BMRBj - BMREntryMaster

	Total	¹H	¹³C
All	85.8 % (362 of 422)	92.0 % (230 of 250)	76.7 % (132 of 172)
Backbone	77.9 % (155 of 199)	95.1 % (77 of 81)	66.1 % (78 of 118)
Sidechain	93.5 % (244 of 261)	90.5 % (153 of 169)	98.9 % (91 of 92)
Methyl	100.0 % (46 of 46)	100.0 % (23 of 23)	100.0 % (23 of 23)

1. entity

ASRAALIEEG QRIAEMLKSK IQGLLQQASK QAQDIQPAMQ

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 298 (±0.1) K, pH 5

#	Name	Isotope labeling	Concentration
1	H2O	natural abundance	40 v/v
2	D2O	[U-100% 2H]	10 v/v
3	TFE	[U-100% 2H]	50 v/v
4	DSS	natural abundance	0.2 uM
5	NS4B	natural abundance	1.2 mM

Protein Blocks Logo

Calculated from 37 models in PDB: 2LVG, Strand ID: A Detail

Release date

2013-06-16

Citation

Aminoterminal amphipathic α-helix AH1 of hepatitis C virus nonstructural protein 4B possesses a dual role in RNA replication and virus production
Montserret, R., Penin, F.
PLoS Pathog. (2014), 10, e1004501-e1004501, PubMed 25392992 , DOI 10.1371/journal.ppat.1004501 , Abstract

Related entities 1. NS4B, : 1 : 1 : 2 : 56 entities Detail

Interaction partners 1. NS4B, : 65 interactors Detail

More details for 65 interactors identified by 28 citations

Experiments performed 3 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_18568_2lvg.nef
Input source #2: Coordindates	2lvg.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
ASRAALIEEGQRIAEMLKSKIQGLLQQASKQAQDIQPAMQ
||||||||||||||||||||||||||||||||||||||||
ASRAALIEEGQRIAEMLKSKIQGLLQQASKQAQDIQPAMQ

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	40	0	0	100.0

Content subtype: combined_18568_2lvg.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	375		100.0 (chain: A, length: 40)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	216 (1)	noe	100.0 (chain: A, length: 40)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	68 (68)	.	100.0 (chain: A, length: 40)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 40, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 243
  - ¹³C chemical shifts: 132
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
18	LYS	HZ1	7.599
18	LYS	HZ2	7.599
18	LYS	HZ3	7.599
20	LYS	HZ1	7.621
20	LYS	HZ2	7.621
20	LYS	HZ3	7.621
30	LYS	HZ1	7.619
30	LYS	HZ2	7.619
30	LYS	HZ3	7.619

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	250	234	93.6
¹³C chemical shifts	172	132	76.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	81	79	97.5
¹³C chemical shifts	80	40	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	169	155	91.7
¹³C chemical shifts	92	92	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	25	25	100.0
¹³C chemical shifts	25	25	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: 40, Sequence coverage: 100.0%
- Total number of restraints: 216
- Weight of restraints: 1.0 (216)
- Potential type of restraints: square-well-parabolic (216)
- Range of distance target values: 2.45, 4.15 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 40, Sequence coverage: 100.0%
- Total number of restraints: 68
- Total number of restraints per polymer type: 68
- Weight of restraints: 1.0 (68)
- Potential type of restraints: square-well-parabolic (68)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords membrane protein

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 (1.551 seconds)

BMRB: 18568

Sample

Related entities 1. NS4B, : 1 : 1 : 2 : 56 entities Detail

Interaction partners 1. NS4B, : 65 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail