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Found 1 Document (0.332 seconds)

BMRB: 30621

6PIP

NMR Solution structure of cyclic tachyplesin III

Authors

Harvey, P.J., Troeira Henriques, S., Vernen, F.

Assembly

Tachyplesin-3

Entity

1. Tachyplesin-3 (polymer, Thiol state: all disulfide bound), 18 monomers, 2297.796 Da Detail

KWCFRVCYRG ICYRKCRG

Formula weight

2297.796 Da

Entity Connection

disulfide 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS3:SG	1:CYS16:SG
2	disulfide	sing	1:CYS7:SG	1:CYS12:SG

Source organism

Tachypleus gigas

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 81.5 %, Completeness (bb): 83.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	81.5 % (190 of 233)	96.8 % (121 of 125)	57.3 % (51 of 89)	94.7 % (18 of 19)
Backbone	83.3 % (90 of 108)	100.0 % (38 of 38)	65.4 % (34 of 52)	100.0 % (18 of 18)
Sidechain	82.3 % (116 of 141)	95.4 % (83 of 87)	62.3 % (33 of 53)	0.0 % (0 of 1)
Aromatic	39.5 % (15 of 38)	78.9 % (15 of 19)	0.0 % (0 of 18)	0.0 % (0 of 1)
Methyl	100.0 % (8 of 8)	100.0 % (4 of 4)	100.0 % (4 of 4)

1. entity 1

KWCFRVCYRG ICYRKCRG

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4, Details 1.0 mg/mL cyclic tachyplesin III, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	cyclic tachyplesin III	natural abundance		1.0 mg/mL

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 4, Details 1.0 mg/mL cyclic tachyplesin III, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	cyclic tachyplesin III	natural abundance		1.0 mg/mL

Protein Blocks Logo

Calculated from 20 models in PDB: 6PIP, Strand ID: A Detail

Release date

2019-08-01

Citation

Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties
Vernen, F., Harvey, P.J., Dias, S.A., Veiga, A.S., Huang, Y.H., Craik, D.J., Lawrence, N., Troeira Henriques, S.
Int. J. Mol. Sci. (2019), 20, E4184-E4184, PubMed 31455019 , DOI 10.3390/ijms20174184 , Abstract

Related entities 1. Tachyplesin-3, : 1 : 4 : 2 : 17 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30621_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:3:CYS:SG	1:16:CYS:SG	oxidized, CA 55.4, CB 48.04 ppm	oxidized, CA 55.617, CB 48.268 ppm	n/a
1:7:CYS:SG	1:12:CYS:SG	oxidized, CA 55.2, CB 48.677 ppm	oxidized, CA 55.133, CB 47.761 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr30621_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	204		100.0 (chain: 1, length: 18)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 18, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 135
  - ¹³C chemical shifts: 51
  - ¹⁵N chemical shifts: 18
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
1	LYS	HZ1	7.345
1	LYS	HZ2	7.345
1	LYS	HZ3	7.345
15	LYS	HZ1	7.464
15	LYS	HZ2	7.464
15	LYS	HZ3	7.464

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	125	121	96.8
¹³C chemical shifts	89	51	57.3
¹⁵N chemical shifts	23	18	78.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	38	100.0
¹³C chemical shifts	36	18	50.0
¹⁵N chemical shifts	18	18	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	87	83	95.4
¹³C chemical shifts	53	33	62.3
¹⁵N chemical shifts	5	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	4	4	100.0
¹³C chemical shifts	4	4	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	15	78.9
¹³C chemical shifts	18	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords ANTIMICROBIAL PROTEIN, cyclic peptide, defense peptide

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Found 1 Document (0.332 seconds)

BMRB: 30621

Sample #1

Sample #2

Related entities 1. Tachyplesin-3, : 1 : 4 : 2 : 17 entities Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

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Instrument

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Chemical shift validation 3 contents Detail