BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	81.7 % (201 of 246)	89.6 % (112 of 125)	72.2 % (70 of 97)	79.2 % (19 of 24)
Backbone	80.4 % (111 of 138)	100.0 % (49 of 49)	66.7 % (44 of 66)	78.3 % (18 of 23)
Sidechain	85.9 % (110 of 128)	82.9 % (63 of 76)	90.2 % (46 of 51)	100.0 % (1 of 1)
Aromatic	25.0 % (1 of 4)	50.0 % (1 of 2)	0.0 % (0 of 2)
Methyl	100.0 % (36 of 36)	100.0 % (18 of 18)	100.0 % (18 of 18)

1. entity 1

GVVDILKGAA KDIAGHLASK VMNX

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Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293.15 K, pH 4, Details 2.0 mM Ocellatin-LB2, 100 mM d-38 DPC, 5 % 99.75% D2O, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	D2O	[U-99.75 2H]	5 %
2	DPC	[D-38]	100 mM
3	Ocellatin-LB2	natural abundance	2.0 mM

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Calculated from 10 models in PDB: 5U9X, Strand ID: A Detail

Release date

2017-02-21

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

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_30215_5u9x.nef
Input source #2: Coordindates	5u9x.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)
1:23:ASN:C	1:24:NH2:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	24	NH2	AMINO GROUP	Coordinates

Sequence alignments

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

--------10--------20----
GVVDILKGAAKDIAGHLASKVMNX
||||||||||||||||||||||||
GVVDILKGAAKDIAGHLASKVMNX

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	24	0	0	100.0

Content subtype: combined_30215_5u9x.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	196		95.8 (chain: A, length: 24)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	510 (1)	noe	95.8 (chain: A, length: 24)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	41 (41)	.	95.8 (chain: A, length: 24)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 24, Sequence coverage: 95.8%
- Total number of assignments
  - ¹H chemical shifts: 111
  - ¹³C chemical shifts: 68
  - ¹⁵N chemical shifts: 17
- 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	127	111	87.4
¹³C chemical shifts	97	68	70.1
¹⁵N chemical shifts	25	17	68.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	48	98.0
¹³C chemical shifts	46	22	47.8
¹⁵N chemical shifts	24	16	66.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	78	63	80.8
¹³C chemical shifts	51	46	90.2
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	18	94.7
¹³C chemical shifts	19	18	94.7

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: 24, Sequence coverage: 95.8%
- Total number of restraints: 508
- Weight of restraints: 1.0 (508)
- Potential type of restraints: square-well-parabolic (508)
- Range of distance target values: 2.3, 4.7 (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: 24, Sequence coverage: 95.8%
- Total number of restraints: 41
- Total number of restraints per polymer type: 41
- Weight of restraints: 1.0 (41)
- Potential type of restraints: square-well-parabolic (41)
- 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: 30215

Sample

Experiments performed 4 experiments Detail

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NMR combined restraints 4 contents Detail