BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	79.7 % (509 of 639)	86.3 % (290 of 336)	83.5 % (207 of 248)	21.8 % (12 of 55)
Backbone	61.4 % (194 of 316)	62.6 % (67 of 107)	73.9 % (116 of 157)	21.2 % (11 of 52)
Sidechain	97.9 % (366 of 374)	97.4 % (223 of 229)	100.0 % (142 of 142)	33.3 % (1 of 3)
Aromatic	100.0 % (26 of 26)	100.0 % (13 of 13)	100.0 % (13 of 13)
Methyl	100.0 % (66 of 66)	100.0 % (33 of 33)	100.0 % (33 of 33)

1. entity 1

GSSSRSVIRS IIKSSKLNID HKDYLLDLLN DVKGSKDLKE FHKMLTAILA KQP

Show sample condition

Sample #1

Solvent system 93% H2O/7% D2O, Pressure 1 bar, Temperature 288.0 (±0.2) K, pH 7.4, Details 200 uM [U-13C; U-15N] PPRV_PXD, 20 mM sodium phosphate, 300 mM sodium chloride, 93% H2O/7% D2O

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

Sample #2

Solvent system 100% D2O, Pressure 1 bar, Temperature 288.0 (±0.2) K, pH 7.4, Details 200 uM [U-13C; U-15N] PPRV_PXD, 20 mM sodium phosphate, 300 mM sodium chloride, 100% D2O

#	Name	Isotope labeling	Concentration
4	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
5	sodium chloride	natural abundance	300 (±30.0) mM
6	sodium phosphate	natural abundance	20 (±2.0) mM

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 88.5 %, Completeness (bb): 79.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	88.5 % (1131 of 1278)	91.4 % (614 of 672)	91.1 % (452 of 496)	59.1 % (65 of 110)
Backbone	79.3 % (501 of 632)	79.4 % (170 of 214)	86.0 % (270 of 314)	58.7 % (61 of 104)
Sidechain	97.9 % (732 of 748)	96.9 % (444 of 458)	100.0 % (284 of 284)	66.7 % (4 of 6)
Aromatic	100.0 % (52 of 52)	100.0 % (26 of 26)	100.0 % (26 of 26)
Methyl	100.0 % (132 of 132)	100.0 % (66 of 66)	100.0 % (66 of 66)

1. entity 1

GSSSRSVIRS IIKSSKLNID HKDYLLDLLN DVKGSKDLKE FHKMLTAILA KQP

Show sample condition

Sample #1

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

Sample #2

Solvent system 100% D2O, Pressure 1 bar, Temperature 288.0 (±0.2) K, pH 7.4, Details 200 uM [U-13C; U-15N] PPRV_PXD, 20 mM sodium phosphate, 300 mM sodium chloride, 100% D2O

#	Name	Isotope labeling	Concentration
4	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
5	sodium chloride	natural abundance	300 (±30.0) mM
6	sodium phosphate	natural abundance	20 (±2.0) mM

Protein Blocks Logo

Calculated from 20 models in PDB: 5LXJ, Strand ID: A Detail

Release date

2017-10-16

Citation

Solution structure of the X domain of Peste des Petits Ruminants Virus phosphoprotein and interaction with the nucleoprotein
Pereira, N., Basbous, N., Piuzzi, M., Bontems, F., Eleouet, J., Sizun, C.

Related entities 1. Phosphoprotein, : 1 : 13 entities Detail

Experiments performed 14 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AvanceIII - 800 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 bar, Temperature 288.0 (±0.2) K, pH 7.4, Details 200 uM [U-13C; U-15N] PPRV_PXD, 20 mM sodium phosphate, 300 mM sodium chloride, 93% H2O/7% D2O

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

2 3D HNCO

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

3 3D HNCA

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

4 3D HNCACB

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

5 3D HN(COCA)CB

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

6 2D NOESY

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

7 3D HBHA(CO)NH

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

8 3D HN(CO)CA

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

9 3D 1H-15N NOESY

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

10 3D HCCH-TOCSY

Instrument

Bruker AvanceIII - 950 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 bar, Temperature 288.0 (±0.2) K, pH 7.4, Details 200 uM [U-13C; U-15N] PPRV_PXD, 20 mM sodium phosphate, 300 mM sodium chloride, 100% D2O

#	Name	Isotope labeling	Concentration
4	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
5	sodium chloride	natural abundance	300 (±30.0) mM
6	sodium phosphate	natural abundance	20 (±2.0) mM

11 2D 1H-13C HSQC aliphatic

Instrument

Bruker AvanceIII - 950 MHz

Sample

#	Name	Isotope labeling	Concentration
4	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
5	sodium chloride	natural abundance	300 (±30.0) mM
6	sodium phosphate	natural abundance	20 (±2.0) mM

12 2D 1H-13C HSQC aliphatic

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
2	sodium chloride	natural abundance	300 (±30.0) mM
3	sodium phosphate	natural abundance	20 (±2.0) mM

13 3D 1H-13C NOESY aliphatic

Instrument

Bruker AvanceIII - 950 MHz

Sample

#	Name	Isotope labeling	Concentration
4	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
5	sodium chloride	natural abundance	300 (±30.0) mM
6	sodium phosphate	natural abundance	20 (±2.0) mM

14 2D NOESY

Instrument

Bruker AvanceIII - 950 MHz

Sample

#	Name	Isotope labeling	Concentration
4	PPRV_PXD	[U-13C; U-15N]	200 (±20.0) uM
5	sodium chloride	natural abundance	300 (±30.0) mM
6	sodium phosphate	natural abundance	20 (±2.0) mM

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_34045_5lxj.nef
Input source #2: Coordindates	5lxj.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

---460-----470-------480-------490-------500---------
GSSSRSVIRSIIKSSKLNIDHKDYLLDLLNDVKGSKDLKEFHKMLTAILAKQP
|||||||||||||||||||||||||||||||||||||||||||||||||||||
GSSSRSVIRSIIKSSKLNIDHKDYLLDLLNDVKGSKDLKEFHKMLTAILAKQP
--------10--------20--------30--------40--------50---

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	53	0	0	100.0

Content subtype: combined_34045_5lxj.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	471		100.0 (chain: A, length: 53)
2	Assigned chemical shifts	assigned_chemical_shifts_2	Warning	632		100.0 (chain: A, length: 53)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	1255 (1)	noe	96.2 (chain: A, length: 53)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	90 (90)	.	96.2 (chain: A, length: 53)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 53, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 276
  - ¹³C chemical shifts: 195
- 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
Saveframe: assigned_chemical_shifts_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 53, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 334
  - ¹³C chemical shifts: 245
  - ¹⁵N chemical shifts: 53
- 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	336	276	82.1
¹³C chemical shifts	248	195	78.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	107	55	51.4
¹³C chemical shifts	106	53	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	229	221	96.5
¹³C chemical shifts	142	142	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	34	100.0
¹³C chemical shifts	34	34	100.0

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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
471	SER	HG	5.23
491	SER	HG	4.92

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	336	332	98.8
¹³C chemical shifts	248	245	98.8
¹⁵N chemical shifts	57	53	93.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	107	105	98.1
¹³C chemical shifts	106	103	97.2
¹⁵N chemical shifts	52	50	96.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	229	227	99.1
¹³C chemical shifts	142	142	100.0
¹⁵N chemical shifts	5	3	60.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	34	100.0
¹³C chemical shifts	34	34	100.0

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

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 53, Sequence coverage: 96.2%
- Total number of restraints: 1254
- Weight of restraints: 1.0 (1254)
- Potential type of restraints: upper-bound-parabolic (1254)
- Range of distance target values: 2.62, 5.5 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 53, Sequence coverage: 96.2%
- Total number of restraints: 90
- Total number of restraints per polymer type: 90
- Weight of restraints: 1.0 (90)
- Potential type of restraints: square-well-parabolic (90)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords STRUCTURE FROM CYANA 3.97, Viral protein, XD domain Nucleocapsid binding domain

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Found 1 Document (0.505 seconds)

BMRB: 34045

Sample #1

Sample #2

Sample #1

Sample #2

Related entities 1. Phosphoprotein, : 1 : 13 entities Detail

Experiments performed 14 experiments Detail

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NMR combined restraints 5 contents Detail