BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	77.5 % (341 of 440)	85.2 % (202 of 237)	62.1 % (105 of 169)	100.0 % (34 of 34)
Backbone	99.0 % (206 of 208)	97.3 % (71 of 73)	100.0 % (101 of 101)	100.0 % (34 of 34)
Sidechain	63.1 % (166 of 263)	79.9 % (131 of 164)	35.4 % (35 of 99)
Aromatic	46.2 % (12 of 26)	92.3 % (12 of 13)	0.0 % (0 of 13)
Methyl	50.0 % (15 of 30)	86.7 % (13 of 15)	13.3 % (2 of 15)

1. SBM

SKKEKKKGPE KTDEYLLARF KGDGVKYKAK LIGID

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details 15N-SBM

#	Name	Isotope labeling	Concentration
1	DSS	[U-2H]	50 uM
2	potassium chloride	natural abundance	40 mM
3	sodium azide	natural abundance	1 mM
4	citric	[U-99% 2H]	10 mM
5	SBM	natural abundance	1 mM

Sample #2

Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details unlabelled-SBM

#	Name	Isotope labeling	Concentration
6	DSS	[U-2H]	50 uM
7	potassium chloride	natural abundance	40 mM
8	sodium azide	natural abundance	1 mM
9	citric	[U-99% 2H]	10 mM
10	SBM	natural abundance	1 mM

Sample #3

Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details 13C,15N-SBM

#	Name	Isotope labeling	Concentration
11	DSS	[U-2H]	50 uM
12	potassium chloride	natural abundance	40 mM
13	sodium azide	natural abundance	1 mM
14	citric	[U-99% 2H]	10 mM
15	SBM	natural abundance	1 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 2LSW, Strand ID: A Detail

Release date

2012-09-16

Citation

Structure, sulfatide binding properties, and inhibition of platelet aggregation by a disabled-2 protein-derived peptide
Xiao, S., Charonko, J.J., Fu, X., Salmanzadeh, A., Davalos, R.V., Vlachos, P.P., Finkielstein, C.V., Capelluto, D.G.S.
J. Biol. Chem. (2012), 287, 37691-37702, PubMed 22977233 , DOI 10.1074/jbc.M112.385609 , Abstract

Related entities 1. SBM, : 1 : 2 : 4 : 13 entities Detail

Interaction partners 1. SBM, : 52 interactors Detail

More details for 52 interactors identified by 18 citations

Experiments performed 7 experiments Detail

1 3D HN(CA)CO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details 13C,15N-SBM

#	Name	Isotope labeling	Concentration
11	DSS	[U-2H]	50 uM
12	potassium chloride	natural abundance	40 mM
13	sodium azide	natural abundance	1 mM
14	citric	[U-99% 2H]	10 mM
15	SBM	natural abundance	1 mM

2 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details 13C,15N-SBM

#	Name	Isotope labeling	Concentration
11	DSS	[U-2H]	50 uM
12	potassium chloride	natural abundance	40 mM
13	sodium azide	natural abundance	1 mM
14	citric	[U-99% 2H]	10 mM
15	SBM	natural abundance	1 mM

3 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details 13C,15N-SBM

#	Name	Isotope labeling	Concentration
11	DSS	[U-2H]	50 uM
12	potassium chloride	natural abundance	40 mM
13	sodium azide	natural abundance	1 mM
14	citric	[U-99% 2H]	10 mM
15	SBM	natural abundance	1 mM

4 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details 13C,15N-SBM

#	Name	Isotope labeling	Concentration
11	DSS	[U-2H]	50 uM
12	potassium chloride	natural abundance	40 mM
13	sodium azide	natural abundance	1 mM
14	citric	[U-99% 2H]	10 mM
15	SBM	natural abundance	1 mM

5 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details 15N-SBM

#	Name	Isotope labeling	Concentration
1	DSS	[U-2H]	50 uM
2	potassium chloride	natural abundance	40 mM
3	sodium azide	natural abundance	1 mM
4	citric	[U-99% 2H]	10 mM
5	SBM	natural abundance	1 mM

6 2D 1H-1H TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details unlabelled-SBM

#	Name	Isotope labeling	Concentration
6	DSS	[U-2H]	50 uM
7	potassium chloride	natural abundance	40 mM
8	sodium azide	natural abundance	1 mM
9	citric	[U-99% 2H]	10 mM
10	SBM	natural abundance	1 mM

7 2D 1H-1H NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 5, Details unlabelled-SBM

#	Name	Isotope labeling	Concentration
6	DSS	[U-2H]	50 uM
7	potassium chloride	natural abundance	40 mM
8	sodium azide	natural abundance	1 mM
9	citric	[U-99% 2H]	10 mM
10	SBM	natural abundance	1 mM

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_18449_2lsw.nef
Input source #2: Coordindates	2lsw.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

-20-------30--------40--------50--------
GPLGSSKKEKKKGPEKTDEYLLARFKGDGVKYKAKLIGID
||||||||||||||||||||||||||||||||||||||||
GPLGSSKKEKKKGPEKTDEYLLARFKGDGVKYKAKLIGID
--------10--------20--------30--------40

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_18449_2lsw.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	340		87.5 (chain: A, length: 40)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	793 (1)	noe	87.5 (chain: A, length: 40)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	36 (36)	.	55.0 (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: 87.5%
- Total number of assignments
  - ¹H chemical shifts: 205
  - ¹³C chemical shifts: 101
  - ¹⁵N chemical shifts: 34
- 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	261	205	78.5
¹³C chemical shifts	187	101	54.0
¹⁵N chemical shifts	39	34	87.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	84	73	86.9
¹³C chemical shifts	80	70	87.5
¹⁵N chemical shifts	38	34	89.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	177	132	74.6
¹³C chemical shifts	107	31	29.0
¹⁵N chemical shifts	1	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	14	82.4
¹³C chemical shifts	17	2	11.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	12	92.3
¹³C chemical shifts	13	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: 40, Sequence coverage: 87.5%
- Total number of restraints: 793
- Weight of restraints: 1.0 (793)
- Potential type of restraints: square-well-parabolic (793)
- Range of distance target values: 2.25, 3.9 (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: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 40, Sequence coverage: 55.0%
- Total number of restraints: 36
- Total number of restraints per polymer type: 36
- Weight of restraints: 1.0 (36)
- Potential type of restraints: square-well-parabolic (36)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords peptide

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Link destinations for BMRB, PDB and EMDB

Found 1 Document (2.533 seconds)

BMRB: 18449

Sample #1

Sample #2

Sample #3

Related entities 1. SBM, : 1 : 2 : 4 : 13 entities Detail

Interaction partners 1. SBM, : 52 interactors Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 4 contents Detail