BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	79.9 % (298 of 373)	89.5 % (171 of 191)	68.9 % (104 of 151)	74.2 % (23 of 31)
Backbone	73.9 % (130 of 176)	91.7 % (55 of 60)	60.2 % (53 of 88)	78.6 % (22 of 28)
Sidechain	82.7 % (186 of 225)	85.5 % (112 of 131)	80.2 % (73 of 91)	33.3 % (1 of 3)
Aromatic	60.0 % (36 of 60)	60.0 % (18 of 30)	64.3 % (18 of 28)	0.0 % (0 of 2)
Methyl	100.0 % (42 of 42)	100.0 % (21 of 21)	100.0 % (21 of 21)

1. entity

HSVSHARPRW FWFSLLLLAA GVGIYLLPNR

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Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	entity	natural abundance	protein	1.4 (±0.05) mM
2	SDS	[U-2H]		1 M
3	H2O	natural abundance	solvent	95 %
4	D2O	[U-2H]	solvent	5 %

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Calculated from 41 models in PDB: 2N1P, Strand ID: A Detail

Release date

2016-04-17

Citation

Structure of the C-terminal membrane domain of HCV NS5B protein
Montserret, R., Penin, F.
J. Biol. Chem.

Related entities 1. ns5bc, : 1 : 3 : 39 entities Detail

Interaction partners 1. ns5bc, : 71 interactors Detail

More details for 71 interactors identified by 48 citations

Experiments performed 6 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25570_2n1p.nef
Input source #2: Coordindates	2n1p.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
HSVSHARPRWFWFSLLLLAAGVGIYLLPNR
||||||||||||||||||||||||||||||
HSVSHARPRWFWFSLLLLAAGVGIYLLPNR

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	30	0	0	100.0

Content subtype: combined_25570_2n1p.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	296		100.0 (chain: A, length: 30)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	204 (1)	noe	96.7 (chain: A, length: 30)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	31 (31)	.	63.3 (chain: A, length: 30)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 170
  - ¹³C chemical shifts: 102
  - ¹⁵N chemical shifts: 24
- 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	191	170	89.0
¹³C chemical shifts	151	102	67.5
¹⁵N chemical shifts	34	24	70.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	60	56	93.3
¹³C chemical shifts	60	28	46.7
¹⁵N chemical shifts	28	23	82.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	131	114	87.0
¹³C chemical shifts	91	74	81.3
¹⁵N chemical shifts	6	1	16.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	21	21	100.0
¹³C chemical shifts	21	21	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	30	18	60.0
¹³C chemical shifts	28	18	64.3
¹⁵N chemical shifts	2	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 96.7%
- Total number of restraints: 204
- Weight of restraints: 1.0 (204)
- Potential type of restraints: square-well-parabolic (204)
- Range of distance target values: 2.45, 5.85 (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: 30, Sequence coverage: 63.3%
- Total number of restraints: 31
- Total number of restraints per polymer type: 31
- Weight of restraints: 1.0 (31)
- Potential type of restraints: square-well-parabolic (31)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Hepatitis C virus, Membrane domain, NS5B protein

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BMRB: 25570

Sample

Related entities 1. ns5bc, : 1 : 3 : 39 entities Detail

Interaction partners 1. ns5bc, : 71 interactors Detail

Experiments performed 6 experiments Detail

Instrument

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NMR combined restraints 4 contents Detail