BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	79.8 % (317 of 397)	93.9 % (199 of 212)	60.0 % (90 of 150)	80.0 % (28 of 35)
Backbone	82.8 % (149 of 180)	98.4 % (60 of 61)	68.5 % (61 of 89)	93.3 % (28 of 30)
Sidechain	80.1 % (197 of 246)	92.1 % (139 of 151)	64.4 % (58 of 90)	0.0 % (0 of 5)
Aromatic	50.0 % (28 of 56)	100.0 % (28 of 28)	0.0 % (0 of 24)	0.0 % (0 of 4)
Methyl	85.7 % (12 of 14)	85.7 % (6 of 7)	85.7 % (6 of 7)

1. entity 1

YCQKWMWTCD SERKCCKGMV CRLWCKKKLW

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 Pa, Temperature 298 K, pH 3.5 (±0.5), Details 2 mg/mL [E17K]ProTx-II, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	[E17K]ProTx-II	natural abundance		2 mg/mL

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Calculated from 20 models in PDB: 6MK4, Strand ID: A Detail

Release date

2018-09-25

Citation

Peptide-membrane interactions affect the inhibitory potency and selectivity of spider toxins ProTx-II and GpTx-1
Lawrence, N., Wu, B., Ligutti, J., Cheneval, O., Agwa, A.J., Benfield, A.H., Biswas, K., Craik, D.J., Miranda, L.P., Henriques, S.T., Schroeder, C.I.
ACS Chem. Biol. (2018), 14, 118-130, PubMed 30507158 , DOI 10.1021/acschembio.8b00989 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 30522 released on 2018-09-25
Title Solution NMR structure of spider toxin analogue [F5A,M6F,T26L,K28R]GpTx-1

Related entities 1. Beta/omega-theraphotoxin-Tp2a, : 1 : 6 : 26 entities Detail

Experiments performed 6 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30521_6mk4.nef
Input source #2: Coordindates	6mk4.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:2:CYS:SG	A:16:CYS:SG	oxidized, CA 53.896, CB 43.3 ppm	oxidized, CA 54.218, CB 40.03 ppm	2.031
A:9:CYS:SG	A:21:CYS:SG	oxidized, CA 53.819, CB 48.347 ppm	oxidized, CA 55.357, CB 39.988 ppm	2.023
A:15:CYS:SG	A:25:CYS:SG	oxidized, CA 55.903, CB 40.719 ppm	oxidized, CA 56.594, CB 40.165 ppm	2.029

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
YCQKWMWTCDSERKCCKGMVCRLWCKKKLW
||||||||||||||||||||||||||||||
YCQKWMWTCDSERKCCKGMVCRLWCKKKLW

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	30	0	0	100.0

Content subtype: combined_30521_6mk4.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_chemical_shifts_1	Warning	321		100.0 (chain: A, length: 30)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	470 (1)	noe	100.0 (chain: A, length: 30)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	10 (1)	hbond	26.7 (chain: A, length: 30)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	38 (38)	.	93.3 (chain: A, length: 30)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 207
  - ¹³C chemical shifts: 86
  - ¹⁵N chemical shifts: 28
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
17	LYS	HZ1	7.541
17	LYS	HZ2	7.541
17	LYS	HZ3	7.541
26	LYS	HZ1	7.622
26	LYS	HZ2	7.622
26	LYS	HZ3	7.622
27	LYS	HZ1	7.072
27	LYS	HZ2	7.072
27	LYS	HZ3	7.072
28	LYS	HZ1	7.435
28	LYS	HZ2	7.435
28	LYS	HZ3	7.435

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	212	195	92.0
¹³C chemical shifts	150	86	57.3
¹⁵N chemical shifts	37	28	75.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	61	60	98.4
¹³C chemical shifts	60	30	50.0
¹⁵N chemical shifts	30	28	93.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	151	135	89.4
¹³C chemical shifts	90	56	62.2
¹⁵N chemical shifts	7	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	6	66.7
¹³C chemical shifts	9	6	66.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	28	28	100.0
¹³C chemical shifts	24	0	0.0
¹⁵N chemical shifts	4	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 100.0%
- Total number of restraints: 470
- Weight of restraints: 1.0 (470)
- Potential type of restraints: square-well-parabolic (470)
- Range of distance target values: 1.38, 2.75 (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_4
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 26.7%
  - Total number of restraints: 10
  - Weight of restraints: 1.0 (10)
  - Potential type of restraints: square-well-parabolic (10)
  - Range of distance target values: 1.15, 1.65 (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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 93.3%
- Total number of restraints: 38
- Total number of restraints per polymer type: 38
- Weight of restraints: 1.0 (38)
- Potential type of restraints: square-well-parabolic (38)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords ProTx-II analogue, TOXIN, peptide-membrane interactions, spider toxin, voltage-sensitive sodium channels

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Found 1 Document (0.576 seconds)

BMRB: 30521

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Beta/omega-theraphotoxin-Tp2a, : 1 : 6 : 26 entities Detail

Experiments performed 6 experiments Detail

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NMR combined restraints 5 contents Detail