BMRBj - BMREntryMaster

	Total	¹H	¹³C
All	76.8 % (252 of 328)	97.9 % (186 of 190)	47.8 % (66 of 138)
Backbone	76.2 % (131 of 172)	98.6 % (72 of 73)	59.6 % (59 of 99)
Sidechain	79.5 % (147 of 185)	97.4 % (114 of 117)	48.5 % (33 of 68)
Aromatic	40.0 % (4 of 10)	80.0 % (4 of 5)	0.0 % (0 of 5)
Methyl	47.1 % (16 of 34)	88.2 % (15 of 17)	5.9 % (1 of 17)

1. Ep-AMP1

CVLIGQRCDN DRGPRCCSGQ GNCVPLPFLG GVCAV

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 3.0

#	Name	Isotope labeling	Concentration
1	Ep-AMP1	natural abundance	6 mg/mL
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 3.0

#	Name	Isotope labeling	Type	Concentration
4	Ep-AMP1	natural abundance		4 mg/mL
5	D2O	natural abundance		100 %

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Calculated from 20 models in PDB: 2MFS, Strand ID: A Detail

Release date

2014-11-09

Citation

A cactus-derived toxin-like cystine knot Peptide with selective antimicrobial activity
Aboye, T.L., Stromstedt, A.A., Bruhn, J.G., El-Seedi, H., Gunasekera, S., Rosengren, K., Goransson, U.
Chembiochem. (2015), 16, 1068-1077, PubMed 25821084 , DOI 10.1002/cbic.201402704 , Abstract

Related entities 1. cactus-derived antimicrobial peptide Ep-AMP1, : 1 : 9 entities Detail

Experiments performed 7 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19570_2mfs.nef
Input source #2: Coordindates	2mfs.cif
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)
A:1:CYS:SG	A:17:CYS:SG	oxidized, CB 40.802 ppm	oxidized, CA 53.495, CB 39.486 ppm	2.034
A:8:CYS:SG	A:23:CYS:SG	oxidized, CA 52.945, CB 48.577 ppm	oxidized, CA 51.888, CB 38.365 ppm	2.025
A:16:CYS:SG	A:33:CYS:SG	oxidized, CA 55.69, CB 39.457 ppm	oxidized, CA 56.391, CB 39.298 ppm	2.012

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

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30-----
CVLIGQRCDNDRGPRCCSGQGNCVPLPFLGGVCAV
|||||||||||||||||||||||||||||||||||
CVLIGQRCDNDRGPRCCSGQGNCVPLPFLGGVCAV

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	35	0	0	100.0

Content subtype: combined_19570_2mfs.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	3		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	248		100.0 (chain: A, length: 35)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	456 (1)	noe	100.0 (chain: A, length: 35)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	30 (1)	hbond	57.1 (chain: A, length: 35)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	68 (68)	.	100.0 (chain: A, length: 35)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 186
  - ¹³C chemical shifts: 62
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	190	186	97.9
¹³C chemical shifts	138	62	44.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	73	72	98.6
¹³C chemical shifts	70	31	44.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	117	114	97.4
¹³C chemical shifts	68	31	45.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	15	88.2
¹³C chemical shifts	17	1	5.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	4	80.0
¹³C chemical shifts	5	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 100.0%
- Total number of restraints: 456
- Weight of restraints: 1.0 (456)
- Potential type of restraints: square-well-parabolic (456)
- Range of distance target values: 2.1, 5.77 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 57.1%
  - Total number of restraints: 30
  - Weight of restraints: 1.0 (30)
  - Potential type of restraints: square-well-parabolic (30)
  - Range of distance target values: 2.05, 2.55 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 100.0%
- Total number of restraints: 68
- Total number of restraints per polymer type: 68
- Weight of restraints: 1.0 (68)
- Potential type of restraints: square-well-parabolic (68)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords cystine-knot, peptide, solution NMR

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Found 1 Document (0.547 seconds)

BMRB: 19570

Sample #1

Sample #2

Related entities 1. cactus-derived antimicrobial peptide Ep-AMP1, : 1 : 9 entities Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 5 contents Detail