BMRBj - BMREntryMaster

Found 1 Document (0.299 seconds)

BMRB: 30650

6Q08

Synoeca peptide was isolated from the venom of wasp synoeca surinama.

Authors

Alves, E.S., Rodrigues, L.V., Liao, L.M.

Assembly

Synoeca peptide

Entity

1. Synoeca peptide (polymer, Thiol state: not present), 14 monomers, 1596.997 Da Detail

INWLKLGKKI IASL

Formula weight

1596.997 Da

Source organism

Synoeca surinama

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 74.9 %, Completeness (bb): 75.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	74.9 % (128 of 171)	87.8 % (86 of 98)	57.5 % (42 of 73)
Backbone	75.7 % (53 of 70)	100.0 % (29 of 29)	58.5 % (24 of 41)
Sidechain	75.4 % (86 of 114)	82.6 % (57 of 69)	64.4 % (29 of 45)
Aromatic	45.5 % (5 of 11)	66.7 % (4 of 6)	20.0 % (1 of 5)
Methyl	88.5 % (23 of 26)	100.0 % (13 of 13)	76.9 % (10 of 13)

1. entity 1

INWLKLGKKI IASL

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7, Details 1 mM synoeca, 100 mM [U-98% 2H] SDS-D25, 5 % v/v [U-98% 2H] DSS, 90 % v/v H2O, 10 % [U-99% 2H] D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	synoeca	natural abundance	1 mM
2	SDS-D25	[U-98% 2H]	100 mM
3	DSS	[U-98% 2H]	5 % v/v
4	H2O	natural abundance	90 % v/v
5	D2O	[U-99% 2H]	10 %

Release date

2019-09-30

Citation

NMR STRUCTURE OF THE ANTIMICROBIAL PEPTIDE ISOLATED FROM THE VENOM OF WASP Synoeca Surinama
Alves, E.S.F., Rodrigues, L.V., Liao, L.M.

Related entities 1. Synoeca peptide, : 1 : 4 entities Detail

Experiments performed 3 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30650_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: bmr30650_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	154		100.0 (chain: 1, length: 14)
1	Chemical shift references	chem_shift_reference_1	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 14, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 112
  - ¹³C chemical shifts: 42
- 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	98	86	87.8
¹³C chemical shifts	73	42	57.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	29	29	100.0
¹³C chemical shifts	28	13	46.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	57	82.6
¹³C chemical shifts	45	29	64.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	13	100.0
¹³C chemical shifts	13	10	76.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	4	66.7
¹³C chemical shifts	5	1	20.0

Keywords ANTIMICROBIAL PROTEIN, Antimicrobial, peptide structure

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Found 1 Document (0.299 seconds)

BMRB: 30650

Sample

Related entities 1. Synoeca peptide, : 1 : 4 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail