - 46	4 - 46
32	16	ASN	ASN	TYR	TYR	J	G	4 - 46	4 - 46
33	17	ASN	ASN	TYR	TYR	D	C	4 - 46	4 - 46
34	17	ASN	ASN	TYR	TYR	M	I	4 - 46	4 - 46
35	18	ASN	ASN	TYR	TYR	D	C	4 - 46	4 - 46
36	18	ASN	ASN	TYR	TYR	P	K	4 - 46	4 - 46
37	19	ASN	ASN	TYR	TYR	D	C	4 - 46	4 - 46
38	19	ASN	ASN	TYR	TYR	S	M	4 - 46	4 - 46
39	20	ASN	ASN	TYR	TYR	D	C	4 - 46	4 - 46
40	20	ASN	ASN	TYR	TYR	V	O	4 - 46	4 - 46
41	21	GLU	GLU	PHE	PHE	E	D	3 - 57	3 - 57
42	21	GLU	GLU	PHE	PHE	H	F	3 - 57	3 - 57
43	22	GLU	GLU	PHE	PHE	E	D	3 - 57	3 - 57
44	22	GLU	GLU	PHE	PHE	K	H	3 - 57	3 - 57
45	23	GLU	GLU	PHE	PHE	E	D	3 - 57	3 - 57
46	23	GLU	GLU	PHE	PHE	N	J	3 - 57	3 - 57
47	24	GLU	GLU	PHE	PHE	E	D	3 - 57	3 - 57
48	24	GLU	GLU	PHE	PHE	Q	L	3 - 57	3 - 57
49	25	GLU	GLU	PHE	PHE	E	D	3 - 57	3 - 57
50	25	GLU	GLU	PHE	PHE	T	N	3 - 57	3 - 57
51	26	GLU	GLU	PHE	PHE	E	D	3 - 57	3 - 57
52	26	GLU	GLU	PHE	PHE	W	P	3 - 57	3 - 57
53	27	ASN	ASN	TYR	TYR	G	E	4 - 46	4 - 46
54	27	ASN	ASN	TYR	TYR	J	G	4 - 46	4 - 46
55	28	ASN	ASN	TYR	TYR	G	E	4 - 46	4 - 46
56	28	ASN	ASN	TYR	TYR	M	I	4 - 46	4 - 46
57	29	ASN	ASN	TYR	TYR	G	E	4 - 46	4 - 46
58	29	ASN	ASN	TYR	TYR	P	K	4 - 46	4 - 46
59	30	ASN	ASN	TYR	TYR	G	E	4 - 46	4 - 46
60	30	ASN	ASN	TYR	TYR	S	M	4 - 46	4 - 46
61	31	ASN	ASN	TYR	TYR	G	E	4 - 46	4 - 46
62	31	ASN	ASN	TYR	TYR	V	O	4 - 46	4 - 46
63	32	GLU	GLU	PHE	PHE	H	F	3 - 57	3 - 57
64	32	GLU	GLU	PHE	PHE	K	H	3 - 57	3 - 57
65	33	GLU	GLU	PHE	PHE	H	F	3 - 57	3 - 57
66	33	GLU	GLU	PHE	PHE	N	J	3 - 57	3 - 57
67	34	GLU	GLU	PHE	PHE	H	F	3 - 57	3 - 57
68	34	GLU	GLU	PHE	PHE	Q	L	3 - 57	3 - 57
69	35	GLU	GLU	PHE	PHE	H	F	3 - 57	3 - 57
70	35	GLU	GLU	PHE	PHE	T	N	3 - 57	3 - 57
71	36	GLU	GLU	PHE	PHE	H	F	3 - 57	3 - 57
72	36	GLU	GLU	PHE	PHE	W	P	3 - 57	3 - 57
73	37	ASN	ASN	TYR	TYR	J	G	4 - 46	4 - 46
74	37	ASN	ASN	TYR	TYR	M	I	4 - 46	4 - 46
75	38	ASN	ASN	TYR	TYR	J	G	4 - 46	4 - 46
76	38	ASN	ASN	TYR	TYR	P	K	4 - 46	4 - 46
77	39	ASN	ASN	TYR	TYR	J	G	4 - 46	4 - 46
78	39	ASN	ASN	TYR	TYR	S	M	4 - 46	4 - 46
79	40	ASN	ASN	TYR	TYR	J	G	4 - 46	4 - 46
80	40	ASN	ASN	TYR	TYR	V	O	4 - 46	4 - 46
81	41	GLU	GLU	PHE	PHE	K	H	3 - 57	3 - 57
82	41	GLU	GLU	PHE	PHE	N	J	3 - 57	3 - 57
83	42	GLU	GLU	PHE	PHE	K	H	3 - 57	3 - 57
84	42	GLU	GLU	PHE	PHE	Q	L	3 - 57	3 - 57
85	43	GLU	GLU	PHE	PHE	K	H	3 - 57	3 - 57
86	43	GLU	GLU	PHE	PHE	T	N	3 - 57	3 - 57
87	44	GLU	GLU	PHE	PHE	K	H	3 - 57	3 - 57
88	44	GLU	GLU	PHE	PHE	W	P	3 - 57	3 - 57
89	45	ASN	ASN	TYR	TYR	M	I	4 - 46	4 - 46
90	45	ASN	ASN	TYR	TYR	P	K	4 - 46	4 - 46
91	46	ASN	ASN	TYR	TYR	M	I	4 - 46	4 - 46
92	46	ASN	ASN	TYR	TYR	S	M	4 - 46	4 - 46
93	47	ASN	ASN	TYR	TYR	M	I	4 - 46	4 - 46
94	47	ASN	ASN	TYR	TYR	V	O	4 - 46	4 - 46
95	48	GLU	GLU	PHE	PHE	N	J	3 - 57	3 - 57
96	48	GLU	GLU	PHE	PHE	Q	L	3 - 57	3 - 57
97	49	GLU	GLU	PHE	PHE	N	J	3 - 57	3 - 57
98	49	GLU	GLU	PHE	PHE	T	N	3 - 57	3 - 57
99	50	GLU	GLU	PHE	PHE	N	J	3 - 57	3 - 57
100	50	GLU	GLU	PHE	PHE	W	P	3 - 57	3 - 57
101	51	ASN	ASN	TYR	TYR	P	K	4 - 46	4 - 46
102	51	ASN	ASN	TYR	TYR	S	M	4 - 46	4 - 46
103	52	ASN	ASN	TYR	TYR	P	K	4 - 46	4 - 46
104	52	ASN	ASN	TYR	TYR	V	O	4 - 46	4 - 46
105	53	GLU	GLU	PHE	PHE	Q	L	3 - 57	3 - 57
106	53	GLU	GLU	PHE	PHE	T	N	3 - 57	3 - 57
107	54	GLU	GLU	PHE	PHE	Q	L	3 - 57	3 - 57
108	54	GLU	GLU	PHE	PHE	W	P	3 - 57	3 - 57
109	55	ASN	ASN	TYR	TYR	S	M	4 - 46	4 - 46
110	55	ASN	ASN	TYR	TYR	V	O	4 - 46	4 - 46
111	56	GLU	GLU	PHE	PHE	T	N	3 - 57	3 - 57
112	56	GLU	GLU	PHE	PHE	W	P	3 - 57	3 - 57

NCS ensembles :

ID	Details
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

#1: Protein/peptide	Light-harvesting protein B:800-850 subunit beta Mass: 5468.237 Da / Num. of mol.: 8 / Source method: isolated from a natural source Source: (natural) Ectothiorhodospira haloalkaliphila ATCC 51935 (bacteria) References: UniProt: W8KQR0
#2: Protein	Light-harvesting protein B-800/850 alpha chain / Antenna complex alpha/beta subunit domain-containing protein Mass: 7855.903 Da / Num. of mol.: 8 / Source method: isolated from a natural source Source: (natural) Ectothiorhodospira haloalkaliphila ATCC 51935 (bacteria) References: UniProt: W8KE12
#3: Chemical	... ChemComp-BCL / BACTERIOCHLOROPHYLL A Mass: 911.504 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: C₅₅H₇₄MgN₄O₆ / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical	ChemComp-A1L0S / Anhydrorhodovibrin / (6~{E},8~{E},10~{E},12~{E},14~{E},16~{E},18~{E},20~{E},22~{E},24~{E},26~{E},28~{E})-31-methoxy-2,6,10,14,19,23,27,31-octamethyl-dotriaconta-2,6,8,10,12,14,16,18,20,22,24,26,28-tridecaene Mass: 566.899 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₄₁H₅₈O / Feature type: SUBJECT OF INVESTIGATION
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 88 / Source method: isolated from a natural source / Formula: H₂O
Has ligand of interest	Y
Has protein modification	N

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Experiment

Experiment	Method: ELECTRON MICROSCOPY
EM experiment	Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

Component	Name: LH2 complex from Ectothiorhodospira haloalkaliphila / Type: COMPLEX / Entity ID: #1-#2 / Source: NATURAL
Molecular weight	Experimental value: NO
Source (natural)	Organism: Ectothiorhodospira haloalkaliphila (bacteria)
Buffer solution	pH: 8
Specimen	Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen support	Details: The grids were stored under low vacuum conditions and were not specifically pretreated. Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R0.6/1
Vitrification	Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 278 K

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Electron microscopy imaging

Experimental equipment	Model: Titan Krios / Image courtesy: FEI Company
Microscopy	Model: FEI TITAN KRIOS / Details: Preliminary grid screening was performed manually.
Electron gun	Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lens	Mode: BRIGHT FIELD / Nominal magnification: 105000 X / Nominal defocus max: 1500 nm / Nominal defocus min: 600 nm / Cs: 0.01 mm / C2 aperture diameter: 100 µm / Alignment procedure: ZEMLIN TABLEAU
Specimen holder	Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recording	Average exposure time: 2.5 sec. / Electron dose: 52.5 e/Å² / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 7346
EM imaging optics	Energyfilter name: GIF Bioquantum / Energyfilter slit width: 15 eV Spherical aberration corrector: Microscope was modified with a Cs corrector (CEOS GmbH, Germany).
Image scans	Width: 5760 / Height: 4092

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Processing

EM software

ID	Name	Version	Category
1	Warp	1.0.9	particle selection
2	SerialEM	4.0.4	image acquisition
4	Warp	1.0.9	CTF correction
7	Coot	0.9.8.92	model fitting
9	cryoSPARC	4.4.1	initial Euler assignment
10	cryoSPARC	4.4.1	final Euler assignment
12	cryoSPARC	4.4.1	3D reconstruction
19	Servalcat	1.6.0	model refinement

CTF correction

Type: NONE

Particle selection

Num. of particles selected: 1589688

Symmetry

Point symmetry: C₈ (8 fold cyclic)

3D reconstruction

Resolution: 1.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 324434 / Symmetry type: POINT

Atomic model building

Protocol: AB INITIO MODEL / Space: REAL

Refinement

Resolution: 1.7→93.8 Å / Cor.coef. F_o:F_c: 0.892 / WR_factor R_work: 0.239 / SU B: 1.442 / SU ML: 0.042 / Average fsc overall: 0.8484 / Average fsc work: 0.8484 / ESU R: 0.073
Details: Hydrogens have been added in their riding positions

	R_factor	Num. reflection	% reflection
R_work	0.2387	281392	-
all	0.239	-	-
R_free	-	-	0 %
obs	-	-	100 %

Solvent computation

Solvent model: BABINET MODEL

Displacement parameters

B_iso mean: 31.95 Å²

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
ELECTRON MICROSCOPY	r_bond_refined_d	0.013	0.014	8368
ELECTRON MICROSCOPY	r_bond_other_d	0.025	0.018	7912
ELECTRON MICROSCOPY	r_angle_refined_deg	4.122	1.947	11768
ELECTRON MICROSCOPY	r_angle_other_deg	1.415	1.838	17880
ELECTRON MICROSCOPY	r_dihedral_angle_1_deg	5.412	5	760
ELECTRON MICROSCOPY	r_dihedral_angle_2_deg	26.483	17.143	448
ELECTRON MICROSCOPY	r_dihedral_angle_3_deg	11.572	15	872
ELECTRON MICROSCOPY	r_dihedral_angle_4_deg	5.163	15	8
ELECTRON MICROSCOPY	r_chiral_restr	0.09	0.2	1000
ELECTRON MICROSCOPY	r_gen_planes_refined	0.012	0.02	9472
ELECTRON MICROSCOPY	r_gen_planes_other	0.006	0.02	1992
ELECTRON MICROSCOPY	r_nbd_refined	0.216	0.2	3696
ELECTRON MICROSCOPY	r_symmetry_nbd_other	0.155	0.2	15634
ELECTRON MICROSCOPY	r_nbtor_refined	0.183	0.2	7952
ELECTRON MICROSCOPY	r_symmetry_nbtor_other	0.074	0.2	6858
ELECTRON MICROSCOPY	r_xyhbond_nbd_refined	0.109	0.2	288
ELECTRON MICROSCOPY	r_mcbond_it	2.257	3.251	3104
ELECTRON MICROSCOPY	r_mcbond_other	2.258	3.25	3103
ELECTRON MICROSCOPY	r_mcangle_it	3.436	4.864	3848
ELECTRON MICROSCOPY	r_mcangle_other	3.435	4.865	3849
ELECTRON MICROSCOPY	r_scbond_it	2.633	3.487	5264
ELECTRON MICROSCOPY	r_scbond_other	2.633	3.487	5265
ELECTRON MICROSCOPY	r_scangle_it	4.024	5.062	7920
ELECTRON MICROSCOPY	r_scangle_other	4.024	5.063	7921
ELECTRON MICROSCOPY	r_lrange_it	6.654	59.154	31282
ELECTRON MICROSCOPY	r_lrange_other	6.654	59.155	31279
ELECTRON MICROSCOPY	r_ncsr_local_group_1	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_2	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_3	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_4	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_5	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_6	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_7	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_8	0	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_9	0	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_10	0.031	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_11	0.033	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_12	0.031	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_13	0.031	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_14	0	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_15	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_16	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_17	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_18	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_19	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_20	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_21	0	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_22	0.031	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_23	0.032	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_24	0.031	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_25	0.031	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_26	0	0.05	3308
ELECTRON MICROSCOPY	r_ncsr_local_group_27	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_28	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_29	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_30	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_31	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_32	0.031	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_33	0.033	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_34	0.031	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_35	0.031	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_36	0	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_37	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_38	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_39	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_40	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_41	0.002	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_42	0	0.05	3308
ELECTRON MICROSCOPY	r_ncsr_local_group_43	0.001	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_44	0.031	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_45	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_46	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_47	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_48	0.002	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_49	0.002	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_50	0.032	0.05	3304
ELECTRON MICROSCOPY	r_ncsr_local_group_51	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_52	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_53	0.001	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_54	0.031	0.05	3306
ELECTRON MICROSCOPY	r_ncsr_local_group_55	0	0.05	2750
ELECTRON MICROSCOPY	r_ncsr_local_group_56	0.031	0.05	3304

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Refine-ID	Type	Rms dev position (Å)	Weight position
1	1	A	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
1	2	D	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
2	3	A	ELECTRON MICROSCOPY	Local ncs	0.00011	0.05006
2	4	G	ELECTRON MICROSCOPY	Local ncs	0.00011	0.05006
3	5	A	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
3	6	J	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
4	7	A	ELECTRON MICROSCOPY	Local ncs	0.00011	0.05006
4	8	M	ELECTRON MICROSCOPY	Local ncs	0.00011	0.05006
5	9	A	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
5	10	P	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
6	11	A	ELECTRON MICROSCOPY	Local ncs	0.00011	0.05006
6	12	S	ELECTRON MICROSCOPY	Local ncs	0.00011	0.05006
7	13	A	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
7	14	V	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
8	15	C	ELECTRON MICROSCOPY	Local ncs	0.00021	0.05009
8	16	E	ELECTRON MICROSCOPY	Local ncs	0.00021	0.05009
9	17	C	ELECTRON MICROSCOPY	Local ncs	7.0E-5	0.05009
9	18	H	ELECTRON MICROSCOPY	Local ncs	7.0E-5	0.05009
10	19	C	ELECTRON MICROSCOPY	Local ncs	0.03124	0.05009
10	20	K	ELECTRON MICROSCOPY	Local ncs	0.03124	0.05009
11	21	C	ELECTRON MICROSCOPY	Local ncs	0.0325	0.05009
11	22	N	ELECTRON MICROSCOPY	Local ncs	0.0325	0.05009
12	23	C	ELECTRON MICROSCOPY	Local ncs	0.03126	0.05009
12	24	Q	ELECTRON MICROSCOPY	Local ncs	0.03126	0.05009
13	25	C	ELECTRON MICROSCOPY	Local ncs	0.03073	0.05009
13	26	T	ELECTRON MICROSCOPY	Local ncs	0.03073	0.05009
14	27	C	ELECTRON MICROSCOPY	Local ncs	0.00021	0.05009
14	28	W	ELECTRON MICROSCOPY	Local ncs	0.00021	0.05009
15	29	D	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
15	30	G	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
16	31	D	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
16	32	J	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
17	33	D	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
17	34	M	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
18	35	D	ELECTRON MICROSCOPY	Local ncs	3.0E-5	0.05006
18	36	P	ELECTRON MICROSCOPY	Local ncs	3.0E-5	0.05006
19	37	D	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
19	38	S	ELECTRON MICROSCOPY	Local ncs	0.00046	0.05006
20	39	D	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
20	40	V	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
21	41	E	ELECTRON MICROSCOPY	Local ncs	0.00021	0.05009
21	42	H	ELECTRON MICROSCOPY	Local ncs	0.00021	0.05009
22	43	E	ELECTRON MICROSCOPY	Local ncs	0.03121	0.05009
22	44	K	ELECTRON MICROSCOPY	Local ncs	0.03121	0.05009
23	45	E	ELECTRON MICROSCOPY	Local ncs	0.03248	0.05009
23	46	N	ELECTRON MICROSCOPY	Local ncs	0.03248	0.05009
24	47	E	ELECTRON MICROSCOPY	Local ncs	0.03123	0.05009
24	48	Q	ELECTRON MICROSCOPY	Local ncs	0.03123	0.05009
25	49	E	ELECTRON MICROSCOPY	Local ncs	0.03072	0.05009
25	50	T	ELECTRON MICROSCOPY	Local ncs	0.03072	0.05009
26	51	E	ELECTRON MICROSCOPY	Local ncs	7.0E-5	0.05009
26	52	W	ELECTRON MICROSCOPY	Local ncs	7.0E-5	0.05009
27	53	G	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
27	54	J	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
28	55	G	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
28	56	M	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
29	57	G	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
29	58	P	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
30	59	G	ELECTRON MICROSCOPY	Local ncs	4.0E-5	0.05006
30	60	S	ELECTRON MICROSCOPY	Local ncs	4.0E-5	0.05006
31	61	G	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
31	62	V	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
32	63	H	ELECTRON MICROSCOPY	Local ncs	0.03124	0.05009
32	64	K	ELECTRON MICROSCOPY	Local ncs	0.03124	0.05009
33	65	H	ELECTRON MICROSCOPY	Local ncs	0.03251	0.05009
33	66	N	ELECTRON MICROSCOPY	Local ncs	0.03251	0.05009
34	67	H	ELECTRON MICROSCOPY	Local ncs	0.03127	0.05009
34	68	Q	ELECTRON MICROSCOPY	Local ncs	0.03127	0.05009
35	69	H	ELECTRON MICROSCOPY	Local ncs	0.03074	0.05009
35	70	T	ELECTRON MICROSCOPY	Local ncs	0.03074	0.05009
36	71	H	ELECTRON MICROSCOPY	Local ncs	0.00021	0.05009
36	72	W	ELECTRON MICROSCOPY	Local ncs	0.00021	0.05009
37	73	J	ELECTRON MICROSCOPY	Local ncs	0.00044	0.05006
37	74	M	ELECTRON MICROSCOPY	Local ncs	0.00044	0.05006
38	75	J	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
38	76	P	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
39	77	J	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
39	78	S	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
40	79	J	ELECTRON MICROSCOPY	Local ncs	4.0E-5	0.05006
40	80	V	ELECTRON MICROSCOPY	Local ncs	4.0E-5	0.05006
41	81	K	ELECTRON MICROSCOPY	Local ncs	0.00179	0.05009
41	82	N	ELECTRON MICROSCOPY	Local ncs	0.00179	0.05009
42	83	K	ELECTRON MICROSCOPY	Local ncs	7.0E-5	0.05009
42	84	Q	ELECTRON MICROSCOPY	Local ncs	7.0E-5	0.05009
43	85	K	ELECTRON MICROSCOPY	Local ncs	0.00075	0.05009
43	86	T	ELECTRON MICROSCOPY	Local ncs	0.00075	0.05009
44	87	K	ELECTRON MICROSCOPY	Local ncs	0.03121	0.05009
44	88	W	ELECTRON MICROSCOPY	Local ncs	0.03121	0.05009
45	89	M	ELECTRON MICROSCOPY	Local ncs	0.00044	0.05006
45	90	P	ELECTRON MICROSCOPY	Local ncs	0.00044	0.05006
46	91	M	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
46	92	S	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
47	93	M	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
47	94	V	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
48	95	N	ELECTRON MICROSCOPY	Local ncs	0.00178	0.05009
48	96	Q	ELECTRON MICROSCOPY	Local ncs	0.00178	0.05009
49	97	N	ELECTRON MICROSCOPY	Local ncs	0.00246	0.05009
49	98	T	ELECTRON MICROSCOPY	Local ncs	0.00246	0.05009
50	99	N	ELECTRON MICROSCOPY	Local ncs	0.03248	0.05009
50	100	W	ELECTRON MICROSCOPY	Local ncs	0.03248	0.05009
51	101	P	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
51	102	S	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
52	103	P	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
52	104	V	ELECTRON MICROSCOPY	Local ncs	5.0E-5	0.05006
53	105	Q	ELECTRON MICROSCOPY	Local ncs	0.00076	0.05009
53	106	T	ELECTRON MICROSCOPY	Local ncs	0.00076	0.05009
54	107	Q	ELECTRON MICROSCOPY	Local ncs	0.03124	0.05009
54	108	W	ELECTRON MICROSCOPY	Local ncs	0.03124	0.05009
55	109	S	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
55	110	V	ELECTRON MICROSCOPY	Local ncs	0.00045	0.05006
56	111	T	ELECTRON MICROSCOPY	Local ncs	0.03072	0.05009
56	112	W	ELECTRON MICROSCOPY	Local ncs	0.03072	0.05009

LS refinement shell

Refine-ID: ELECTRON MICROSCOPY / Num. reflection R_free: _ / Total num. of bins used: 20 / % reflection obs: 100 %

Resolution (Å)	R_factor R_work	Num. reflection R_work	R_factor all	Num. reflection all	Fsc work	WR_factor R_work
1.7-1.744	1.035	20839	1.035	20839	0.464	1.035
1.744-1.792	0.779	20398	0.779	20398	0.564	0.779
1.792-1.844	0.643	19633	0.643	19633	0.681	0.643
1.844-1.901	0.595	19061	0.595	19061	0.754	0.595
1.901-1.963	0.515	18647	0.515	18647	0.831	0.515
1.963-2.032	0.335	17922	0.335	17922	0.901	0.335
2.032-2.108	0.245	17339	0.245	17339	0.929	0.245
2.108-2.195	0.212	16623	0.212	16623	0.949	0.212
2.195-2.292	0.203	16082	0.203	16082	0.961	0.203
2.292-2.404	0.195	15325	0.195	15325	0.966	0.195
2.404-2.534	0.182	14516	0.182	14516	0.967	0.182
2.534-2.687	0.19	13764	0.19	13764	0.964	0.19
2.687-2.873	0.178	12899	0.178	12899	0.968	0.178
2.873-3.103	0.163	12126	0.163	12126	0.971	0.163
3.103-3.398	0.165	11000	0.165	11000	0.972	0.165
3.398-3.799	0.154	10009	0.154	10009	0.975	0.154
3.799-4.385	0.161	8812	0.161	8812	0.971	0.161
4.385-5.368	0.196	7434	0.196	7434	0.959	0.196
5.368-7.579	0.291	5774	0.291	5774	0.921	0.291
7.579-93.8	0.46	3189	0.46	3189	0.949	0.46

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