BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	71.5 % (176 of 246)	88.8 % (111 of 125)	59.8 % (58 of 97)	29.2 % (7 of 24)
Backbone	64.5 % (89 of 138)	98.0 % (48 of 49)	51.5 % (34 of 66)	30.4 % (7 of 23)
Sidechain	81.3 % (104 of 128)	82.9 % (63 of 76)	80.4 % (41 of 51)	0.0 % (0 of 1)
Aromatic	25.0 % (1 of 4)	50.0 % (1 of 2)	0.0 % (0 of 2)
Methyl	97.2 % (35 of 36)	100.0 % (18 of 18)	94.4 % (17 of 18)

1. entity 1

GVVDILKGAA KDIAGHLASK VMNX

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Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303.15 K, pH 4, Details 2 mM Ocellatin-LB2, 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-LB2	natural abundance	2 mM
4	SDS	d-25	400 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 5UA7, 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_30218_5ua7.nef
Input source #2: Coordindates	5ua7.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_30218_5ua7.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	173		95.8 (chain: A, length: 24)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	549 (1)	noe	95.8 (chain: A, length: 24)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	28 (28)	.	87.5 (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: 56
  - ¹⁵N chemical shifts: 6
- 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	56	57.7
¹⁵N chemical shifts	25	6	24.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	48	98.0
¹³C chemical shifts	46	15	32.6
¹⁵N chemical shifts	24	6	25.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	78	63	80.8
¹³C chemical shifts	51	41	80.4
¹⁵N chemical shifts	1	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	18	94.7
¹³C chemical shifts	19	17	89.5

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: 549
- Weight of restraints: 1.0 (549)
- Potential type of restraints: square-well-parabolic (549)
- 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: 87.5%
- Total number of restraints: 28
- Total number of restraints per polymer type: 28
- Weight of restraints: 1.0 (28)
- Potential type of restraints: square-well-parabolic (28)
- 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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Sample

Experiments performed 4 experiments Detail

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NMR combined restraints 4 contents Detail