BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	61.7 % (475 of 770)	58.4 % (236 of 404)	59.3 % (178 of 300)	92.4 % (61 of 66)
Backbone	96.0 % (363 of 378)	98.5 % (132 of 134)	93.4 % (171 of 183)	98.4 % (60 of 61)
Sidechain	35.6 % (159 of 447)	38.5 % (104 of 270)	31.4 % (54 of 172)	20.0 % (1 of 5)
Aromatic	6.0 % (5 of 84)	4.8 % (2 of 42)	7.3 % (3 of 41)	0.0 % (0 of 1)
Methyl	9.1 % (6 of 66)	9.1 % (3 of 33)	9.1 % (3 of 33)

1. entity

LDRWYLGGSP KGDVDPFYYD YETVRNGGLI FAGLAFIVGL LILLSRRFRS GGNKKRRQIN EDEP

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.21 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.21 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.07 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.28 ppm, Outliers: 1 Detail

Protein Blocks Logo

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

Release date

2014-05-11

Citation

Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: implications for membrane-water interfacial arginines
Gong, X., Marassi, F.
Biochim. Biophys. Acta (2015), 1848, 299-306, PubMed 24794573 , DOI 10.1016/j.bbamem.2014.04.021 , Abstract

Related entities 1. NA,K-ATPASE REGULATORY PROTEIN FXYD2b, : 1 : 5 : 60 entities Detail

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

2 3D HNCA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

3 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

4 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

5 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

6 3D H(CCO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

7 2D 1H-1H TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

8 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

9 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State anisotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

10 3D 1H-13C NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 5

#	Name	Isotope labeling	Concentration
1	FXYD2b	[U-99% 13C; U-99% 15N]	0.2 mM
2	SDS micelles	natural abundance	500 mM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_19797_2mkv.nef
Input source #2: Coordindates	2mkv.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----
LDRWYLGGSPKGDVDPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRSGGNKKRRQINEDEP
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LDRWYLGGSPKGDVDPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRSGGNKKRRQINEDEP

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	64	0	0	100.0

Content subtype: combined_19797_2mkv.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	454		98.4 (chain: A, length: 64)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	38 (1)	hbond	35.9 (chain: A, length: 64)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	76 (76)	.	68.8 (chain: A, length: 64)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_3	OK	60 (60)	.	93.8 (chain: A, length: 64)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 64, Sequence coverage: 98.4%
- Total number of assignments
  - ¹H chemical shifts: 225
  - ¹³C chemical shifts: 169
  - ¹⁵N chemical shifts: 60
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- 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	404	225	55.7
¹³C chemical shifts	300	169	56.3
¹⁵N chemical shifts	73	60	82.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	134	132	98.5
¹³C chemical shifts	128	123	96.1
¹⁵N chemical shifts	61	60	98.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	270	93	34.4
¹³C chemical shifts	172	46	26.7
¹⁵N chemical shifts	12	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	33	2	6.1
¹³C chemical shifts	33	2	6.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	42	0	0.0
¹³C chemical shifts	41	0	0.0
¹⁵N chemical shifts	1	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: hbond
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 64, Sequence coverage: 35.9%
- Total number of restraints: 38
- Weight of restraints: 1.0 (38)
- Potential type of restraints: square-well-parabolic (38)
- Range of distance target values: 2.0, 3.0 (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_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 64, Sequence coverage: 68.8%
- Total number of restraints: 76
- Total number of restraints per polymer type: 76
- Weight of restraints: 1.0 (76)
- Potential type of restraints: square-well-parabolic (76)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 64, Sequence coverage: 93.8%
- Total number of restraints: 60
- Potential type of restraints: undefined (60)
- Range of observed RDC values: 100.0, -100.0 (Hz)
- RDC restraints per residue
  - Chain_ID: A
    None

Keywords FXYD, FXYD2b, micelle, Na, K-ATPase

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Found 1 Document (0.581 seconds)

BMRB: 19797

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. NA,K-ATPASE REGULATORY PROTEIN FXYD2b, : 1 : 5 : 60 entities Detail

Experiments performed 10 experiments Detail

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NMR combined restraints 5 contents Detail