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BMRB: 19854

2MMG

Structural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance

Authors

Bacot-Davis, V.R., Palmenberg, A.C., Cornilescu, C.C., Markley, J.L.

Assembly

Mengovirus Leader Protein Bound to Ran GTPase

Entity

1. Mengovirus Leader Protein Bound to Ran GTPase (polymer, Thiol state: all free), 216 monomers, 24422.78 Da Detail

MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL

Formula weight

24422.78 Da

Source organism

Exptl. method

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.5 %, Completeness: 85.9 %, Completeness (bb): 85.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	85.9 % (2213 of 2575)	82.6 % (1105 of 1337)	87.3 % (883 of 1012)	99.6 % (225 of 226)
Backbone	85.6 % (1089 of 1272)	62.2 % (270 of 434)	97.2 % (616 of 634)	99.5 % (203 of 204)
Sidechain	87.7 % (1320 of 1505)	92.5 % (835 of 903)	79.8 % (463 of 580)	100.0 % (22 of 22)
Aromatic	100.0 % (234 of 234)	100.0 % (117 of 117)	100.0 % (114 of 114)	100.0 % (3 of 3)
Methyl	96.9 % (248 of 256)	96.1 % (123 of 128)	97.7 % (125 of 128)

1. entity

MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

Protein Blocks Logo

Calculated from 10 models in PDB: 2MMG, Strand ID: A Detail

Release date

2014-10-06

Citation

Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase
Bacot-Davis, V.R., Ciomperlik, J.J., Basta, H.A., Cornilescu, C.C., Palmenberg, A.C.
Proc. Natl. Acad. Sci. U. S. A. (2014), 111, 15792-15797, PubMed 25331866 , DOI 10.1073/pnas.1411098111 , Abstract

Related entities 1. Mengovirus Leader Protein Bound to Ran GTPase, : 1 : 70 : 1 : 32 : 91 entities Detail

Interaction partners 1. Mengovirus Leader Protein Bound to Ran GTPase, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

3 3D HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

4 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

5 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

6 3D H(CCO)NH

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

7 3D HNCACB

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

8 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

9 3D 1H-13C NOESY

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

10 31-P

Instrument

Bruker Avance - 600 MHz Dexter, NMR FAM Madison, WI

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.

#	Name	Isotope labeling	Type	Concentration
1	RAN GTPASE	[U-100% 13C; U-100% 15N]		0.5 mM
2	L MENGO	natural abundance		0.5 mM
3	HEPES	natural abundance		20 mM
4	potassium chloride	natural abundance		100 mM
5	magnesium chloride	natural abundance		2 mM
6	DTT	natural abundance		2 mM
7	sodium azide	natural abundance		0.04 %
8	H2O	natural abundance		90 %
9	D2O	natural abundance		10 %

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Dihedral angle restraints	combined_19854_2mmg.nef
Input source #2: Coordindates	2mmg.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKN
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKN

-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200
VPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHD
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
VPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHD

-------210------
LEVAQTTALPDEDDDL
||||||||||||||||
LEVAQTTALPDEDDDL

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	216	0	0	100.0

Content subtype: combined_19854_2mmg.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	2377		99.5 (chain: A, length: 216)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	146 (146)	.	63.0 (chain: A, length: 216)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 216, Sequence coverage: 99.5%

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKN
|||||||||||||||||||||||||||||||||||||||| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYV.TLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKN

-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200
VPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHD
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
VPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHD

-------210------
LEVAQTTALPDEDDDL
||||||||||||||||
LEVAQTTALPDEDDDL

Total number of assignments
- ¹H chemical shifts: 1184
- ¹³C chemical shifts: 899
- ¹⁵N chemical shifts: 293

Completeness of assignments

Entity_assemble_ID: A

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
7	PRO	N	118.677
12	LYS	HZ1	7.452
12	LYS	HZ2	7.452
12	LYS	HZ3	7.452
12	LYS	NZ	49.89
21	THR	HG1	5.078
23	LYS	HZ1	7.472
23	LYS	HZ2	7.472
23	LYS	HZ3	7.472
23	LYS	NZ	53.295
24	THR	HG1	5.907
25	THR	HG1	5.389
28	LYS	HZ1	7.501
28	LYS	HZ2	7.501
28	LYS	HZ3	7.501
28	LYS	NZ	59.203
29	ARG	HH11	6.768
29	ARG	HH12	6.915
29	ARG	HH21	6.69
29	ARG	HH22	6.621
29	ARG	CZ	161.621
29	ARG	NH1	79.302
29	ARG	NH2	79.392
30	HIS	HD1	10.269
30	HIS	HE2	11.376
30	HIS	ND1	194.294
30	HIS	NE2	177.332
32	THR	HG1	6.408
34	GLU	CD	178.617
36	GLU	CD	190.449
37	LYS	HZ1	7.247
37	LYS	HZ2	7.247
37	LYS	HZ3	7.247
37	LYS	NZ	53.201
38	LYS	HZ1	7.364
38	LYS	HZ2	7.364
38	LYS	HZ3	7.364
38	LYS	NZ	52.396
39	TYR	HH	9.193
39	TYR	CZ	155.174
42	THR	HG1	5.311
48	HIS	HD1	10.435
48	HIS	HE2	11.298
48	HIS	ND1	194.229
48	HIS	NE2	178.938
49	PRO	N	123.193
53	HIS	HD1	10.367
53	HIS	HE2	11.083
53	HIS	ND1	197.322
53	HIS	NE2	177.382
54	THR	HG1	5.594
56	ARG	HH11	6.885
56	ARG	HH12	6.983
56	ARG	HH21	6.797
56	ARG	HH22	6.758
56	ARG	CZ	161.914
56	ARG	NH1	81.229
56	ARG	NH2	81.938
58	PRO	N	114.56
60	LYS	HZ1	7.971
60	LYS	HZ2	7.971
60	LYS	HZ3	7.971
60	LYS	NZ	49.993
64	TRP	CD2	128.509
64	TRP	CE2	139.058
66	THR	HG1	6.015
69	GLN	CD	178.902
71	LYS	HZ1	7.511
71	LYS	HZ2	7.511
71	LYS	HZ3	7.511
71	LYS	NZ	49.002
76	ARG	HH11	6.875
76	ARG	HH12	6.905
76	ARG	HH21	6.778
76	ARG	HH22	6.748
76	ARG	CZ	159.57
76	ARG	NH1	79.394
76	ARG	NH2	81.395
79	TYR	HH	9.203
79	TYR	CZ	154.881
80	TYR	HH	11.462
80	TYR	CZ	156.343
82	GLN	CD	170.406
84	GLN	CD	174.508
93	THR	HG1	5.563
95	ARG	HH11	6.827
95	ARG	HH12	6.934
95	ARG	HH21	6.748
95	ARG	HH22	6.719
95	ARG	CZ	158.984
95	ARG	NH1	77.294
95	ARG	NH2	77.483
97	THR	HG1	5.477
98	TYR	HH	9.193
98	TYR	CZ	154.295
99	LYS	HZ1	7.746
99	LYS	HZ2	7.746
99	LYS	HZ3	7.746
99	LYS	NZ	53.295
102	PRO	N	117.084
104	TRP	CD2	155.174
104	TRP	CE2	135.43
105	HIS	HD1	10.396
105	HIS	HE2	11.112
105	HIS	ND1	192.113
105	HIS	NE2	179.221
106	ARG	HH11	6.866
106	ARG	HH12	6.905
106	ARG	HH21	6.797
106	ARG	HH22	6.729
106	ARG	CZ	159.863
106	ARG	NH1	79.294
106	ARG	NH2	79.729
110	ARG	HH11	6.885
110	ARG	HH12	6.827
110	ARG	HH21	6.719
110	ARG	HH22	6.748
110	ARG	CZ	158.984
110	ARG	NH1	80.394
110	ARG	NH2	80.302
116	PRO	N	117.548
123	LYS	HZ1	9.279
123	LYS	HZ2	9.279
123	LYS	HZ3	9.279
123	LYS	NZ	53.492
127	LYS	HZ1	8.108
127	LYS	HZ2	8.108
127	LYS	HZ3	8.108
127	LYS	NZ	53.294
129	ARG	HH11	6.885
129	ARG	HH12	6.905
129	ARG	HH21	6.846
129	ARG	HH22	6.797
129	ARG	CZ	162.793
129	ARG	NH1	80.393
129	ARG	NH2	80.284
130	LYS	HZ1	7.668
130	LYS	HZ2	7.668
130	LYS	HZ3	7.668
130	LYS	NZ	42.394
132	LYS	HZ1	7.228
132	LYS	HZ2	7.228
132	LYS	HZ3	7.228
132	LYS	NZ	49.592
134	LYS	HZ1	7.404
134	LYS	HZ2	7.404
134	LYS	HZ3	7.404
134	LYS	NZ	49.302
139	HIS	HD1	10.476
139	HIS	HE2	12.494
139	HIS	ND1	198.229
139	HIS	NE2	183.28
140	ARG	HH11	6.619
140	ARG	HH12	6.494
140	ARG	HH21	6.856
140	ARG	HH22	6.963
140	ARG	CZ	159.82
140	ARG	NH1	84.292
140	ARG	NH2	79.393
141	LYS	HZ1	7.306
141	LYS	HZ2	7.306
141	LYS	HZ3	7.306
141	LYS	NZ	49.238
142	LYS	HZ1	7.355
142	LYS	HZ2	7.355
142	LYS	HZ3	7.355
142	LYS	NZ	49.223
146	TYR	HH	9.213
146	TYR	CZ	154.881
147	TYR	HH	9.291
147	TYR	CZ	154.588
152	LYS	HZ1	7.462
152	LYS	HZ2	7.462
152	LYS	HZ3	7.462
152	LYS	NZ	49.22
155	TYR	HH	10.484
155	TYR	CZ	165.718
159	LYS	NZ	42.592
160	PRO	N	113.099
163	TRP	CD2	128.509
163	TRP	CE2	138.472
166	ARG	HH11	6.875
166	ARG	HH12	6.915
166	ARG	HH21	6.797
166	ARG	HH22	6.748
166	ARG	CZ	159.57
166	ARG	NH1	77.392
166	ARG	NH2	77.827
167	LYS	HZ1	7.316
167	LYS	HZ2	7.316
167	LYS	HZ3	7.316
167	LYS	NZ	46.773
172	PRO	N	120.802
180	PRO	N	132.236
184	PRO	N	117.482
185	PRO	N	116.22
186	GLU	CD	198.609
191	PRO	N	121.4
196	GLN	CD	178.617
197	TYR	HH	10.191
197	TYR	CZ	160.445
199	HIS	HD1	11.47
199	HIS	HE2	12.445
199	HIS	ND1	198.293
199	HIS	NE2	183.292
205	GLN	CD	179.902
206	THR	HG1	5.956
207	THR	HG1	5.986
210	PRO	N	113.896

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1337	1065	79.7
¹³C chemical shifts	1012	868	85.8
¹⁵N chemical shifts	235	233	99.1

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	434	230	53.0
¹³C chemical shifts	432	423	97.9
¹⁵N chemical shifts	204	203	99.5

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	903	835	92.5
¹³C chemical shifts	580	445	76.7
¹⁵N chemical shifts	31	30	96.8

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	132	127	96.2
¹³C chemical shifts	132	128	97.0

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	117	117	100.0
¹³C chemical shifts	114	114	100.0
¹⁵N chemical shifts	3	3	100.0

Redox state of CYS
Peptide bond of PRO
Tautomeric state of HIS
Rotameric state of ILE , LEU, and VAL
Histogram of normalized assigned chemical shifts
Random coil index and derived parameters (S² and NMR RMSD)
- Chain_ID: A

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 216, Sequence coverage: 63.0%
- Total number of restraints: 146
- Total number of restraints per polymer type: 146
- Weight of restraints: 1.0 (146)
- Potential type of restraints: square-well-parabolic (146)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords CARDIOVIRUSES, CYTOPLASM, G-PROTEIN, GTPASE, GTP-BINDING, LEADER, NUCLEAR PORE COMPLEX, NUCLEOCYTOPLASMIC TRANSPORT, NUCLEOTIDE-BINDING, NUCLEUS, TRANSPORT, TRANSPORT PROTEIN, VIRUS-HOST INTERACTIONS