BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	76.8 % (255 of 332)	76.4 % (133 of 174)	74.2 % (98 of 132)	92.3 % (24 of 26)
Backbone	77.6 % (121 of 156)	85.5 % (47 of 55)	66.7 % (50 of 75)	92.3 % (24 of 26)
Sidechain	78.9 % (157 of 199)	72.3 % (86 of 119)	88.7 % (71 of 80)
Aromatic	52.6 % (20 of 38)	52.6 % (10 of 19)	52.6 % (10 of 19)
Methyl	100.0 % (30 of 30)	100.0 % (15 of 15)	100.0 % (15 of 15)

1. Molecule 1

MKFYTIKLAK FLGGIVRAML GSFRKD

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6, Details 13C,15N SpoVM P9A in 16 mM phosphate (pH6.), 80 mM NaCl, 16% deuterated DMPC/DHPC bicelles (q=0.3)

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

Protein Blocks Logo

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

Release date

2015-03-29

Citation

Structural and mechanistic basis for the geometric-driven subcellular localization of a small protein
Tian, F., Gill, R.L., Castaining, J., Hsin, J., Tan, I.S., Wang, X., Huang, K., Ramamurthi, K.
Nat. Struct. Biol.

Related entities 1. SpoVM P9A mutant, : 1 : 2 : 3 entities Detail

Experiments performed 9 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6, Details 13C,15N SpoVM P9A in 16 mM phosphate (pH6.), 80 mM NaCl, 16% deuterated DMPC/DHPC bicelles (q=0.3)

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 850 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

3 3D HNCA

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

4 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

5 3D HN(CO)CA

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

6 3D 1H-15N NOESY

Instrument

Bruker Avance - 850 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

7 3D 1H-13C NOESY

Instrument

Bruker Avance - 850 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

8 3D HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

9 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Molecule_1	[U-100% 13C; U-100% 15N]	0.5 ~ 1.0 mM
2	sodium phosphate	natural abundance	16 mM
3	sodium chloride	natural abundance	80 mM
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25270_2mvj.nef
Input source #2: Coordindates	2mvj.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	Error

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------
MKFYTIKLAKFLGGIVRAMLGSFRKD
||||||||||||||||||||||||||
MKFYTIKLAKFLGGIVRAMLGSFRKD

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	26	0	0	100.0

Content subtype: combined_25270_2mvj.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list	Warning	263		100.0 (chain: A, length: 26)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	32 (32)	.	76.9 (chain: A, length: 26)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 142
  - ¹³C chemical shifts: 97
  - ¹⁵N chemical shifts: 24
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	174	142	81.6
¹³C chemical shifts	132	97	73.5
¹⁵N chemical shifts	28	24	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	51	92.7
¹³C chemical shifts	52	26	50.0
¹⁵N chemical shifts	26	24	92.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	119	91	76.5
¹³C chemical shifts	80	71	88.7
¹⁵N chemical shifts	2	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	17	100.0
¹³C chemical shifts	17	17	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	10	52.6
¹³C chemical shifts	19	10	52.6

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 76.9%
- Total number of restraints: 32
- Total number of restraints per polymer type: 32
- Weight of restraints: 1.0 (32)
- Potential type of restraints: square-well-parabolic (32)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords membrane protein, membrane curvature

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Found 1 Document (0.423 seconds)

BMRB: 25270

Sample

Related entities 1. SpoVM P9A mutant, : 1 : 2 : 3 entities Detail

Experiments performed 9 experiments Detail

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NMR combined restraints 4 contents Detail