BMRBj - BMREntryMaster

Found 1 Document (0.675 seconds)

BMRB: 30954

7SAV

Mu-conotoxin KIIIA isomer 2

Authors

Schroeder, C.I., Tran, H.N.T.

Assembly

Mu-conotoxin KIIIA

Entity

1. Mu-conotoxin KIIIA (polymer, Thiol state: all disulfide bound), 16 monomers, 1891.187 Da Detail

CCNCSSKWCR DHSRCC

Formula weight

1891.187 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS1:SG	1:CYS16:SG
2	disulfide	sing	1:CYS2:SG	1:CYS9:SG
3	disulfide	sing	1:CYS4:SG	1:CYS15:SG

Source organism

Conus kinoshitai

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 82.6 %, Completeness (bb): 79.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	82.6 % (142 of 172)	98.9 % (89 of 90)	61.3 % (38 of 62)	75.0 % (15 of 20)
Backbone	79.2 % (76 of 96)	96.9 % (31 of 32)	64.6 % (31 of 48)	87.5 % (14 of 16)
Sidechain	88.0 % (81 of 92)	100.0 % (58 of 58)	73.3 % (22 of 30)	25.0 % (1 of 4)
Aromatic	50.0 % (8 of 16)	100.0 % (8 of 8)	0.0 % (0 of 7)	0.0 % (0 of 1)

1. entity 1

CCNCSSKWCR DHSRCC

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 3, Details 2 mg/mL KIIIA, 90% H2O/10% D2O

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

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 3, Details 2 mg/mL KIIIA, 100% D2O

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

Release date

2021-09-26

Citation

Structural and functional insights into the inhibition of human voltage-gated sodium channels by μ-conotoxin KIIIA disulfide isomers
Tran, H.N.T., McMahon, K.L., Dueis, J.R., Vetter, I., Schroeder, C.I.
J. Biol. Chem. (2022), 298, 101728-101728, PubMed 35167877 , DOI 10.1016/j.jbc.2022.101728 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 30953 released on 2021-09-26
Title Native mu-conotoxin KIIIA isomer

Related entities 1. Mu-conotoxin KIIIA, : 1 : 4 : 14 entities Detail

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30954_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)
1:1:CYS:SG	1:16:CYS:SG	oxidized, CA 54.608, CB 41.66 ppm	oxidized, CA 54.315, CB 41.707 ppm	n/a
1:2:CYS:SG	1:9:CYS:SG	reduced, CA 54.766, CB 27.912 ppm	oxidized, CA 56.107, CB 39.887 ppm	n/a
1:4:CYS:SG	1:15:CYS:SG	oxidized, CA 56.893, CB 39.864 ppm	oxidized, CA 55.037, CB 40.27 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr30954_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	146		100.0 (chain: 1, length: 16)
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: 16, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 92
  - ¹³C chemical shifts: 38
  - ¹⁵N chemical shifts: 16
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Tautomeric state of HIS
- 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)
7	LYS	HZ1	7.563
7	LYS	HZ2	7.563
7	LYS	HZ3	7.563
12	HIS	ND1	115.931

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	89	98.9
¹³C chemical shifts	62	38	61.3
¹⁵N chemical shifts	20	15	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	32	31	96.9
¹³C chemical shifts	32	16	50.0
¹⁵N chemical shifts	16	14	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	58	58	100.0
¹³C chemical shifts	30	22	73.3
¹⁵N chemical shifts	4	1	25.0

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, disulfide-bond isomer

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 (0.675 seconds)

BMRB: 30954

Sample #1

Sample #2

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Mu-conotoxin KIIIA, : 1 : 4 : 14 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail