BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	85.8 % (211 of 246)	92.8 % (116 of 125)	74.2 % (72 of 97)	95.8 % (23 of 24)
Backbone	82.6 % (114 of 138)	98.0 % (48 of 49)	66.7 % (44 of 66)	95.7 % (22 of 23)
Sidechain	91.4 % (117 of 128)	89.5 % (68 of 76)	94.1 % (48 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 trifluoroethanol/water, Pressure 1 atm, Temperature 293.15 K, pH 7, Details 2.0 mM Ocellatin-LB1, 1 mM DSS, 20 mM potassium phosphate, 60 % d2 TFE, 40 % H2O, trifluoroethanol/water.

#	Name	Isotope labeling	Concentration
1	DSS	natural abundance	1 mM
2	H2O	natural abundance	40 %
3	Ocellatin-LB1	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: 5U9R, 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_30212_5u9r.nef
Input source #2: Coordindates	5u9r.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_30212_5u9r.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	209		95.8 (chain: A, length: 24)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	541 (1)	noe	91.7 (chain: A, length: 24)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	42 (42)	.	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: 116
  - ¹³C chemical shifts: 71
  - ¹⁵N chemical shifts: 22
- 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	116	91.3
¹³C chemical shifts	97	71	73.2
¹⁵N chemical shifts	25	22	88.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	48	98.0
¹³C chemical shifts	46	23	50.0
¹⁵N chemical shifts	24	21	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	78	68	87.2
¹³C chemical shifts	51	48	94.1
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: 91.7%
- Total number of restraints: 539
- Weight of restraints: 1.0 (539)
- Potential type of restraints: square-well-parabolic (539)
- 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: 42
- Total number of restraints per polymer type: 42
- Weight of restraints: 1.0 (42)
- Potential type of restraints: square-well-parabolic (42)
- 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: 30212

Sample

Experiments performed 4 experiments Detail

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NMR combined restraints 4 contents Detail