BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	77.1 % (324 of 420)	89.7 % (200 of 223)	59.0 % (92 of 156)	78.0 % (32 of 41)
Backbone	77.9 % (162 of 208)	94.4 % (67 of 71)	63.1 % (65 of 103)	88.2 % (30 of 34)
Sidechain	79.6 % (195 of 245)	87.5 % (133 of 152)	69.8 % (60 of 86)	28.6 % (2 of 7)
Aromatic	47.2 % (17 of 36)	94.4 % (17 of 18)	0.0 % (0 of 15)	0.0 % (0 of 3)
Methyl	100.0 % (24 of 24)	100.0 % (12 of 12)	100.0 % (12 of 12)

1. entity 1

GCLGIWKACN PSNDQCCKSS KLVCSRKTRW CKWQIX

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1		0.0 ~ 0.0 mM
2	D2O	[U-2H]	10 %
3	H2O	natural abundance	90 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 100 % D2O, 100% D2O

#	Name	Isotope labeling	Type	Concentration
4	entity_1			0.0 ~ 0.0 mM
5	D2O	[U-2H]		100 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.768 ppm	internal	direct	0.2514495
¹H	water	protons	4.768 ppm	internal	direct	1.0
¹⁵N	water	protons	4.768 ppm	internal	direct	0.1013291

Referencing offset: 0.21 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.768 ppm	internal	direct	0.2514495
¹H	water	protons	4.768 ppm	internal	direct	1.0
¹⁵N	water	protons	4.768 ppm	internal	direct	0.1013291

Referencing offset: 0.21 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.768 ppm	internal	direct	0.2514495
¹H	water	protons	4.768 ppm	internal	direct	1.0
¹⁵N	water	protons	4.768 ppm	internal	direct	0.1013291

Referencing offset: 0.07 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5TLR, Strand ID: A Detail

Release date

2017-02-12

Citation

Spider peptide toxin HwTx-IV engineered to bind to lipid membranes has an increased inhibitory potency at human voltage-gated sodium channel hNa_V1.7
Agwa, A.J., Lawrence, N., Deplazes, E., Cheneval, O., Chen, R., Craik, D.J., Schroeder, C.I., Henriques, S.T.
Biochim. Biophys. Acta (2017), 1859, 835-844, PubMed 28115115 , DOI 10.1016/j.bbamem.2017.01.020 , Abstract

Related entities 1. Mu-theraphotoxin-Hs2a, : 1 : 91 entities Detail

Experiments performed 11 experiments Detail

1 1D 1H

Instrument

Bruker Avance - 600 MHz Cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1		0.0 ~ 0.0 mM
2	D2O	[U-2H]	10 %
3	H2O	natural abundance	90 %

2 2D 1H-1H TOCSY

Instrument

Bruker Avance - 600 MHz Cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1		0.0 ~ 0.0 mM
2	D2O	[U-2H]	10 %
3	H2O	natural abundance	90 %

3 2D 1H-1H NOESY

Instrument

Bruker Avance - 600 MHz Cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1		0.0 ~ 0.0 mM
2	D2O	[U-2H]	10 %
3	H2O	natural abundance	90 %

4 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz Cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1		0.0 ~ 0.0 mM
2	D2O	[U-2H]	10 %
3	H2O	natural abundance	90 %

5 2D 1H-13C HSQC

Instrument

Bruker Avance - 600 MHz Cryoprobe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1		0.0 ~ 0.0 mM
2	D2O	[U-2H]	10 %
3	H2O	natural abundance	90 %

6 1D 1H

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 283 K, pH 4.0, Details 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1		0.0 ~ 0.0 mM
2	D2O	[U-2H]	10 %
3	H2O	natural abundance	90 %

7 2D 1H-1H TOCSY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 283 K, pH 4.0, Details 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1		0.0 ~ 0.0 mM
2	D2O	[U-2H]	10 %
3	H2O	natural abundance	90 %

8 1D 1H

Instrument

Bruker Avance - 600 MHz Cryoprobe

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 100 % D2O, 100% D2O

#	Name	Isotope labeling	Type	Concentration
4	entity_1			0.0 ~ 0.0 mM
5	D2O	[U-2H]		100 %

9 2D 1H-1H NOESY

Instrument

Bruker Avance - 600 MHz Cryoprobe

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 100 % D2O, 100% D2O

#	Name	Isotope labeling	Type	Concentration
4	entity_1			0.0 ~ 0.0 mM
5	D2O	[U-2H]		100 %

10 2D 1H-1H TOCSY

Instrument

Bruker Avance - 600 MHz Cryoprobe

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 100 % D2O, 100% D2O

#	Name	Isotope labeling	Type	Concentration
4	entity_1			0.0 ~ 0.0 mM
5	D2O	[U-2H]		100 %

11 2D E.COSY

Instrument

Bruker Avance - 600 MHz Cryoprobe

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 4.0, Details 100 % D2O, 100% D2O

#	Name	Isotope labeling	Type	Concentration
4	entity_1			0.0 ~ 0.0 mM
5	D2O	[U-2H]		100 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30190_5tlr.nef
Input source #2: Coordindates	5tlr.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	True (see coodinates for details)
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:17:CYS:SG	oxidized, CA 54.651, CB 44.239 ppm	oxidized, CA 55.648, CB 41.289 ppm	2.03
A:9:CYS:SG	A:24:CYS:SG	oxidized, CB 46.489 ppm	oxidized, CA 55.348, CB 37.958 ppm	2.02
A:16:CYS:SG	A:31:CYS:SG	oxidized, CA 56.454, CB 38.902 ppm	oxidized, CB 39.7 ppm	2.015

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

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:35:ILE:C	1:36:NH2:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	36	NH2	AMINO GROUP	Coordinates

Sequence alignments

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

--------10--------20--------30------
GCLGIWKACNPSNDQCCKSSKLVCSRKTRWCKWQIX
||||||||||||||||||||||||||||||||||||
GCLGIWKACNPSNDQCCKSSKLVCSRKTRWCKWQIX

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	36	0	0	100.0

Content subtype: combined_30190_5tlr.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	4		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	325		94.4 (chain: A, length: 36)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	615 (1)	noe	94.4 (chain: A, length: 36)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	10 (1)	hbond	27.8 (chain: A, length: 36)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	28 (28)	.	47.2 (chain: A, length: 36)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 36, Sequence coverage: 94.4%
- Total number of assignments
  - ¹H chemical shifts: 205
  - ¹³C chemical shifts: 89
  - ¹⁵N chemical shifts: 31
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
18	LYS	HZ1	7.181
18	LYS	HZ2	7.181
18	LYS	HZ3	7.181
29	ARG	HH11	7.268
29	ARG	HH21	7.267

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	225	200	88.9
¹³C chemical shifts	156	89	57.1
¹⁵N chemical shifts	44	31	70.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	71	67	94.4
¹³C chemical shifts	70	29	41.4
¹⁵N chemical shifts	35	29	82.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	154	133	86.4
¹³C chemical shifts	86	60	69.8
¹⁵N chemical shifts	9	2	22.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	12	12	100.0
¹³C chemical shifts	12	12	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	17	94.4
¹³C chemical shifts	15	0	0.0
¹⁵N chemical shifts	3	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: 36, Sequence coverage: 94.4%
- Total number of restraints: 615
- Weight of restraints: 1.0 (615)
- Potential type of restraints: square-well-parabolic (615)
- Range of distance target values: 1.12, 4.0 (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: 36, Sequence coverage: 27.8%
  - Total number of restraints: 10
  - Weight of restraints: 1.0 (10)
  - Potential type of restraints: square-well-parabolic (10)
  - 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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 36, Sequence coverage: 47.2%
- Total number of restraints: 28
- Total number of restraints per polymer type: 28
- Weight of restraints: 1.0 (28)
- Potential type of restraints: square-well-parabolic (28)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue

Keywords TOXIN, disulfide-rich, sodium channel inhibitor, spider toxin

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Found 1 Document (0.535 seconds)

BMRB: 30190

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Mu-theraphotoxin-Hs2a, : 1 : 91 entities Detail

Experiments performed 11 experiments Detail

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NMR combined restraints 5 contents Detail