BMRBj - BMREntryMaster

	Total	¹H	¹³C
All	82.9 % (223 of 269)	93.3 % (139 of 149)	70.0 % (84 of 120)
Backbone	71.6 % (96 of 134)	91.1 % (51 of 56)	57.7 % (45 of 78)
Sidechain	94.3 % (150 of 159)	94.6 % (88 of 93)	93.9 % (62 of 66)
Aromatic	100.0 % (22 of 22)	100.0 % (11 of 11)	100.0 % (11 of 11)
Methyl	84.2 % (32 of 38)	84.2 % (16 of 19)	84.2 % (16 of 19)

1. NS2(1-27)

MDREMAASAG GAVFVGLVLL TLSPHYK

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 298 K, Details mixture of 50% Trifluoro Ethanol D2OH and 50% H2O (v/v).

#	Name	Isotope labeling	Concentration
1	NS2(1-27)	natural abundance	0.9 (±0.1) mM
2	Trifluoro ethanol D2OH	[U-100% 2H]	50 % v/v
3	H2O		90 % v/v

Protein Blocks Logo

Calculated from 40 models in PDB: 2JY0, Strand ID: A Detail

Release date

2008-06-03

Citation

Structural and functional characterization of nonstructural protein 2 for its role in hepatitis C virus assembly
Jirasko, V., Montserret, R., Appel, N., Janvier, A., Eustachi, L., Brohm, C., Steinmann, E., Pietschmann, T., Penin, F., Bartenschlager, R.
J. Biol. Chem. (2008), 283, 28546-28562, PubMed 18644781 , DOI 10.1074/jbc.M803981200 , Abstract

Related entities 1. NS2, : 1 : 1 : 15 entities Detail

Interaction partners 1. NS2, : 6 interactors Detail

More details for 6 interactors identified by 5 citations

Experiments performed 6 experiments Detail

1 2D 1H-1H NOESY

Instrument

Varian UnityPlus - 500 MHz

Sample

State isotropic, Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 298 K, Details mixture of 50% Trifluoro Ethanol D2OH and 50% H2O (v/v).

#	Name	Isotope labeling	Concentration
1	NS2(1-27)	natural abundance	0.9 (±0.1) mM
2	Trifluoro ethanol D2OH	[U-100% 2H]	50 % v/v
3	H2O		90 % v/v

2 2D 1H-1H TOCSY

Instrument

Varian UnityPlus - 500 MHz

Sample

State isotropic, Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 298 K, Details mixture of 50% Trifluoro Ethanol D2OH and 50% H2O (v/v).

#	Name	Isotope labeling	Concentration
1	NS2(1-27)	natural abundance	0.9 (±0.1) mM
2	Trifluoro ethanol D2OH	[U-100% 2H]	50 % v/v
3	H2O		90 % v/v

3 2D 1H-13C HSQC

Instrument

Varian UnityPlus - 500 MHz

Sample

State isotropic, Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 298 K, Details mixture of 50% Trifluoro Ethanol D2OH and 50% H2O (v/v).

#	Name	Isotope labeling	Concentration
1	NS2(1-27)	natural abundance	0.9 (±0.1) mM
2	Trifluoro ethanol D2OH	[U-100% 2H]	50 % v/v
3	H2O		90 % v/v

4 2D 1H-1H NOESY

Instrument

Varian UnityPlus - 500 MHz

Sample

State isotropic, Solvent system trifluoroethanol/water, Temperature 308 K, Details mixture of 50% Trifluoro Ethanol D2OH and 50% H2O (v/v).

#	Name	Isotope labeling	Concentration
1	NS2(1-27)	natural abundance	0.9 (±0.1) mM
2	Trifluoro ethanol D2OH	[U-100% 2H]	50 % v/v
3	H2O		90 % v/v

5 2D 1H-1H TOCSY

Instrument

Varian UnityPlus - 500 MHz

Sample

State isotropic, Solvent system trifluoroethanol/water, Temperature 308 K, Details mixture of 50% Trifluoro Ethanol D2OH and 50% H2O (v/v).

#	Name	Isotope labeling	Concentration
1	NS2(1-27)	natural abundance	0.9 (±0.1) mM
2	Trifluoro ethanol D2OH	[U-100% 2H]	50 % v/v
3	H2O		90 % v/v

6 2D 1H-13C HSQC

Instrument

Varian UnityPlus - 500 MHz

Sample

State isotropic, Solvent system trifluoroethanol/water, Temperature 308 K, Details mixture of 50% Trifluoro Ethanol D2OH and 50% H2O (v/v).

#	Name	Isotope labeling	Concentration
1	NS2(1-27)	natural abundance	0.9 (±0.1) mM
2	Trifluoro ethanol D2OH	[U-100% 2H]	50 % v/v
3	H2O		90 % v/v

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_15579_2jy0.nef
Input source #2: Coordindates	2jy0.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-------
MDREMAASAGGAVFVGLVLLTLSPHYK
|||||||||||||||||||||||||||
MDREMAASAGGAVFVGLVLLTLSPHYK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	27	0	0	100.0

Content subtype: combined_15579_2jy0.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	230		100.0 (chain: A, length: 27)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	181 (1)	noe	100.0 (chain: A, length: 27)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 147
  - ¹³C chemical shifts: 83
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	149	147	98.7
¹³C chemical shifts	120	83	69.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	56	55	98.2
¹³C chemical shifts	54	22	40.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	93	92	98.9
¹³C chemical shifts	66	61	92.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	21	20	95.2
¹³C chemical shifts	21	16	76.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	11	100.0
¹³C chemical shifts	11	11	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 100.0%
- Total number of restraints: 181
- Weight of restraints: 1.0 (181)
- Potential type of restraints: square-well-parabolic (181)
- Range of distance target values: 2.45, 5.15 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords HCV NS2 protein, membrane segment, NMR structure

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.565 seconds)

BMRB: 15579

Sample

Related entities 1. NS2, : 1 : 1 : 15 entities Detail

Interaction partners 1. NS2, : 6 interactors Detail

Experiments performed 6 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail