BMRBj - BMREntryMaster

Found 1 Document (0.297 seconds)

BMRB: 34479

6XTI

NMR solution structure of class IV lasso peptide felipeptin A2 from Amycolatopsis sp. YIM10

Authors

Madland, E., Guerrero-Garzon, J.F., Zotchev, S.B., Aachmann, F.L., Courtade, G.

Assembly

Felipeptin A2, CYS-LEU-ILE-PHE-CYS

Entity

1. Felipeptin A2, CYS-LEU-ILE-PHE-CYS (polymer, Thiol state: all disulfide bound), 17 monomers, 1865.099 Da Detail

GGGGRGYEYN KQCLIFC

Formula weight

1865.099 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS13:SG	1:CYS17:SG

Source organism

Amycolatopsis sp.

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 88.2 %, Completeness: 66.3 %, Completeness (bb): 62.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	66.3 % (128 of 193)	74.3 % (75 of 101)	56.9 % (41 of 72)	60.0 % (12 of 20)
Backbone	62.7 % (64 of 102)	79.5 % (31 of 39)	45.7 % (21 of 46)	70.6 % (12 of 17)
Sidechain	69.9 % (72 of 103)	71.0 % (44 of 62)	73.7 % (28 of 38)	0.0 % (0 of 3)
Aromatic	53.8 % (14 of 26)	53.8 % (7 of 13)	53.8 % (7 of 13)
Methyl	100.0 % (8 of 8)	100.0 % (4 of 4)	100.0 % (4 of 4)

1. entity 1

GGGGRGYEYN KQCLIFC

Show sample condition

Sample

Solvent system DMSO, Pressure 1 atm, Temperature 298 K, pH 7, Details 0.5 mM Felipeptin A2, DMSO

#	Name	Isotope labeling	Type	Concentration
1	Felipeptin A2	natural abundance		0.5 mM

Release date

2020-01-23

Citation

Class IV Lasso Peptides Synergistically Induce Proliferation of Cancer Cells and Sensitize Them to Doxorubicin
Guerrero-Garzon, J.F., Madland, E., Zehl, M., Singh, M., Rezaei, S., Aachmann, F.L., Courtade, G., Urban, E., Ruckert, C., Busche, T., Kalinowski, J., Cao, Y.R., Jiang, Y., Jiang, C.L., Selivanova, G., Zotchev, S.B.
iScience (2020), 23, 101785-101785, PubMed 33294793 , DOI 10.1016/j.isci.2020.101785 , Abstract

Related entities 1. Felipeptin A2, CYS-LEU-ILE-PHE-CYS, : 1 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34479_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)
1:13:CYS:SG	1:17:CYS:SG	unknown	unknown	n/a

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

None

Non-standard residues

None

Content subtype: bmr34479_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	144		88.2 (chain: 1, length: 17)
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: 17, Sequence coverage: 88.2%
- Total number of assignments
  - ¹H chemical shifts: 87
  - ¹³C chemical shifts: 45
  - ¹⁵N chemical shifts: 12
- 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)
7	TYR	CG	155.6
8	GLU	CD	174.5
9	TYR	CG	155.9
11	LYS	HZ1	5.35
11	LYS	HZ2	5.35
11	LYS	HZ3	5.35
16	PHE	CG	156.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	101	76	75.2
¹³C chemical shifts	72	41	56.9
¹⁵N chemical shifts	20	12	60.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	32	82.1
¹³C chemical shifts	34	13	38.2
¹⁵N chemical shifts	17	12	70.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	62	44	71.0
¹³C chemical shifts	38	28	73.7
¹⁵N chemical shifts	3	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	13	7	53.8
¹³C chemical shifts	13	7	53.8

Keywords ANTIMICROBIAL PROTEIN, antibacterial, class IV, lasso peptide

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Found 1 Document (0.297 seconds)

BMRB: 34479

Sample

Related entities 1. Felipeptin A2, CYS-LEU-ILE-PHE-CYS, : 1 entities Detail

Experiments performed 5 experiments Detail

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Chemical shift validation 3 contents Detail