BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	86.3 % (239 of 277)	93.7 % (133 of 142)	74.3 % (81 of 109)	96.2 % (25 of 26)
Backbone	84.7 % (127 of 150)	100.0 % (53 of 53)	69.4 % (50 of 72)	96.0 % (24 of 25)
Sidechain	89.9 % (134 of 149)	89.9 % (80 of 89)	89.8 % (53 of 59)	100.0 % (1 of 1)
Aromatic	25.0 % (1 of 4)	50.0 % (1 of 2)	0.0 % (0 of 2)
Methyl	100.0 % (40 of 40)	100.0 % (20 of 20)	100.0 % (20 of 20)

1. entity 1

GVVDILKGAA KDIAGHLASK VMNKLX

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Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 293.15 K, pH 7, Details 2.0 mM Ocellatin-F1, 1.0 mM DSS, 20 mM potassium phosphate, 60 % d2 TFE, 40 % H2O, trifluoroethanol/water.

#	Name	Isotope labeling	Concentration
1	DSS	natural abundance	1.0 mM
2	H2O	natural abundance	40 %
3	Ocellatin-F1	natural abundance	2.0 mM
4	TFE	[U-2H]	60 %
5	potassium phosphate	natural abundance	20 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 5U9S, Strand ID: A Detail

Release date

2017-03-21

Citation

Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions
Gusmao, K., Dos Santos, D.M., Santos, V.M., Cortes, M.E., Reis, P., Santos, V.L., Pilo-Veloso, D., Verly, R.M., de Lima, M.E., Resende, J.M.
J. Venom. Anim. Toxins Incl. Trop. Dis. (2017), 23, 4-4, PubMed 28115922 , DOI 10.1186/s40409-017-0094-y , Abstract

Related entities 1. Ocellatin-F1, : 1 entities Detail

Experiments performed 4 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30213_5u9s.nef
Input source #2: Coordindates	5u9s.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:25:LEU:C	1:26:NH2:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	26	NH2	AMINO GROUP	Coordinates

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20------
GVVDILKGAAKDIAGHLASKVMNKLX
||||||||||||||||||||||||||
GVVDILKGAAKDIAGHLASKVMNKLX

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_30213_5u9s.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	1		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	234		96.2 (chain: A, length: 26)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	588 (1)	noe	92.3 (chain: A, length: 26)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	46 (46)	.	96.2 (chain: A, length: 26)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 96.2%
- Total number of assignments
  - ¹H chemical shifts: 132
  - ¹³C chemical shifts: 78
  - 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	144	132	91.7
¹³C chemical shifts	109	78	71.6
¹⁵N chemical shifts	27	24	88.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	53	52	98.1
¹³C chemical shifts	50	25	50.0
¹⁵N chemical shifts	26	23	88.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	91	80	87.9
¹³C chemical shifts	59	53	89.8
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	21	20	95.2
¹³C chemical shifts	21	20	95.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	2	1	50.0
¹³C chemical shifts	2	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 92.3%
- Total number of restraints: 586
- Weight of restraints: 1.0 (586)
- Potential type of restraints: square-well-parabolic (586)
- Range of distance target values: 2.3, 4.2 (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: 26, Sequence coverage: 96.2%
- Total number of restraints: 46
- Total number of restraints per polymer type: 46
- Weight of restraints: 1.0 (46)
- Potential type of restraints: square-well-parabolic (46)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords ALPHA HELIX, AMPHIPATHIC CHARACTER, ANTIMICROBIAL PEPTIDE, ANTIMICROBIAL PROTEIN, C-TERMINAL CARBOXYAMIDATION, OCELLATIN

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BMRB: 30213

Sample

Related entities 1. Ocellatin-F1, : 1 entities Detail

Experiments performed 4 experiments Detail

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Instrument

Sample

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Sample

Instrument

Sample

NMR combined restraints 4 contents Detail