BMRBj - BMREntryMaster

Found 1 Document (0.455 seconds)

BMRB: 30620

6PIO

NMR Solution structure of cyclic tachyplesin II

Authors

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

Assembly

Tachyplesin-2

Entity

1. Tachyplesin-2 (polymer, Thiol state: all disulfide bound), 18 monomers, 2325.810 Da Detail

RWCFRVCYRG ICYRKCRG

Formula weight

2325.81 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 tridentatus

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 73.6 %, Completeness (bb): 72.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	73.6 % (170 of 231)	91.1 % (113 of 124)	50.0 % (44 of 88)	68.4 % (13 of 19)
Backbone	72.2 % (78 of 108)	94.7 % (36 of 38)	55.8 % (29 of 52)	72.2 % (13 of 18)
Sidechain	77.7 % (108 of 139)	89.5 % (77 of 86)	59.6 % (31 of 52)	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

RWCFRVCYRG 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 II, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	cyclic tachyplesin II	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 II, 100% D2O

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

Protein Blocks Logo

Calculated from 20 models in PDB: 6PIO, 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

Entries sharing articles BMRB: 4 entries Detail

  BMRB: 30617 released on 2019-08-01
    Title NMR Solution structure of native tachyplesin II peptide
  BMRB: 30619 released on 2019-08-01
    Title NMR Solution structure of cyclic tachyplesin I
  BMRB: 30621 released on 2019-08-01
    Title NMR Solution structure of cyclic tachyplesin III
  BMRB: 30618 released on 2019-07-17
    Title NMR Solution structure of native tachyplesin III peptide

Related entities 1. Tachyplesin-2, : 1 : 1 : 3 : 3 : 16 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30620_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	OK

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 55.362, CB 48.126 ppm	oxidized, CA 55.64, CB 48.233 ppm	n/a
1:7:CYS:SG	1:12:CYS:SG	oxidized, CA 55.203, CB 48.678 ppm	oxidized, CA 55.134, CB 47.751 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr30620_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	178		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: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 18, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 121
  - ¹³C chemical shifts: 44
  - ¹⁵N chemical shifts: 13
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	124	113	91.1
¹³C chemical shifts	88	44	50.0
¹⁵N chemical shifts	24	13	54.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	36	94.7
¹³C chemical shifts	36	13	36.1
¹⁵N chemical shifts	18	13	72.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	86	77	89.5
¹³C chemical shifts	52	31	59.6
¹⁵N chemical shifts	6	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

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.455 seconds)

BMRB: 30620

Sample #1

Sample #2

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. Tachyplesin-2, : 1 : 1 : 3 : 3 : 16 entities Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail