PDB-8pop: HK97 small terminase in complex with DNA

ID or keywords:

Entry

Database: PDB / ID: 8pop

Title

HK97 small terminase in complex with DNA

Components

(DNA (31-MER)) x 2
Terminase small subunit

Keywords

DNA BINDING PROTEIN / small terminase /

HK97 /

bacteriophage / complex with DNA

Function / homology

DNA / DNA (> 10) / Terminase small subunit

Function and homology information

Biological species

Escherichia phage HK97 (virus)

Byrnievirus HK97

Method

ELECTRON MICROSCOPY /

single particle reconstruction /

cryo EM / Resolution: 3 Å

Authors

Chechik, M. / Greive, S.J. / Antson, A.A. / Jenkins, H.T.

Funding support

United Kingdom, 1items

Citation

Journal: bioRxiv / Year: 2023
Title: Structure of HK97 small terminase:DNA complex unveils a novel DNA binding mechanism by a circular protein.
Authors: Maria Chechik / Sandra J Greive / Alfred A Antson / Huw T Jenkins /

Abstract: DNA recognition is critical for assembly of double-stranded DNA viruses, in particular for the initiation of packaging the viral genome into the capsid. DNA packaging has been extensively studied for ...

History

Deposition	Jul 5, 2023	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Aug 9, 2023	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	8pop.cif.gz	234.8 KB	Display	PDBx/mmCIF format
PDB format	pdb8pop.ent.gz	183.6 KB	Display	PDB format
PDBx/mmJSON format	8pop.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/po/8pop ftp://data.pdbj.org/pub/pdb/validation_reports/po/8pop	HTTPS FTP

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Related structure data

Related structure data	17794MC 17818C M: map data used to model this data C: citing same article (ref.)
Similar structure data	Similarity search - Function & homologyF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
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PDB pages

PDBj /

wwPDB /

NCBI

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Deposited unit

A: Terminase small subunit

B: Terminase small subunit

C: Terminase small subunit

D: Terminase small subunit

E: Terminase small subunit

F: Terminase small subunit

G: Terminase small subunit

H: Terminase small subunit

I: Terminase small subunit

J: DNA (31-MER)

K: DNA (31-MER)

186 kDa, 11 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software
Evidence: electron microscopy, gel filtration x-ray structure

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Auth asym-ID: A / Label asym-ID: A

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth seq-ID	Label seq-ID
1	1	1	ASP	ASP	THR	THR	24 - 123	24 - 123
2	1	1	ASP	ASP	THR	THR	24 - 123	24 - 123
3	2	2	ASP	ASP	THR	THR	24 - 123	24 - 123
4	2	2	ASP	ASP	THR	THR	24 - 123	24 - 123
5	3	3	ASP	ASP	THR	THR	24 - 123	24 - 123
6	3	3	ASP	ASP	THR	THR	24 - 123	24 - 123
7	4	4	ASP	ASP	THR	THR	24 - 123	24 - 123
8	4	4	ASP	ASP	THR	THR	24 - 123	24 - 123
9	5	5	VAL	VAL	THR	THR	23 - 123	23 - 123
10	5	5	VAL	VAL	THR	THR	23 - 123	23 - 123
11	6	6	ASP	ASP	THR	THR	24 - 123	24 - 123
12	6	6	ASP	ASP	THR	THR	24 - 123	24 - 123
13	7	7	VAL	VAL	THR	THR	23 - 123	23 - 123
14	7	7	VAL	VAL	THR	THR	23 - 123	23 - 123
15	8	8	ASP	ASP	THR	THR	24 - 123	24 - 123
16	8	8	ASP	ASP	THR	THR	24 - 123	24 - 123
17	9	9	ASP	ASP	THR	THR	24 - 123	24 - 123
18	9	9	ASP	ASP	THR	THR	24 - 123	24 - 123
19	10	10	ASP	ASP	THR	THR	24 - 123	24 - 123
20	10	10	ASP	ASP	THR	THR	24 - 123	24 - 123
21	11	11	ASP	ASP	THR	THR	24 - 123	24 - 123
22	11	11	ASP	ASP	THR	THR	24 - 123	24 - 123
23	12	12	ASP	ASP	THR	THR	24 - 123	24 - 123
24	12	12	ASP	ASP	THR	THR	24 - 123	24 - 123
25	13	13	ASP	ASP	THR	THR	24 - 123	24 - 123
26	13	13	ASP	ASP	THR	THR	24 - 123	24 - 123
27	14	14	ASP	ASP	THR	THR	24 - 123	24 - 123
28	14	14	ASP	ASP	THR	THR	24 - 123	24 - 123
29	15	15	ASP	ASP	THR	THR	24 - 123	24 - 123
30	15	15	ASP	ASP	THR	THR	24 - 123	24 - 123
31	16	16	ASP	ASP	ASN	ASN	24 - 124	24 - 124
32	16	16	ASP	ASP	ASN	ASN	24 - 124	24 - 124
33	17	17	ASP	ASP	ASN	ASN	24 - 124	24 - 124
34	17	17	ASP	ASP	ASN	ASN	24 - 124	24 - 124
35	18	18	ASP	ASP	THR	THR	24 - 123	24 - 123
36	18	18	ASP	ASP	THR	THR	24 - 123	24 - 123
37	19	19	ASP	ASP	ASN	ASN	24 - 124	24 - 124
38	19	19	ASP	ASP	ASN	ASN	24 - 124	24 - 124
39	20	20	ASP	ASP	THR	THR	24 - 123	24 - 123
40	20	20	ASP	ASP	THR	THR	24 - 123	24 - 123
41	21	21	ASP	ASP	ASN	ASN	24 - 124	24 - 124
42	21	21	ASP	ASP	ASN	ASN	24 - 124	24 - 124
43	22	22	ASP	ASP	ASN	ASN	24 - 124	24 - 124
44	22	22	ASP	ASP	ASN	ASN	24 - 124	24 - 124
45	23	23	ASP	ASP	THR	THR	24 - 123	24 - 123
46	23	23	ASP	ASP	THR	THR	24 - 123	24 - 123
47	24	24	ASP	ASP	ASN	ASN	24 - 124	24 - 124
48	24	24	ASP	ASP	ASN	ASN	24 - 124	24 - 124
49	25	25	ASP	ASP	THR	THR	24 - 123	24 - 123
50	25	25	ASP	ASP	THR	THR	24 - 123	24 - 123
51	26	26	ASP	ASP	ASN	ASN	24 - 124	24 - 124
52	26	26	ASP	ASP	ASN	ASN	24 - 124	24 - 124
53	27	27	ASP	ASP	THR	THR	24 - 123	24 - 123
54	27	27	ASP	ASP	THR	THR	24 - 123	24 - 123
55	28	28	ASP	ASP	ASN	ASN	24 - 124	24 - 124
56	28	28	ASP	ASP	ASN	ASN	24 - 124	24 - 124
57	29	29	ASP	ASP	THR	THR	24 - 123	24 - 123
58	29	29	ASP	ASP	THR	THR	24 - 123	24 - 123
59	30	30	ASP	ASP	ASN	ASN	24 - 124	24 - 124
60	30	30	ASP	ASP	ASN	ASN	24 - 124	24 - 124
61	31	31	ASP	ASP	THR	THR	24 - 123	24 - 123
62	31	31	ASP	ASP	THR	THR	24 - 123	24 - 123
63	32	32	VAL	VAL	ASN	ASN	23 - 124	23 - 124
64	32	32	VAL	VAL	ASN	ASN	23 - 124	23 - 124
65	33	33	ASP	ASP	THR	THR	24 - 123	24 - 123
66	33	33	ASP	ASP	THR	THR	24 - 123	24 - 123
67	34	34	ASP	ASP	THR	THR	24 - 123	24 - 123
68	34	34	ASP	ASP	THR	THR	24 - 123	24 - 123
69	35	35	ASP	ASP	ASN	ASN	24 - 124	24 - 124
70	35	35	ASP	ASP	ASN	ASN	24 - 124	24 - 124
71	36	36	ASP	ASP	THR	THR	24 - 123	24 - 123
72	36	36	ASP	ASP	THR	THR	24 - 123	24 - 123

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

#1: Protein	Terminase small subunit Mass: 18497.648 Da / Num. of mol.: 9 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia phage HK97 (virus) / Plasmid: Champion pET SUMO Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: Q9MBW4
#2: DNA chain	DNA (31-MER) Mass: 9600.261 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Byrnievirus HK97
#3: DNA chain	DNA (31-MER) Mass: 9457.115 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Byrnievirus HK97

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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: HK97 small terminase in complex with DNA / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT

Molecular weight

ID	Entity assembly-ID	Value (°)	Units	Experimental value
1	1	0.185 MDa		NO
2	1	0.166 MDa		NO
3	1		MEGADALTONS	NO

Source (natural)

Organism:

Hendrixvirus

Source (recombinant)

Organism:

Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
Plasmid: Champion pET SUMO

Buffer solution

pH: 7.5

Buffer component

ID	Conc.	Name	Formula	Buffer-ID
1	200 mM	sodium chloride	NaClSodium chloride	1
2	10 mM	magnesium chloride	MgCl₂	1
3	25 mM	Tris-HClTris	C₄H₁₁NO₃.HCl	1

Specimen

Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: complex was purified on S200 10/30 column

Specimen support

Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: UltrAuFoil R1.2/1.3

Vitrification

Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy imaging

Experimental equipment	Model: Titan Krios / Image courtesy: FEI Company
Microscopy	Model: FEI TITAN KRIOS
Electron gun	Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lens	Mode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 130000 X / Nominal defocus max: 2400 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE
Specimen holder	Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recording	Average exposure time: 8 sec. / Electron dose: 53.6 e/Å² / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 2767 Details: Two datasets were collected from the same grid. 1st set: 682 images 2nd set: 2085 images
EM imaging optics	Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV

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Processing

EM software

ID	Name	Version	Category	Details
1	Topaz		particle selection
2	EPU		image acquisition
4	CTFFIND	4.1	CTF correction	CTF estimation
5	RELION	3.1	CTF correction	CTF correction
8	Coot	0.9.8	model fitting
10	RELION	3.1	initial Euler assignment
11	RELION	3.1	final Euler assignment
12	RELION	3.1	classification
13	RELION	3.1	3D reconstruction
14	REFMAC	5.8.0411	model refinement	Servalcat/REFMAC

CTF correction

Details: CTF correction in RELION / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION

Particle selection

Num. of particles selected: 1144385 / Details: dataset 1:306866 dataset 2:837519

Symmetry

Point symmetry: C₁ (asymmetric)

3D reconstruction

Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 76628 / Algorithm: FOURIER SPACE / Num. of class averages: 1 / Symmetry type: POINT

Atomic model building

Protocol: AB INITIO MODEL / Space: RECIPROCAL

Atomic model building

PDB-ID: 6z6e

6z6e

Pdb chain-ID: A / Accession code: 6z6e / Chain residue range: 24-124 / Pdb chain residue range: 24-124 / Source name: PDB / Type: experimental model

Refinement

Resolution: 3→114.133 Å / Cor.coef. F_o:F_c: 0.896 / WR_factor R_work: 0.304 / SU B: 14.201 / SU ML: 0.25 / Average fsc free: 0 / Average fsc overall: 0.8472 / Average fsc work: 0.8472 / ESU R: 0.331
Details: Hydrogens have been added in their riding positions

	R_factor	Num. reflection	% reflection
R_work	0.3043	103499	-
all	0.304	-	-
R_free	-	-	0 %
obs	-	-	100 %

Solvent computation

Solvent model: NONE

Displacement parameters

B_iso mean: 88.647 Å²

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
ELECTRON MICROSCOPY	r_bond_refined_d	0.006	0.012	9248
ELECTRON MICROSCOPY	r_bond_other_d	0	0.016	8392
ELECTRON MICROSCOPY	r_angle_refined_deg	1.335	1.68	12636
ELECTRON MICROSCOPY	r_angle_other_deg	0.434	1.586	19326
ELECTRON MICROSCOPY	r_dihedral_angle_1_deg	5.856	5.241	1242
ELECTRON MICROSCOPY	r_dihedral_angle_2_deg	5.981	5	96
ELECTRON MICROSCOPY	r_dihedral_angle_other_2_deg	0.511	5	36
ELECTRON MICROSCOPY	r_dihedral_angle_3_deg	13.993	10	1519
ELECTRON MICROSCOPY	r_dihedral_angle_6_deg	13.981	10	425
ELECTRON MICROSCOPY	r_chiral_restr	0.102	0.211	1470
ELECTRON MICROSCOPY	r_gen_planes_refined	0.007	0.02	10097
ELECTRON MICROSCOPY	r_gen_planes_other	0.001	0.02	2012
ELECTRON MICROSCOPY	r_nbd_refined	0.223	0.2	1918
ELECTRON MICROSCOPY	r_symmetry_nbd_other	0.188	0.2	7047
ELECTRON MICROSCOPY	r_nbtor_refined	0.187	0.2	4399
ELECTRON MICROSCOPY	r_symmetry_nbtor_other	0.071	0.2	5098
ELECTRON MICROSCOPY	r_xyhbond_nbd_refined	0.17	0.2	100
ELECTRON MICROSCOPY	r_paralell_plane_angle_deg	2.262	0.6	49
ELECTRON MICROSCOPY	r_mcbond_it	8.971	7.476	3803
ELECTRON MICROSCOPY	r_mcbond_other	8.969	7.475	3803
ELECTRON MICROSCOPY	r_mcangle_it	13.854	13.4	4738
ELECTRON MICROSCOPY	r_mcangle_other	13.853	13.402	4739
ELECTRON MICROSCOPY	r_scbond_it	13.625	9.926	5445
ELECTRON MICROSCOPY	r_scbond_other	13.625	9.926	5445
ELECTRON MICROSCOPY	r_scangle_it	22.869	17.482	7898
ELECTRON MICROSCOPY	r_scangle_other	22.868	17.482	7899
ELECTRON MICROSCOPY	r_lrange_it	35.901	115.651	16057
ELECTRON MICROSCOPY	r_lrange_other	35.901	115.663	16058
ELECTRON MICROSCOPY	r_ncsr_local_group_1	0.094	0.05	3045
ELECTRON MICROSCOPY	r_ncsr_local_group_2	0.078	0.05	3059
ELECTRON MICROSCOPY	r_ncsr_local_group_3	0.083	0.05	3053
ELECTRON MICROSCOPY	r_ncsr_local_group_4	0.091	0.05	3031
ELECTRON MICROSCOPY	r_ncsr_local_group_5	0.091	0.05	3059
ELECTRON MICROSCOPY	r_ncsr_local_group_6	0.081	0.05	3056
ELECTRON MICROSCOPY	r_ncsr_local_group_7	0.087	0.05	3078
ELECTRON MICROSCOPY	r_ncsr_local_group_8	0.094	0.05	3049
ELECTRON MICROSCOPY	r_ncsr_local_group_9	0.096	0.05	3039
ELECTRON MICROSCOPY	r_ncsr_local_group_10	0.1	0.05	3024
ELECTRON MICROSCOPY	r_ncsr_local_group_11	0.092	0.05	3034
ELECTRON MICROSCOPY	r_ncsr_local_group_12	0.097	0.05	3029
ELECTRON MICROSCOPY	r_ncsr_local_group_13	0.096	0.05	3033
ELECTRON MICROSCOPY	r_ncsr_local_group_14	0.093	0.05	3029
ELECTRON MICROSCOPY	r_ncsr_local_group_15	0.1	0.05	3034
ELECTRON MICROSCOPY	r_ncsr_local_group_16	0.077	0.05	3101
ELECTRON MICROSCOPY	r_ncsr_local_group_17	0.079	0.05	3079
ELECTRON MICROSCOPY	r_ncsr_local_group_18	0.081	0.05	3046
ELECTRON MICROSCOPY	r_ncsr_local_group_19	0.072	0.05	3107
ELECTRON MICROSCOPY	r_ncsr_local_group_20	0.078	0.05	3061
ELECTRON MICROSCOPY	r_ncsr_local_group_21	0.09	0.05	3094
ELECTRON MICROSCOPY	r_ncsr_local_group_22	0.09	0.05	3087
ELECTRON MICROSCOPY	r_ncsr_local_group_23	0.065	0.05	3084
ELECTRON MICROSCOPY	r_ncsr_local_group_24	0.08	0.05	3100
ELECTRON MICROSCOPY	r_ncsr_local_group_25	0.086	0.05	3054
ELECTRON MICROSCOPY	r_ncsr_local_group_26	0.086	0.05	3088
ELECTRON MICROSCOPY	r_ncsr_local_group_27	0.084	0.05	3054
ELECTRON MICROSCOPY	r_ncsr_local_group_28	0.087	0.05	3099
ELECTRON MICROSCOPY	r_ncsr_local_group_29	0.07	0.05	3071
ELECTRON MICROSCOPY	r_ncsr_local_group_30	0.094	0.05	3072
ELECTRON MICROSCOPY	r_ncsr_local_group_31	0.087	0.05	3071
ELECTRON MICROSCOPY	r_ncsr_local_group_32	0.099	0.05	3082
ELECTRON MICROSCOPY	r_ncsr_local_group_33	0.092	0.05	3047
ELECTRON MICROSCOPY	r_ncsr_local_group_34	0.084	0.05	3059
ELECTRON MICROSCOPY	r_ncsr_local_group_35	0.082	0.05	3092
ELECTRON MICROSCOPY	r_ncsr_local_group_36	0.089	0.05	3066

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	0.09425	0.05009
1	2	A	ELECTRON MICROSCOPY	Local ncs	0.09425	0.05009
2	3	A	ELECTRON MICROSCOPY	Local ncs	0.07824	0.05009
2	4	A	ELECTRON MICROSCOPY	Local ncs	0.07824	0.05009
3	5	A	ELECTRON MICROSCOPY	Local ncs	0.0826	0.05009
3	6	A	ELECTRON MICROSCOPY	Local ncs	0.0826	0.05009
4	7	A	ELECTRON MICROSCOPY	Local ncs	0.09054	0.05009
4	8	A	ELECTRON MICROSCOPY	Local ncs	0.09054	0.05009
5	9	A	ELECTRON MICROSCOPY	Local ncs	0.09098	0.05009
5	10	A	ELECTRON MICROSCOPY	Local ncs	0.09098	0.05009
6	11	A	ELECTRON MICROSCOPY	Local ncs	0.08076	0.05009
6	12	A	ELECTRON MICROSCOPY	Local ncs	0.08076	0.05009
7	13	A	ELECTRON MICROSCOPY	Local ncs	0.08691	0.05009
7	14	A	ELECTRON MICROSCOPY	Local ncs	0.08691	0.05009
8	15	A	ELECTRON MICROSCOPY	Local ncs	0.09356	0.05009
8	16	A	ELECTRON MICROSCOPY	Local ncs	0.09356	0.05009
9	17	A	ELECTRON MICROSCOPY	Local ncs	0.09583	0.05009
9	18	A	ELECTRON MICROSCOPY	Local ncs	0.09583	0.05009
10	19	A	ELECTRON MICROSCOPY	Local ncs	0.0999	0.05009
10	20	A	ELECTRON MICROSCOPY	Local ncs	0.0999	0.05009
11	21	A	ELECTRON MICROSCOPY	Local ncs	0.09225	0.05009
11	22	A	ELECTRON MICROSCOPY	Local ncs	0.09225	0.05009
12	23	A	ELECTRON MICROSCOPY	Local ncs	0.0967	0.05009
12	24	A	ELECTRON MICROSCOPY	Local ncs	0.0967	0.05009
13	25	A	ELECTRON MICROSCOPY	Local ncs	0.09577	0.05009
13	26	A	ELECTRON MICROSCOPY	Local ncs	0.09577	0.05009
14	27	A	ELECTRON MICROSCOPY	Local ncs	0.09297	0.05009
14	28	A	ELECTRON MICROSCOPY	Local ncs	0.09297	0.05009
15	29	A	ELECTRON MICROSCOPY	Local ncs	0.09962	0.05009
15	30	A	ELECTRON MICROSCOPY	Local ncs	0.09962	0.05009
16	31	A	ELECTRON MICROSCOPY	Local ncs	0.07701	0.05009
16	32	A	ELECTRON MICROSCOPY	Local ncs	0.07701	0.05009
17	33	A	ELECTRON MICROSCOPY	Local ncs	0.07934	0.05009
17	34	A	ELECTRON MICROSCOPY	Local ncs	0.07934	0.05009
18	35	A	ELECTRON MICROSCOPY	Local ncs	0.08118	0.05009
18	36	A	ELECTRON MICROSCOPY	Local ncs	0.08118	0.05009
19	37	A	ELECTRON MICROSCOPY	Local ncs	0.07184	0.05009
19	38	A	ELECTRON MICROSCOPY	Local ncs	0.07184	0.05009
20	39	A	ELECTRON MICROSCOPY	Local ncs	0.07767	0.05009
20	40	A	ELECTRON MICROSCOPY	Local ncs	0.07767	0.05009
21	41	A	ELECTRON MICROSCOPY	Local ncs	0.08979	0.05009
21	42	A	ELECTRON MICROSCOPY	Local ncs	0.08979	0.05009
22	43	A	ELECTRON MICROSCOPY	Local ncs	0.09048	0.05009
22	44	A	ELECTRON MICROSCOPY	Local ncs	0.09048	0.05009
23	45	A	ELECTRON MICROSCOPY	Local ncs	0.06462	0.0501
23	46	A	ELECTRON MICROSCOPY	Local ncs	0.06462	0.0501
24	47	A	ELECTRON MICROSCOPY	Local ncs	0.07976	0.05009
24	48	A	ELECTRON MICROSCOPY	Local ncs	0.07976	0.05009
25	49	A	ELECTRON MICROSCOPY	Local ncs	0.08554	0.05009
25	50	A	ELECTRON MICROSCOPY	Local ncs	0.08554	0.05009
26	51	A	ELECTRON MICROSCOPY	Local ncs	0.08644	0.05009
26	52	A	ELECTRON MICROSCOPY	Local ncs	0.08644	0.05009
27	53	A	ELECTRON MICROSCOPY	Local ncs	0.08354	0.0501
27	54	A	ELECTRON MICROSCOPY	Local ncs	0.08354	0.0501
28	55	A	ELECTRON MICROSCOPY	Local ncs	0.08733	0.05009
28	56	A	ELECTRON MICROSCOPY	Local ncs	0.08733	0.05009
29	57	A	ELECTRON MICROSCOPY	Local ncs	0.06958	0.0501
29	58	A	ELECTRON MICROSCOPY	Local ncs	0.06958	0.0501
30	59	A	ELECTRON MICROSCOPY	Local ncs	0.09365	0.05009
30	60	A	ELECTRON MICROSCOPY	Local ncs	0.09365	0.05009
31	61	A	ELECTRON MICROSCOPY	Local ncs	0.08687	0.0501
31	62	A	ELECTRON MICROSCOPY	Local ncs	0.08687	0.0501
32	63	A	ELECTRON MICROSCOPY	Local ncs	0.09882	0.05009
32	64	A	ELECTRON MICROSCOPY	Local ncs	0.09882	0.05009
33	65	A	ELECTRON MICROSCOPY	Local ncs	0.09152	0.0501
33	66	A	ELECTRON MICROSCOPY	Local ncs	0.09152	0.0501
34	67	A	ELECTRON MICROSCOPY	Local ncs	0.08391	0.05009
34	68	A	ELECTRON MICROSCOPY	Local ncs	0.08391	0.05009
35	69	A	ELECTRON MICROSCOPY	Local ncs	0.08235	0.05009
35	70	A	ELECTRON MICROSCOPY	Local ncs	0.08235	0.05009
36	71	A	ELECTRON MICROSCOPY	Local ncs	0.08894	0.05009
36	72	A	ELECTRON MICROSCOPY	Local ncs	0.08894	0.05009

LS refinement shell

Refine-ID: ELECTRON MICROSCOPY / Num. reflection R_free: 0 / 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
3-3.078	0.731	7665	0.731	7665	0.557	0.731
3.078-3.162	0.472	7476	0.472	7476	0.687	0.472
3.162-3.254	0.387	7231	0.387	7231	0.801	0.387
3.254-3.354	0.347	7081	0.347	7081	0.849	0.347
3.354-3.464	0.327	6794	0.327	6794	0.851	0.327
3.464-3.585	0.31	6613	0.31	6613	0.867	0.31
3.585-3.72	0.286	6361	0.286	6361	0.884	0.286
3.72-3.872	0.277	6184	0.277	6184	0.896	0.277
3.872-4.044	0.269	5854	0.269	5854	0.91	0.269
4.044-4.241	0.262	5608	0.262	5608	0.914	0.262
4.241-4.47	0.268	5358	0.268	5358	0.919	0.268
4.47-4.741	0.271	5065	0.271	5065	0.934	0.271
4.741-5.068	0.263	4707	0.263	4707	0.935	0.263
5.068-5.473	0.249	4465	0.249	4465	0.925	0.249
5.473-5.994	0.282	4057	0.282	4057	0.894	0.282
5.994-6.699	0.326	3676	0.326	3676	0.852	0.326
6.699-7.731	0.306	3247	0.306	3247	0.865	0.306
7.731-9.457	0.275	2755	0.275	2755	0.904	0.275
9.457-13.329	0.242	2109	0.242	2109	0.928	0.242
13.329-114.133	0.43	1193	0.43	1193	0.964	0.43

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