BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	78.7 % (185 of 235)	89.1 % (106 of 119)	64.9 % (61 of 94)	81.8 % (18 of 22)
Backbone	76.5 % (101 of 132)	97.9 % (46 of 47)	58.7 % (37 of 63)	81.8 % (18 of 22)
Sidechain	84.4 % (103 of 122)	83.3 % (60 of 72)	86.0 % (43 of 50)
Aromatic	25.0 % (1 of 4)	50.0 % (1 of 2)	0.0 % (0 of 2)
Methyl	91.7 % (33 of 36)	94.4 % (17 of 18)	88.9 % (16 of 18)

1. entity 1

GVVDILKGAA KDIAGHLASK VMX

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Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303.15 K, pH 4, Details 2 mM Ocellatin-LB1, 1 mM DSS, 400 mM d-25 SDS, 5 % 99.75 D2O, 95% H2O/5% D2O.

#	Name	Isotope labeling	Concentration
1	D2O	[U-99.75 2H]	5 %
2	DSS	natural abundance	1 mM
3	Ocellatin-LB1	natural abundance	2 mM
4	SDS	d-25	400 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 5UA6, Strand ID: A Detail

Release date

2017-03-21

Citation

NMR structures in different membrane environments of three ocellatin peptides isolated from Leptodactylus labyrinthicus
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.
Peptides (2018), 103, 72-83, PubMed 29596881 , DOI 10.1016/j.peptides.2018.03.016 , 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_30217_5ua6.nef
Input source #2: Coordindates	5ua6.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)
1:22:MET:C	1:23:NH2:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	23	NH2	AMINO GROUP	Coordinates

Sequence alignments

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

--------10--------20---
GVVDILKGAAKDIAGHLASKVMX
|||||||||||||||||||||||
GVVDILKGAAKDIAGHLASKVMX

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	23	0	0	100.0

Content subtype: combined_30217_5ua6.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	183		95.7 (chain: A, length: 23)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	486 (1)	noe	95.7 (chain: A, length: 23)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	40 (40)	.	95.7 (chain: A, length: 23)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 23, Sequence coverage: 95.7%
- Total number of assignments
  - ¹H chemical shifts: 106
  - ¹³C chemical shifts: 59
  - ¹⁵N chemical shifts: 18
- 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	121	106	87.6
¹³C chemical shifts	94	59	62.8
¹⁵N chemical shifts	23	18	78.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	46	97.9
¹³C chemical shifts	44	16	36.4
¹⁵N chemical shifts	23	18	78.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	74	60	81.1
¹³C chemical shifts	50	43	86.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	17	89.5
¹³C chemical shifts	19	16	84.2

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: 23, Sequence coverage: 95.7%
- Total number of restraints: 486
- Weight of restraints: 1.0 (486)
- Potential type of restraints: square-well-parabolic (486)
- Range of distance target values: 2.3, 4.5 (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: 23, Sequence coverage: 95.7%
- 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, AMPHIPATHIC CHARACTER, ANTIMICROBIAL PEPTIDE, ANTIMICROBIAL PROTEIN, C-TERMINAL CARBOXYAMIDATION, OCELLATIN

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BMRB: 30217

Sample

Experiments performed 4 experiments Detail

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NMR combined restraints 4 contents Detail