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Found 1 Document (0.466 seconds)

BMRB: 25769

2N6M

Structural elucidation of the frog skin-derived peptide Esculentin-1a[Esc(1-21)NH2] in Lipopolysaccharide and correlation with their function

Authors

Ghosh, A., Bhunia, A.

Assembly

frog skin-derived peptide Esculentin-1a[Esc(1-21)NH2]

Entity

1. frog skin-derived peptide Esculentin-1a[Esc(1-21)NH2] (polymer, Thiol state: not present), 21 monomers, 2185.695 Da Detail

GIFSKLAGKK IKNLLISGLK G

Formula weight

2185.695 Da

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 70.1 %, Completeness (bb): 54.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	70.1 % (96 of 137)	70.1 % (96 of 137)
Backbone	54.3 % (25 of 46)	54.3 % (25 of 46)
Sidechain	78.0 % (71 of 91)	78.0 % (71 of 91)
Aromatic	80.0 % (4 of 5)	80.0 % (4 of 5)
Methyl	80.0 % (12 of 15)	80.0 % (12 of 15)

1. entity

GIFSKLAGKK IKNLLISGLK G

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	natural abundance		1 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 2N6M, Strand ID: A Detail

Release date

2016-02-28

Citation

NMR structure and binding of esculentin-1a (1-21)NH₂ and its diastereomer to lipopolysaccharide: Correlation with biological functions
Ghosh, A., Bera, S., Shai, Y., Mangoni, M., Bhunia, A.
Biochim. Biophys. Acta (2015), 1858, 800-812, PubMed 26724203 , DOI 10.1016/j.bbamem.2015.12.027 , Abstract

Related entities 1. frog skin-derived peptide Esculentin-1a[Esc(1-21)NH2], : 1 : 1 : 3 : 8 entities Detail

Experiments performed 1 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25769_2n6m.nef
Input source #2: Coordindates	2n6m.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-
GIFSKLAGKKIKNLLISGLKG
|||||||||||||||||||||
GIFSKLAGKKIKNLLISGLKG

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	21	0	0	100.0

Content subtype: combined_25769_2n6m.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	96		100.0 (chain: A, length: 21)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	267 (1)	noe	100.0 (chain: A, length: 21)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	40 (40)	.	100.0 (chain: A, length: 21)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 96
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	137	96	70.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	46	25	54.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	91	71	78.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	15	12	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	4	80.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
- Total number of restraints: 267
- Weight of restraints: 1.0 (267)
- Potential type of restraints: upper-bound-parabolic (267)
- Range of distance target values: 3.0, 4.9 (Å)
- Histogram of 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: 21, Sequence coverage: 100.0%
- Total number of restraints: 40
- Total number of restraints per polymer type: 40
- Weight of restraints: 1.0 (40)
- Potential type of restraints: square-well-parabolic (40)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Alpha helix, Peptide

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Found 1 Document (0.466 seconds)

BMRB: 25769

Sample

Related entities 1. frog skin-derived peptide Esculentin-1a[Esc(1-21)NH2], : 1 : 1 : 3 : 8 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 4 contents Detail