BMRBj - BMREntryMaster

Found 1 Document (0.454 seconds)

BMRB: 30758

6X8R

Pharmacological characterisation and NMR structure of the novel mu-conotoxin SxIIIC, a potent irreversible NaV channel inhibitor

Authors

Schroeder, C.I., McMahon, K.L.

Assembly

SxIIIC peptide

Entity

1. SxIIIC peptide (polymer, Thiol state: all disulfide bound), 23 monomers, 2441.787 Da Detail

RGCCNGRGGC SSRWCRDHAR CCX

Formula weight

2441.787 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS3:SG	1:CYS15:SG
2	disulfide	sing	1:CYS4:SG	1:CYS21:SG
3	disulfide	sing	1:CYS10:SG	1:CYS22:SG

Source organism

Conus striolatus

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.7 %, Completeness: 81.0 %, Completeness (bb): 78.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	81.0 % (183 of 226)	99.2 % (117 of 118)	63.3 % (50 of 79)	55.2 % (16 of 29)
Backbone	78.0 % (103 of 132)	97.9 % (47 of 48)	64.5 % (40 of 62)	72.7 % (16 of 22)
Sidechain	87.5 % (98 of 112)	100.0 % (70 of 70)	80.0 % (28 of 35)	0.0 % (0 of 7)
Aromatic	50.0 % (8 of 16)	100.0 % (8 of 8)	0.0 % (0 of 7)	0.0 % (0 of 1)
Methyl	100.0 % (2 of 2)	100.0 % (1 of 1)	100.0 % (1 of 1)

1. entity 1

RGCCNGRGGC SSRWCRDHAR CCX

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 null, Temperature 298 K, pH 4, Details 1 mg/mL SxIIIC, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	SxIIIC	natural abundance		1 mg/mL

Sample #2

Solvent system 100% D2O, Pressure 1 null, Temperature 298 K, pH 4, Details 1 mg/mL SxIIIC, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	SxIIIC	natural abundance		1 mg/mL

Protein Blocks Logo

Calculated from 20 models in PDB: 6X8R, Strand ID: A Detail

Release date

2020-06-28

Citation

Discovery, Pharmacological Characterisation and NMR Structure of the Novel µ-Conotoxin SxIIIC, a Potent and Irreversible Na_V Channel Inhibitor
McMahon, K.L., Tran, H.N.T., Deuis, J.R., Lewis, R.J., Vetter, I., Schroeder, C.I.
Biomedicines (2020), 8, E391-E391, PubMed 33023152 , DOI 10.3390/biomedicines8100391 , Abstract

Related entities 1. SxIIIC peptide, : 1 : 16 entities Detail

Experiments performed 6 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30758_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)
1:3:CYS:SG	1:15:CYS:SG	oxidized, CA 55.076, CB 39.414 ppm	oxidized, CA 57.515, CB 36.845 ppm	n/a
1:4:CYS:SG	1:21:CYS:SG	oxidized, CA 54.521, CB 40.538 ppm	oxidized, CA 56.715, CB 43.003 ppm	n/a
1:10:CYS:SG	1:22:CYS:SG	oxidized, CA 55.142, CB 39.462 ppm	oxidized, CA 53.556, CB 38.432 ppm	n/a

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

None

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
1	23	NH2	AMINO GROUP	Assigned chemical shifts

Content subtype: bmr30758_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	188		100.0 (chain: 1, length: 23)
1	Chemical shift references	chem_shift_reference_1	OK	1		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 23, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 122
  - ¹³C chemical shifts: 50
  - ¹⁵N chemical shifts: 16
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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)
18	HIS	HD1	9.998

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	120	119	99.2
¹³C chemical shifts	79	50	63.3
¹⁵N chemical shifts	30	16	53.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	47	97.9
¹³C chemical shifts	44	22	50.0
¹⁵N chemical shifts	23	16	69.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	72	72	100.0
¹³C chemical shifts	35	28	80.0
¹⁵N chemical shifts	7	0	0.0

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	8	100.0
¹³C chemical shifts	7	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords TOXIN, sodium channels

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.454 seconds)

BMRB: 30758

Sample #1

Sample #2

Related entities 1. SxIIIC peptide, : 1 : 16 entities Detail

Experiments performed 6 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail