PDB-7nt6: CryoEM structure of the Nipah virus nucleocapsid spiral clam-shap...

ID or keywords:

Entry

Database: PDB / ID: 7nt6

Title

CryoEM structure of the Nipah virus nucleocapsid spiral clam-shaped assembly

Components

Nucleoprotein
RNA (42-MER)
RNA (48-MER)

Keywords

VIRAL PROTEIN / Protein-RNA complex / Nucleocapsid

Function / homology

Function and homology information

negative stranded viral RNA transcription / negative stranded viral RNA replication / helical viral capsid / viral nucleocapsid / host cell cytoplasm / molecular adaptor activity / ribonucleoprotein complex / structural molecule activity / RNA binding
Similarity search - Function

Biological species

Nipah virus

Escherichia coli BL21 (bacteria)

Method

ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å

Authors

Ker, D.S. / Jenkins, H.T. / Greive, S.J. / Antson, A.A.

Funding support

United Kingdom, 1items

Citation

Journal: PLoS Pathog / Year: 2021
Title: CryoEM structure of the Nipah virus nucleocapsid assembly.
Authors: De-Sheng Ker / Huw T Jenkins / Sandra J Greive / Alfred A Antson /

Abstract: Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we ...

History

Deposition	Mar 9, 2021	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jul 7, 2021	Provider: repository / Type: Initial release
Revision 1.1	Jul 28, 2021	Group: Database references / Category: citation Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2	Jul 10, 2024	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_3d_fitting_list / em_admin / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type / _em_admin.last_update

Movie	Deposited structure unit Imaged by Jmol Download Simplified surface model + fitted atomic model EMDB-12584 Imaged by Jmol Download Superimposition on EM map EMDB-12584 Imaged by UCSF Chimera Download Movie viewer
Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	7nt6.cif.gz	768.7 KB	Display	PDBx/mmCIF format
PDB format	pdb7nt6.ent.gz	481.8 KB	Display	PDB format
PDBx/mmJSON format	7nt6.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	7nt6_validation.pdf.gz	1.5 MB	Display	wwPDB validaton report
Full document	7nt6_full_validation.pdf.gz	1.5 MB	Display
Data in XML	7nt6_validation.xml.gz	111.6 KB	Display
Data in CIF	7nt6_validation.cif.gz	198.3 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/nt/7nt6 ftp://data.pdbj.org/pub/pdb/validation_reports/nt/7nt6	HTTPS FTP

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Related structure data

Related structure data	12584MC 12581C 12582C 12583C 7nt5C M: map data used to model this data C: citing same article (ref.)
Similar structure data	5334 6338 10689 9400 3696 Search similar-shape structures by Omokage search (details) 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
Related items in Molecule of the Month	#121 - Jan 2010 70S Ribosomes similarity (1) #130 - Oct 2010 Riboswitches similarity (1) #16 - Apr 2001 Aminoacyl-tRNA Synthetases similarity (1) #157 - Jan 2013 Transfer-Messenger RNA similarity (1) #181 - Jan 2015 Cascade and CRISPR similarity (1) #260 - Aug 2021 Ribonuclease P similarity (1) #229 - Jan 2019 Fluorescent RNA Aptamers similarity (1) #253 - Jan 2021 Expressome similarity (1) #146 - Feb 2012 Aminoglycoside Antibiotics similarity (1) #249 - Sep 2020 SARS-CoV-2 RNA-dependent RNA Polymerase similarity (1) #15 - Mar 2001 Transfer RNA similarity (1) #10 - Oct 2000 Ribosome similarity (1) #87 - Mar 2007 Zinc Fingers similarity (1) #210 - Jun 2017 Adenine Riboswitch in Action similarity (1) #98 - Feb 2008 Small Interfering RNA similarity (1) #262 - Oct 2021 Fifty Years of Open Access to PDB Structures similarity (1) #65 - May 2005 Self-splicing RNA similarity (1) #245 - May 2020 Spliceosomes similarity (1) #226 - Oct 2018 Aminoglycoside Antibiotics and Resistance similarity (1) #105 - Sep 2008 Ribonuclease A similarity (1) #231 - Mar 2019 Measles Virus Proteins similarity (2) #230 - Feb 2019 Initiation Factor eIF4E similarity (1) #227 - Nov 2018 Telomerase similarity (1) #161 - May 2013 Ricin similarity (1) #143 - Nov 2011 Toll-like Receptors similarity (1) #106 - Oct 2008 Poly(A) Polymerase similarity (1) #266 - Feb 2022 Oligosaccharyltransferase similarity (1) #81 - Sep 2006 Elongation Factors similarity (1) #104 - Aug 2008 Selenocysteine Synthase similarity (1) #89 - May 2007 Aconitase and Iron Regulatory Protein 1 similarity (1) #62 - Feb 2005 Major Histocompatibility Complex similarity (2) #241 - Jan 2020 Twenty Years of Molecules similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#121 - Jan 2010
70S Ribosomes
similarity (1)
#130 - Oct 2010
Riboswitches
similarity (1)
#16 - Apr 2001
Aminoacyl-tRNA Synthetases
similarity (1)
#157 - Jan 2013
Transfer-Messenger RNA
similarity (1)
#181 - Jan 2015
Cascade and CRISPR
similarity (1)
#260 - Aug 2021
Ribonuclease P
similarity (1)
#229 - Jan 2019
Fluorescent RNA Aptamers
similarity (1)
#253 - Jan 2021
Expressome
similarity (1)
#146 - Feb 2012
Aminoglycoside Antibiotics
similarity (1)
#249 - Sep 2020
SARS-CoV-2 RNA-dependent RNA Polymerase
similarity (1)
#15 - Mar 2001
Transfer RNA
similarity (1)
#10 - Oct 2000
Ribosome
similarity (1)
#87 - Mar 2007
Zinc Fingers
similarity (1)
#210 - Jun 2017
Adenine Riboswitch in Action
similarity (1)
#98 - Feb 2008
Small Interfering RNA
similarity (1)
#262 - Oct 2021
Fifty Years of Open Access to PDB Structures
similarity (1)
#65 - May 2005
Self-splicing RNA
similarity (1)
#245 - May 2020
Spliceosomes
similarity (1)
#226 - Oct 2018
Aminoglycoside Antibiotics and Resistance
similarity (1)
#105 - Sep 2008
Ribonuclease A
similarity (1)
#231 - Mar 2019
Measles Virus Proteins
similarity (2)
#230 - Feb 2019
Initiation Factor eIF4E
similarity (1)
#227 - Nov 2018
Telomerase
similarity (1)
#161 - May 2013
Ricin
similarity (1)
#143 - Nov 2011
Toll-like Receptors
similarity (1)
#106 - Oct 2008
Poly(A) Polymerase
similarity (1)
#266 - Feb 2022
Oligosaccharyltransferase
similarity (1)
#81 - Sep 2006
Elongation Factors
similarity (1)
#104 - Aug 2008
Selenocysteine Synthase
similarity (1)
#89 - May 2007
Aconitase and Iron Regulatory Protein 1
similarity (1)
#62 - Feb 2005
Major Histocompatibility Complex
similarity (2)
#241 - Jan 2020
Twenty Years of Molecules
similarity (1)

Deposited unit

A: Nucleoprotein

B: Nucleoprotein

C: Nucleoprotein

D: Nucleoprotein

E: Nucleoprotein

F: Nucleoprotein

G: Nucleoprotein

H: Nucleoprotein

I: Nucleoprotein

J: Nucleoprotein

K: Nucleoprotein

L: Nucleoprotein

M: Nucleoprotein

N: Nucleoprotein

O: Nucleoprotein

X: RNA (48-MER)

Z: RNA (42-MER)

937 kDa, 17 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Ens-ID	Auth asym-ID	Auth seq-ID
1	1	X	7 - 47
2	1	Z	1 - 41
1	2	A	32 - 367
2	2	B	32 - 367
1	3	A	32 - 367
2	3	C	32 - 367
1	4	A	32 - 367
2	4	D	32 - 367
1	5	A	32 - 367
2	5	E	32 - 367
1	6	A	32 - 367
2	6	F	32 - 367
1	7	A	32 - 367
2	7	G	32 - 367
1	8	A	32 - 367
2	8	H	32 - 367
1	9	A	32 - 367
2	9	I	32 - 367
1	10	A	32 - 367
2	10	J	32 - 367
1	11	A	32 - 367
2	11	K	32 - 367
1	12	A	32 - 367
2	12	L	32 - 367
1	13	A	32 - 367
2	13	M	32 - 367
1	14	A	32 - 367
2	14	N	32 - 367
1	15	A	32 - 366
2	15	O	32 - 366
1	16	B	4 - 368
2	16	C	4 - 368
1	17	B	4 - 368
2	17	D	4 - 368
1	18	B	4 - 368
2	18	E	4 - 368
1	19	B	4 - 368
2	19	F	4 - 368
1	20	B	4 - 369
2	20	G	4 - 369
1	21	B	4 - 368
2	21	H	4 - 368
1	22	B	4 - 368
2	22	I	4 - 368
1	23	B	4 - 368
2	23	J	4 - 368
1	24	B	4 - 368
2	24	K	4 - 368
1	25	B	4 - 368
2	25	L	4 - 368
1	26	B	4 - 369
2	26	M	4 - 369
1	27	B	4 - 368
2	27	N	4 - 368
1	28	B	4 - 366
2	28	O	4 - 366
1	29	C	4 - 371
2	29	D	4 - 371
1	30	C	4 - 370
2	30	E	4 - 370
1	31	C	4 - 370
2	31	F	4 - 370
1	32	C	4 - 371
2	32	G	4 - 371
1	33	C	4 - 370
2	33	H	4 - 370
1	34	C	4 - 370
2	34	I	4 - 370
1	35	C	4 - 370
2	35	J	4 - 370
1	36	C	4 - 370
2	36	K	4 - 370
1	37	C	4 - 370
2	37	L	4 - 385
1	38	C	4 - 368
2	38	M	4 - 368
1	39	C	4 - 370
2	39	N	4 - 370
1	40	C	4 - 366
2	40	O	4 - 366
1	41	D	4 - 370
2	41	E	4 - 370
1	42	D	4 - 370
2	42	F	4 - 370
1	43	D	4 - 371
2	43	G	4 - 371
1	44	D	4 - 370
2	44	H	4 - 370
1	45	D	4 - 370
2	45	I	4 - 370
1	46	D	4 - 370
2	46	J	4 - 370
1	47	D	4 - 370
2	47	K	4 - 370
1	48	D	4 - 370
2	48	L	4 - 385
1	49	D	4 - 368
2	49	M	4 - 368
1	50	D	4 - 370
2	50	N	4 - 370
1	51	D	4 - 366
2	51	O	4 - 366
1	52	E	4 - 393
2	52	F	4 - 393
1	53	E	4 - 372
2	53	G	4 - 372
1	54	E	4 - 394
2	54	H	4 - 394
1	55	E	4 - 393
2	55	I	4 - 393
1	56	E	4 - 394
2	56	J	4 - 394
1	57	E	4 - 393
2	57	K	4 - 393
1	58	E	4 - 393
2	58	L	4 - 393
1	59	E	4 - 368
2	59	M	4 - 368
1	60	E	4 - 372
2	60	N	4 - 372
1	61	E	4 - 366
2	61	O	4 - 366
1	62	F	4 - 372
2	62	G	4 - 372
1	63	F	4 - 394
2	63	H	4 - 394
1	64	F	4 - 397
2	64	I	4 - 397
1	65	F	4 - 396
2	65	J	4 - 396
1	66	F	4 - 393
2	66	K	4 - 393
1	67	F	4 - 393
2	67	L	4 - 393
1	68	F	4 - 368
2	68	M	4 - 368
1	69	F	4 - 372
2	69	N	4 - 372
1	70	F	4 - 366
2	70	O	4 - 366
1	71	G	4 - 372
2	71	H	4 - 376
1	72	G	4 - 372
2	72	I	4 - 372
1	73	G	4 - 372
2	73	J	4 - 372
1	74	G	4 - 372
2	74	K	4 - 372
1	75	G	4 - 373
2	75	L	4 - 388
1	76	G	4 - 369
2	76	M	4 - 369
1	77	G	4 - 373
2	77	N	4 - 373
1	78	G	4 - 367
2	78	O	4 - 367
1	79	H	4 - 394
2	79	I	4 - 394
1	80	H	4 - 394
2	80	J	4 - 394
1	81	H	4 - 393
2	81	K	4 - 393
1	82	H	4 - 393
2	82	L	4 - 393
1	83	H	4 - 368
2	83	M	4 - 368
1	84	H	4 - 376
2	84	N	4 - 372
1	85	H	4 - 366
2	85	O	4 - 366
1	86	I	4 - 396
2	86	J	4 - 396
1	87	I	4 - 393
2	87	K	4 - 393
1	88	I	4 - 393
2	88	L	4 - 393
1	89	I	4 - 368
2	89	M	4 - 368
1	90	I	4 - 372
2	90	N	4 - 372
1	91	I	4 - 366
2	91	O	4 - 366
1	92	J	4 - 392
2	92	K	4 - 392
1	93	J	4 - 382
2	93	L	4 - 392
1	94	J	4 - 368
2	94	M	4 - 368
1	95	J	4 - 372
2	95	N	4 - 372
1	96	J	4 - 366
2	96	O	4 - 366
1	97	K	4 - 382
2	97	L	4 - 392
1	98	K	4 - 368
2	98	M	4 - 368
1	99	K	4 - 372
2	99	N	4 - 372
1	100	K	4 - 366
2	100	O	4 - 366
1	101	L	4 - 368
2	101	M	4 - 368
1	102	L	4 - 387
2	102	N	4 - 372
1	103	L	4 - 366
2	103	O	4 - 366
1	104	M	4 - 368
2	104	N	4 - 368
1	105	M	4 - 366
2	105	O	4 - 366
1	106	N	4 - 366
2	106	O	4 - 366

NCS ensembles :

#1: Protein	Nucleoprotein / Protein N / Nucleocapsid protein Mass: 60609.484 Da / Num. of mol.: 15 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Nipah virus / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9IK92
#2: RNA chain	RNA (48-MER) Mass: 14650.994 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli BL21(DE3) (bacteria) / Production host: Escherichia coli BL21(DE3) (bacteria)
#3: RNA chain	RNA (42-MER) Mass: 12814.002 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli BL21(DE3) (bacteria) / Production host: Escherichia coli BL21(DE3) (bacteria)

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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

ID	Name	Type	Entity ID	Parent-ID	Source
1	Nipah virus nucleocapsid Protein-RNA complex	COMPLEX	all	0	RECOMBINANT
2	Nucleoprotein	COMPLEX	#1	1	RECOMBINANT
3	RNA (48-MER)	COMPLEX	#2	1	RECOMBINANT
4	RNA (42-MER)	COMPLEX	#3	1	RECOMBINANT

Molecular weight

Value: 1 MDa / Experimental value: NO

Source (natural)

ID	Entity assembly-ID	Organism	Ncbi tax-ID
1	2	Nipah virus	121791
2	3	Escherichia coli BL21(DE3) (bacteria)	469008
3	4	Escherichia coli BL21(DE3) (bacteria)	469008

Source (recombinant)

ID	Entity assembly-ID	Organism	Ncbi tax-ID
1	2	Escherichia coli BL21(DE3) (bacteria)	469008
2	3	Escherichia coli BL21(DE3) (bacteria)	469008
3	4	Escherichia coli BL21(DE3) (bacteria)	469008

Buffer solution

pH: 8

Buffer component

ID	Conc.	Name	Formula	Buffer-ID
1	20 mM	Tris	C₄H₁₁NO₃	1
2	300 mM	sodium chloride	NaCl	1

Specimen

Conc.: 0.4 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES

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 FIELD / Nominal defocus max: 2100 nm / Nominal defocus min: 500 nm
Specimen holder	Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recording	Electron dose: 41 e/Å² / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k)
Image scans	Movie frames/image: 40 / Used frames/image: 1-40

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Processing

Software

Name: REFMAC / Version: 5.8.0267 / Classification: refinement

EM software

ID	Name	Version	Category
1	RELION	3	particle selection
2	EPU		image acquisition
4	CTFFIND	4	CTF correction
7	UCSF Chimera	1.13	model fitting
11	RELION	3.1beta	classification
12	RELION	3.1beta	3D reconstruction
19	REFMAC	5.8.0267	model refinement
20	PHENIX	1.17	model refinement
21	ERRASER	2	model refinement
22	ISOLDE	0.9	model refinement

CTF correction

Type: PHASE FLIPPING AND AMPLITUDE CORRECTION

Particle selection

Num. of particles selected: 217522

Symmetry

Point symmetry: C₁ (asymmetric)

3D reconstruction

Resolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 23029 / Num. of class averages: 1 / Symmetry type: POINT

Atomic model building

Protocol: RIGID BODY FIT

Atomic model building

PDB-ID: 7NT5

7nt5

Pdb chain-ID: H / Accession code: 7NT5 / Pdb chain residue range: 4-397 / Source name: PDB / Type: experimental model

Refinement

Resolution: 4.3→201.22 Å / Cor.coef. F_o:F_c: 0.983 / SU B: 81.568 / SU ML: 0.79 / ESU R: 0.757
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES

	R_factor	Num. reflection	% reflection
R_work	0.27534	-	-
obs	0.27534	155589	100 %

Solvent computation

Solvent model: PARAMETERS FOR MASK CACLULATION

Displacement parameters

B_iso mean: 113.558 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-3.36 Å²	2.6 Å²	0.4 Å²
2-	-	5.19 Å²	-7.1 Å²
3-	-	-	-1.82 Å²

Refinement step

Cycle: 1 / Total: 24128

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
ELECTRON MICROSCOPY	r_bond_refined_d	0.011	0.011	24281
ELECTRON MICROSCOPY	r_bond_other_d
ELECTRON MICROSCOPY	r_angle_refined_deg	1.96	1.538	30887
ELECTRON MICROSCOPY	r_angle_other_deg
ELECTRON MICROSCOPY	r_dihedral_angle_1_deg	8.138	5	5557
ELECTRON MICROSCOPY	r_dihedral_angle_2_deg
ELECTRON MICROSCOPY	r_dihedral_angle_3_deg
ELECTRON MICROSCOPY	r_dihedral_angle_4_deg
ELECTRON MICROSCOPY	r_chiral_restr	0.123	0.2	360
ELECTRON MICROSCOPY	r_gen_planes_refined	0.01	0.02	23038
ELECTRON MICROSCOPY	r_gen_planes_other
ELECTRON MICROSCOPY	r_nbd_refined
ELECTRON MICROSCOPY	r_nbd_other
ELECTRON MICROSCOPY	r_nbtor_refined
ELECTRON MICROSCOPY	r_nbtor_other
ELECTRON MICROSCOPY	r_xyhbond_nbd_refined
ELECTRON MICROSCOPY	r_xyhbond_nbd_other
ELECTRON MICROSCOPY	r_metal_ion_refined
ELECTRON MICROSCOPY	r_metal_ion_other
ELECTRON MICROSCOPY	r_symmetry_vdw_refined
ELECTRON MICROSCOPY	r_symmetry_vdw_other
ELECTRON MICROSCOPY	r_symmetry_hbond_refined
ELECTRON MICROSCOPY	r_symmetry_hbond_other
ELECTRON MICROSCOPY	r_symmetry_metal_ion_refined
ELECTRON MICROSCOPY	r_symmetry_metal_ion_other
ELECTRON MICROSCOPY	r_mcbond_it	19.206	21.259	22303
ELECTRON MICROSCOPY	r_mcbond_other
ELECTRON MICROSCOPY	r_mcangle_it	28.663	31.778	27835
ELECTRON MICROSCOPY	r_mcangle_other
ELECTRON MICROSCOPY	r_scbond_it	14.11	23.173	1978
ELECTRON MICROSCOPY	r_scbond_other
ELECTRON MICROSCOPY	r_scangle_it
ELECTRON MICROSCOPY	r_scangle_other
ELECTRON MICROSCOPY	r_long_range_B_refined	35.24		88366
ELECTRON MICROSCOPY	r_long_range_B_other
ELECTRON MICROSCOPY	r_rigid_bond_restr
ELECTRON MICROSCOPY	r_sphericity_free
ELECTRON MICROSCOPY	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: ELECTRON MICROSCOPY / Type: interatomic distance / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	X	5720	0.16
1	2	Z	5720	0.16
2	1	A	9520	0.04
2	2	B	9520	0.04
3	1	A	9540	0.04
3	2	C	9540	0.04
4	1	A	9516	0.04
4	2	D	9516	0.04
5	1	A	9490	0.04
5	2	E	9490	0.04
6	1	A	9498	0.05
6	2	F	9498	0.05
7	1	A	9470	0.04
7	2	G	9470	0.04
8	1	A	9536	0.04
8	2	H	9536	0.04
9	1	A	9506	0.04
9	2	I	9506	0.04
10	1	A	9482	0.04
10	2	J	9482	0.04
11	1	A	9524	0.04
11	2	K	9524	0.04
12	1	A	9524	0.04
12	2	L	9524	0.04
13	1	A	9526	0.03
13	2	M	9526	0.03
14	1	A	9498	0.04
14	2	N	9498	0.04
15	1	A	9464	0.04
15	2	O	9464	0.04
16	1	B	10468	0.04
16	2	C	10468	0.04
17	1	B	10482	0.03
17	2	D	10482	0.03
18	1	B	10454	0.04
18	2	E	10454	0.04
19	1	B	10428	0.04
19	2	F	10428	0.04
20	1	B	10272	0.05
20	2	G	10272	0.05
21	1	B	10490	0.04
21	2	H	10490	0.04
22	1	B	10508	0.03
22	2	I	10508	0.03
23	1	B	10430	0.05
23	2	J	10430	0.05
24	1	B	10510	0.04
24	2	K	10510	0.04
25	1	B	10494	0.04
25	2	L	10494	0.04
26	1	B	10524	0.03
26	2	M	10524	0.03
27	1	B	10468	0.04
27	2	N	10468	0.04
28	1	B	10358	0.05
28	2	O	10358	0.05
29	1	C	10542	0.04
29	2	D	10542	0.04
30	1	C	10488	0.05
30	2	E	10488	0.05
31	1	C	10476	0.04
31	2	F	10476	0.04
32	1	C	10334	0.04
32	2	G	10334	0.04
33	1	C	10512	0.05
33	2	H	10512	0.05
34	1	C	10520	0.04
34	2	I	10520	0.04
35	1	C	10478	0.05
35	2	J	10478	0.05
36	1	C	10530	0.04
36	2	K	10530	0.04
37	1	C	10494	0.05
37	2	L	10494	0.05
38	1	C	10486	0.03
38	2	M	10486	0.03
39	1	C	10504	0.05
39	2	N	10504	0.05
40	1	C	10360	0.04
40	2	O	10360	0.04
41	1	D	10518	0.04
41	2	E	10518	0.04
42	1	D	10488	0.04
42	2	F	10488	0.04
43	1	D	10318	0.04
43	2	G	10318	0.04
44	1	D	10530	0.04
44	2	H	10530	0.04
45	1	D	10530	0.04
45	2	I	10530	0.04
46	1	D	10488	0.05
46	2	J	10488	0.05
47	1	D	10554	0.04
47	2	K	10554	0.04
48	1	D	10520	0.04
48	2	L	10520	0.04
49	1	D	10506	0.03
49	2	M	10506	0.03
50	1	D	10518	0.04
50	2	N	10518	0.04
51	1	D	10368	0.05
51	2	O	10368	0.05
52	1	E	10696	0.05
52	2	F	10696	0.05
53	1	E	10330	0.04
53	2	G	10330	0.04
54	1	E	10678	0.04
54	2	H	10678	0.04
55	1	E	10752	0.03
55	2	I	10752	0.03
56	1	E	10704	0.06
56	2	J	10704	0.06
57	1	E	10770	0.04
57	2	K	10770	0.04
58	1	E	10600	0.04
58	2	L	10600	0.04
59	1	E	10470	0.04
59	2	M	10470	0.04
60	1	E	10552	0.04
60	2	N	10552	0.04
61	1	E	10348	0.04
61	2	O	10348	0.04
62	1	F	10334	0.05
62	2	G	10334	0.05
63	1	F	10652	0.05
63	2	H	10652	0.05
64	1	F	10760	0.06
64	2	I	10760	0.06
65	1	F	10734	0.06
65	2	J	10734	0.06
66	1	F	10728	0.06
66	2	K	10728	0.06
67	1	F	10562	0.05
67	2	L	10562	0.05
68	1	F	10446	0.04
68	2	M	10446	0.04
69	1	F	10512	0.05
69	2	N	10512	0.05
70	1	F	10350	0.05
70	2	O	10350	0.05
71	1	G	10330	0.04
71	2	H	10330	0.04
72	1	G	10336	0.03
72	2	I	10336	0.03
73	1	G	10294	0.05
73	2	J	10294	0.05
74	1	G	10358	0.04
74	2	K	10358	0.04
75	1	G	10338	0.04
75	2	L	10338	0.04
76	1	G	10288	0.04
76	2	M	10288	0.04
77	1	G	10360	0.04
77	2	N	10360	0.04
78	1	G	10230	0.04
78	2	O	10230	0.04
79	1	H	10724	0.04
79	2	I	10724	0.04
80	1	H	10682	0.06
80	2	J	10682	0.06
81	1	H	10752	0.04
81	2	K	10752	0.04
82	1	H	10646	0.03
82	2	L	10646	0.03
83	1	H	10498	0.04
83	2	M	10498	0.04
84	1	H	10554	0.03
84	2	N	10554	0.03
85	1	H	10386	0.04
85	2	O	10386	0.04
86	1	I	10792	0.06
86	2	J	10792	0.06
87	1	I	10826	0.03
87	2	K	10826	0.03
88	1	I	10628	0.03
88	2	L	10628	0.03
89	1	I	10502	0.03
89	2	M	10502	0.03
90	1	I	10560	0.03
90	2	N	10560	0.03
91	1	I	10362	0.03
91	2	O	10362	0.03
92	1	J	10862	0.06
92	2	K	10862	0.06
93	1	J	10520	0.06
93	2	L	10520	0.06
94	1	J	10440	0.04
94	2	M	10440	0.04
95	1	J	10490	0.06
95	2	N	10490	0.06
96	1	J	10320	0.05
96	2	O	10320	0.05
97	1	K	10618	0.03
97	2	L	10618	0.03
98	1	K	10524	0.03
98	2	M	10524	0.03
99	1	K	10588	0.03
99	2	N	10588	0.03
100	1	K	10382	0.03
100	2	O	10382	0.03
101	1	L	10522	0.03
101	2	M	10522	0.03
102	1	L	10550	0.03
102	2	N	10550	0.03
103	1	L	10388	0.03
103	2	O	10388	0.03
104	1	M	10492	0.04
104	2	N	10492	0.04
105	1	M	10374	0.04
105	2	O	10374	0.04
106	1	N	10398	0.04
106	2	O	10398	0.04

LS refinement shell

Resolution: 4.3→4.412 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0	0	-
R_work	0.576	11513	-
obs	-	-	100 %

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