BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	90.8 % (129 of 142)	98.6 % (71 of 72)	81.0 % (47 of 58)	91.7 % (11 of 12)
Backbone	81.9 % (59 of 72)	96.3 % (26 of 27)	66.7 % (22 of 33)	91.7 % (11 of 12)
Sidechain	100.0 % (79 of 79)	100.0 % (45 of 45)	100.0 % (34 of 34)
Methyl	100.0 % (30 of 30)	100.0 % (15 of 15)	100.0 % (15 of 15)

1. entity 1

ILGTILGLLK GLX

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Sample

Solvent system 70% H20/30% TFE, Pressure 1 atm, Temperature 298 K, pH 4.2, Details 1 mM peptide, 70% H20/30% TFE

#	Name	Isotope labeling	Type	Concentration
1	peptide	natural abundance		1 mM

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Calculated from 20 models in PDB: 7JGY, Strand ID: A Detail

Release date

2020-08-16

Citation

Antimicrobial and Anticancer Properties of Synthetic Peptides Derived from the Wasp Parachartergus fraternus
Muller, J., Lawrence, N., Chan, L.Y., Harvey, P.J., Elliott, A.G., Blaskovich, M., Goncalves, J.C., Galante, P., Mortari, M.R., Toffoli-Kadri, M.C., Koehbach, J., Craik, D.
Chembiochem. (2021), 22, 1415-1423, PubMed 33244888 , DOI 10.1002/cbic.202000716 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 30775 released on 2020-08-16
    Title Solution NMR structure of neuroVAL, a derived peptide from wasp
  BMRB: 30778 released on 2020-08-16
    Title Solution NMR structure of protonectin-F, a derived peptide from wasp

Related entities 1. Protonectin peptide, : 1 : 1 entities Detail

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30776_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	OK

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr30776_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	158		92.3 (chain: 1, length: 13)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 13, Sequence coverage: 92.3%
- Total number of assignments
  - ¹H chemical shifts: 101
  - ¹³C chemical shifts: 46
  - ¹⁵N chemical shifts: 11
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	74	71	95.9
¹³C chemical shifts	58	46	79.3
¹⁵N chemical shifts	13	11	84.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	27	26	96.3
¹³C chemical shifts	24	12	50.0
¹⁵N chemical shifts	13	11	84.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	45	95.7
¹³C chemical shifts	34	34	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	15	15	100.0
¹³C chemical shifts	15	15	100.0

Keywords ANTIMICROBIAL PROTEIN, alpha-helical, antimicrobial, non-haemolytic

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Found 1 Document (0.474 seconds)

BMRB: 30776

Sample

Entries sharing articles BMRB: 2 entries Detail

Related entities 1. Protonectin peptide, : 1 : 1 entities Detail

Experiments performed 4 experiments Detail

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Chemical shift validation 3 contents Detail