BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	88.3 % (151 of 171)	98.9 % (90 of 91)	73.5 % (50 of 68)	91.7 % (11 of 12)
Backbone	80.3 % (53 of 66)	95.5 % (21 of 22)	66.7 % (22 of 33)	90.9 % (10 of 11)
Sidechain	94.0 % (109 of 116)	100.0 % (69 of 69)	84.8 % (39 of 46)	100.0 % (1 of 1)
Aromatic	87.5 % (28 of 32)	100.0 % (16 of 16)	73.3 % (11 of 15)	100.0 % (1 of 1)
Methyl	100.0 % (12 of 12)	100.0 % (6 of 6)	100.0 % (6 of 6)

1. entity 1

KFKKVIWKSF L

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Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 4 (±0.1), Details 1 mM peptide 12530, 100 mM dodecylphosphocholine, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	peptide 12530	natural abundance		1 (±0.2) mM
2	dodecylphosphocholine	natural abundance		100 (±5.0) mM

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

Release date

2019-10-10

Citation

Medicinal leech antimicrobial peptides lacking toxicity represent a promising alternative strategy to combat antibiotic-resistant pathogens
Grafskaia, E.N., Nadezhdin, K.D., Talyzina, I.A., Polina, N.F., Podgorny, O.V., Pavlova, E.R., Bashkirov, P.V., Kharlampieva, D.D., Bobrovsky, P.A., Latsis, I.A., Manuvera, V.A., Babenko, V.V., Trukhan, V.M., Arseniev, A.S., Klinov, D.V., Lazarev, V.N.
Eur. J. Med. Chem. (2019), 180, 143-153, PubMed 31302447 , DOI 10.1016/j.ejmech.2019.06.080 , Abstract

Related entities 1. peptide 3967, : 1 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34406_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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr34406_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	172		100.0 (chain: 1, length: 11)
1	Chemical shift references	chem_shift_reference_1	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 11, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 111
  - ¹³C chemical shifts: 50
  - 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
3	LYS	HZ1	7.701
3	LYS	HZ2	7.701
3	LYS	HZ3	7.701
4	LYS	HZ1	7.685
4	LYS	HZ2	7.685
4	LYS	HZ3	7.685
8	LYS	HZ1	7.687
8	LYS	HZ2	7.687
8	LYS	HZ3	7.687

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	91	90	98.9
¹³C chemical shifts	68	50	73.5
¹⁵N chemical shifts	12	11	91.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	22	21	95.5
¹³C chemical shifts	22	11	50.0
¹⁵N chemical shifts	11	10	90.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	69	100.0
¹³C chemical shifts	46	39	84.8
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	6	6	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	16	16	100.0
¹³C chemical shifts	15	11	73.3
¹⁵N chemical shifts	1	1	100.0

Keywords ANTIMICROBIAL PROTEIN, Hirudo medicinalis, antimicrobial peptides, dooecylphosphocholine micelles, genome, medicinal leech, prediction algorithm

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Found 1 Document (0.34 seconds)

BMRB: 34406

Sample

Related entities 1. peptide 3967, : 1 entities Detail

Experiments performed 5 experiments Detail

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Chemical shift validation 3 contents Detail