BMRBj - BMREntryMaster

Found 1 Document (0.283 seconds)

BMRB: 34478

6XTH

NMR solution structure of class IV lasso peptide felipeptin A1 from Amycolatopsis sp. YIM10

Authors

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

Assembly

Felipeptin A1, CYS-LEU-ILE-TRP-CYS-ASP

Entity

1. Felipeptin A1, CYS-LEU-ILE-TRP-CYS-ASP (polymer, Thiol state: all disulfide bound), 18 monomers, 2038.312 Da Detail

GSRGWGFEPG VRCLIWCD

Formula weight

2038.312 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: 100.0 %, Completeness: 79.8 %, Completeness (bb): 81.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	79.8 % (166 of 208)	95.3 % (102 of 107)	57.5 % (46 of 80)	85.7 % (18 of 21)
Backbone	81.1 % (86 of 106)	100.0 % (39 of 39)	62.0 % (31 of 50)	94.1 % (16 of 17)
Sidechain	79.3 % (92 of 116)	92.6 % (63 of 68)	61.4 % (27 of 44)	50.0 % (2 of 4)
Aromatic	47.1 % (16 of 34)	82.4 % (14 of 17)	0.0 % (0 of 15)	100.0 % (2 of 2)
Methyl	100.0 % (12 of 12)	100.0 % (6 of 6)	100.0 % (6 of 6)

1. entity 1

GSRGWGFEPG VRCLIWCD

Show sample condition

Sample

Solvent system DMSO, Pressure 1 atm, Temperature 298 K, pH 7, Details 0.5 mM Felipeptin A1, DMSO

#	Name	Isotope labeling	Type	Concentration
1	Felipeptin A1	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 A1, CYS-LEU-ILE-TRP-CYS-ASP, : 1 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34478_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	oxidized, CA 54.5, CB 40.6 ppm	oxidized, CA 50.8, CB 41.6 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr34478_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	176		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: 114
  - ¹³C chemical shifts: 45
  - ¹⁵N chemical shifts: 17
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- 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	107	102	95.3
¹³C chemical shifts	80	45	56.2
¹⁵N chemical shifts	21	17	81.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	39	100.0
¹³C chemical shifts	36	18	50.0
¹⁵N chemical shifts	17	15	88.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	68	63	92.6
¹³C chemical shifts	44	27	61.4
¹⁵N chemical shifts	4	2	50.0

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	17	14	82.4
¹³C chemical shifts	15	0	0.0
¹⁵N chemical shifts	2	2	100.0

Keywords ANTIMICROBIAL PROTEIN, antibacterial, class IV, lasso peptide

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Found 1 Document (0.283 seconds)

BMRB: 34478

Sample

Related entities 1. Felipeptin A1, CYS-LEU-ILE-TRP-CYS-ASP, : 1 entities Detail

Experiments performed 5 experiments Detail

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Chemical shift validation 3 contents Detail